|
Name |
Accession |
Description |
Interval |
E-value |
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-350 |
0e+00 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 549.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS-VGARERQVGFV 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVKPrrerPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRP----PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGA 239
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 240 ANRLDGTVSGNGFVAHGAAQAIAVDADfAGPARAYVRPHDLELAAPHARAQGIAADVRRVVPLGGSVRVELAA--RSGEV 317
Cdd:COG1118 237 VNVLRGRVIGGQLEADGLTLPVAEPLP-DGPAVAGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLedGEGQP 315
|
330 340 350
....*....|....*....|....*....|...
gi 490296977 318 LEAELDRNAWRALALDVGDALTAVPRAVRVFPA 350
Cdd:COG1118 316 LEAEVTKEAWAELGLAPGDPVYLRPRPARVFLP 348
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-239 |
8.25e-167 |
|
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: 464.51 E-value: 8.25e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVF 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGA 239
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-350 |
7.62e-159 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 448.78 E-value: 7.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMR----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANR 242
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 243 LDGTVS---GNGFVAHGAAQAIAVDADFA--GPARAYVRPHDLELAAPHARAqGIAADVRRVVPLGGSVRVELAARSGEV 317
Cdd:COG3842 242 LPGTVLgdeGGGVRTGGRTLEVPADAGLAagGPVTVAIRPEDIRLSPEGPEN-GLPGTVEDVVFLGSHVRYRVRLGDGQE 320
|
330 340 350
....*....|....*....|....*....|....*
gi 490296977 318 LEAELDRNAWRALAldVGDALTAV--PRAVRVFPA 350
Cdd:COG3842 321 LVVRVPNRAALPLE--PGDRVGLSwdPEDVVVLPA 353
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-282 |
5.74e-150 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 426.42 E-value: 5.74e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVF 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAA 240
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490296977 241 NRLDGTVSGNGFVAHGAAQAIAVDADFAGPARAYVRPHDLEL 282
Cdd:PRK10851 241 NRLQGTIRGGQFHVGAHRWPLGYTPAYQGPVDLFLRPWEVDI 282
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-243 |
2.01e-134 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 382.61 E-value: 2.01e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIR----KHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANR 242
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
.
gi 490296977 243 L 243
Cdd:TIGR00968 237 L 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-348 |
3.72e-134 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 385.97 E-value: 3.72e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLR----KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLG--AA 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGspPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 241 NRLDGTVSGNGFVAHGAAQAI--AVDADFAGPARAYVRPHDLELAAPHarAQGIAADVRRVVPLGGSVRVELAArSGEVL 318
Cdd:COG3839 240 NLLPGTVEGGGVRLGGVRLPLpaALAAAAGGEVTLGIRPEHLRLADEG--DGGLEATVEVVEPLGSETLVHVRL-GGQEL 316
|
330 340 350
....*....|....*....|....*....|..
gi 490296977 319 EAELDRNAwralALDVGDA--LTAVPRAVRVF 348
Cdd:COG3839 317 VARVPGDT----RLRPGDTvrLAFDPERLHLF 344
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-349 |
5.59e-122 |
|
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: 355.11 E-value: 5.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLrvKPRRErpSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGL--KNRGM--GRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANR 242
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 243 LDGTVSGNGFVAHGAAQaIAVDADFAGPA---RAYVRPHDLELAAPHARAQGIAADVRRVVPLGGSVRVELAARS--GEV 317
Cdd:TIGR03265 241 LPGTRGGGSRARVGGLT-LACAPGLAQPGasvRLAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGlpGQA 319
|
330 340 350
....*....|....*....|....*....|....
gi 490296977 318 LEAELDRNAWRALALDVGDAL-TAVPRA-VRVFP 349
Cdd:TIGR03265 320 LVADVSASEVERLGIRAGQPIwIELPAErLRAFA 353
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-238 |
5.26e-121 |
|
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: 348.07 E-value: 5.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLK----KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLG 238
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-247 |
7.46e-112 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 330.37 E-value: 7.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKPRrerpSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKT----PAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANR 242
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINI 250
|
....*
gi 490296977 243 LDGTV 247
Cdd:PRK09452 251 FDATV 255
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-219 |
1.55e-109 |
|
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: 318.31 E-value: 1.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLR----GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-219 |
8.67e-97 |
|
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: 286.07 E-value: 8.67e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKPRRERpseaAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKD----EIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-239 |
3.02e-96 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 288.14 E-value: 3.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFV 79
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAfglrVKPRRERPSEAAIRAKVHELLSLVQLD--WLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:COG1125 82 IQQIGLFPHMTVAENIA----TVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFL 237
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
..
gi 490296977 238 GA 239
Cdd:COG1125 238 GA 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-347 |
8.49e-96 |
|
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: 287.47 E-value: 8.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 33 LLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYALFRHMTVFENVAFGLRVK--PRRErpse 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRkvPRAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 111 aaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHIST 190
Cdd:TIGR01187 77 --IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 191 IFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANRLDGTV---SGNGFVAHGAAQAIA-VDAD 266
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVierKSEQVVLAGVEGRRCdIYTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 267 FAGPARA----YVRPHDLEL--AAPHARAQGIAADVRRVVPLGGSVRVELAARSGE-VLEAELDRNAWRALALDVGD--A 337
Cdd:TIGR01187 235 VPVEKDQplhvVLRPEKIVIeeEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQkVLVSEFFNEDDPHMSPSIGDrvG 314
|
330
....*....|
gi 490296977 338 LTAVPRAVRV 347
Cdd:TIGR01187 315 LTWHPGSEVV 324
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
2.24e-95 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 283.90 E-value: 2.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARerqV 76
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRgvPKAER------RERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNH--GRV 215
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-215 |
4.09e-90 |
|
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: 269.34 E-value: 4.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvASVGARERQVGF 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQ----GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLN--HGRV 215
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-237 |
6.36e-90 |
|
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: 269.54 E-value: 6.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQVG 77
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHMTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLR---EHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 158 LLLDEPFGALD---AKVRKELrgwLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY--DHPrsaF 232
Cdd:COG1127 163 LLYDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDP---W 236
|
....*
gi 490296977 233 VYEFL 237
Cdd:COG1127 237 VRQFL 241
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-335 |
6.63e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 270.79 E-value: 6.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAaLDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLR----KVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANR 242
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 243 LDGTV--SGNGFVAHGAAQAIAVDADFAGPARAYVRPHDLELA----APHARAQgIAADVRRVVPLGGSVRVELAArsGE 316
Cdd:NF040840 237 IEGVAekGGEGTILDTGNIKIELPEEKKGKVRIGIRPEDITIStekvKTSARNE-FKGKVEEIEDLGPLVKLTLDV--GI 313
|
330
....*....|....*....
gi 490296977 317 VLEAELDRNAWRALALDVG 335
Cdd:NF040840 314 ILVAFITRSSFLDLEINEG 332
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-303 |
6.97e-89 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 270.82 E-value: 6.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYAL 85
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 86 FRHMTVFENVAFGLRVKPRrerpSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLGV----PKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 166 ALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANRLDG 245
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 246 TVSGNGFVAHGAAQAIAVDADFAGPARAY---VRPHDLELAAPHARAQgiAADVRRVVPLG 303
Cdd:PRK11432 246 TLSGDYVDIYGYRLPRPAAFAFNLPDGECtvgVRPEAITLSEQGEESQ--RCTIKHVAYMG 304
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-327 |
2.70e-88 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 269.41 E-value: 2.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVF 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIR----GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLG-- 238
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGsp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 239 AANRLDGTVSGNGfVAHGAAQAIAVDADFAGPARAY------VRPHDLELAAPharAQGIAADVRRVVPLGG-------- 304
Cdd:PRK11650 239 AMNLLDGRVSADG-AAFELAGGIALPLGGGYRQYAGrkltlgIRPEHIALSSA---EGGVPLTVDTVELLGAdnlahgrw 314
|
330 340 350
....*....|....*....|....*....|
gi 490296977 305 -----SVRV--ELAARSGEVLEAELDRNAW 327
Cdd:PRK11650 315 ggqplVVRLphQERPAAGSTLWLHLPANQL 344
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-239 |
1.04e-86 |
|
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: 261.47 E-value: 1.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFV 79
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAfglrVKPRRERPSEAAIRAKVHELLSLVQLD--WLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIA----LVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFL 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
..
gi 490296977 238 GA 239
Cdd:cd03295 237 GA 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-328 |
3.44e-86 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 264.78 E-value: 3.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYA 84
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 85 LFRHMTVFENVAFGLrvkpRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK11607 102 LFPHMTVEQNIAFGL----KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 165 GALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAANRLD 244
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 245 GTV---SGNGFV--AHGAAQAIAVDADFA----GPARAYVRPHDLELA-APHARAQGIA-ADVRRVVPLGGSVRVELAAR 313
Cdd:PRK11607 258 GVLkerQEDGLVidSPGLVHPLKVDADASvvdnVPVHVALRPEKIMLCeEPPADGCNFAvGEVIHIAYLGDLSIYHVRLK 337
|
330
....*....|....*
gi 490296977 314 SGEVLEAELdRNAWR 328
Cdd:PRK11607 338 SGQMISAQL-QNAHR 351
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-241 |
9.17e-84 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 253.80 E-value: 9.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAaLDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKpRRERPSeaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKR-KVDKKE---IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAAN 241
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-238 |
8.88e-81 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 246.06 E-value: 8.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV----ASVGARERQVGF 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLrVKPRRERPSEAaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAP-IKVKKMSKAEA--EERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLG 238
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
1.08e-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: 1.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE---- 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 -RQVGFVFQH--YALFRHMTVFENVAFGLRVkprRERPSEAAIRAKVHELLSLVQLD-WLAQRYPSELSGGQRQRIALAR 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRL---HGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
..
gi 490296977 230 SA 231
Cdd:COG1123 498 HP 499
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-229 |
3.31e-80 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 244.72 E-value: 3.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQVG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHMTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLR---EHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY--DHPR 229
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
2.22e-78 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 239.56 E-value: 2.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER---- 74
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 --QVGFVFQHYALFRHMTVFENVAFGLRV--KPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARA 150
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLagVSRKER------RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDqEEALEVADRIVVLNHGRVE 216
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
3.14e-78 |
|
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: 238.93 E-value: 3.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER---- 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 --QVGFVFQHYALFRHMTVFENVAFGLRV--KPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARA 150
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLagVPKKER------RERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEAlEVADRIVVLNHGRV 215
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-219 |
2.81e-77 |
|
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: 236.42 E-value: 2.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 9 HKRFGEFAAldDVSLDFPaGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL---------QGLDVASvgaRERQVGFV 79
Cdd:cd03297 7 EKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrKKINLPP---QQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVKPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRKRNRED------RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-229 |
2.82e-77 |
|
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: 236.85 E-value: 2.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFV 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQH--YALFrHMTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFG----PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-239 |
3.37e-77 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 241.47 E-value: 3.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQ 81
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLA----GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGA 239
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-345 |
2.21e-76 |
|
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: 238.85 E-value: 2.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRnLHKRFGEFAaLDdVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG---LDVAS---VGARER 74
Cdd:COG4148 1 MMLEVD-FRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 QVGFVFQHYALFRHMTVFENVAFGLRVKPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAER------RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVY 234
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 235 EFLGAANRLDGTVsgngfVAHGAAQAIAVdADFAG--------------PARAYVRPHD--LELAAPH---ARAQgIAAD 295
Cdd:COG4148 232 GGEEAGSVLEATV-----AAHDPDYGLTR-LALGGgrlwvprldlppgtRVRVRIRARDvsLALEPPEgssILNI-LPGR 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 296 VRRVVPL-GGSVRVELAArSGEVLEAELDRNAWRALALDVGDALTAVPRAV 345
Cdd:COG4148 305 VVEIEPAdGGQVLVRLDL-GGQTLLARITRRSADELGLAPGQTVYAQIKSV 354
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-271 |
7.57e-75 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 234.59 E-value: 7.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE----- 73
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRHMTVFENVAFGLRV--KPRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARAL 151
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIagVPKAE------IRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 152 AVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSpqaVYD---HP 228
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP---VLDvfaNP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490296977 229 RSAFVYEFLGAANRLDGTVSGNGFVAHGAAQAIAVDADFAGPA 271
Cdd:COG1135 233 QSELTRRFLPTVLNDELPEELLARLREAAGGGRLVRLTFVGES 275
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-214 |
2.55e-74 |
|
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: 227.46 E-value: 2.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS----VGARERQVGF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGlrvkprrerpseaairakvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-236 |
3.30e-74 |
|
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: 230.61 E-value: 3.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE------RQ 75
Cdd:cd03294 24 GKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAV 153
Cdd:cd03294 104 ISMVFQSFALLPHRTVLENVAFGLEVQgvPRAER------EERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFV 233
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYV 257
|
...
gi 490296977 234 YEF 236
Cdd:cd03294 258 REF 260
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-224 |
7.11e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 225.71 E-value: 7.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ-VGFVFQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAF--GLRVKPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLYGLPRKEA------RERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHisTIFV-THDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGK--TVLLsTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
2.35e-70 |
|
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: 218.55 E-value: 2.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR----ERQVGF 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLrVKPRRERPSEAaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAP-IKVKGMSKAEA--EERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-237 |
4.69e-69 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 216.11 E-value: 4.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQV----GF 78
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGlrvkPRRER-PSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFG----PLRVRgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFL 237
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-239 |
9.50e-69 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 215.00 E-value: 9.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAAldDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRvkPRReRPSEAAiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLR--PGL-KLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGA 239
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-229 |
1.67e-68 |
|
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: 214.37 E-value: 1.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE----- 73
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRHMTVFENVAFGLRVkprrERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAV 153
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEI----AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-229 |
1.69e-68 |
|
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: 215.29 E-value: 1.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER-QVGFV--FQ 81
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIArtFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVKPR-----------RERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARA 150
Cdd:COG0411 87 NPRLFPELTVLENVLVAAHARLGrgllaallrlpRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-214 |
1.85e-68 |
|
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: 213.48 E-value: 1.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVF 80
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QH--YALFRHmTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:cd03225 82 QNpdDQFFGP-TVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-217 |
4.64e-68 |
|
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: 213.14 E-value: 4.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGA-----RE 73
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHY--ALFRHMTVFENVAFGLRVkpRRERPSEAAIRAKVHELLSLVQLD-WLAQRYPSELSGGQRQRIALARA 150
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRI--HGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGR-VEQ 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
5.38e-68 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 213.75 E-value: 5.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVF 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRvkPRR---ERPSEAAiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRY--PHLglfGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
10-238 |
6.94e-67 |
|
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: 214.72 E-value: 6.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 10 KRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV------GARERQVGFVFQHY 83
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQspvelrEVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 84 ALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLgwPEQER------KEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLG 238
Cdd:TIGR01186 155 EAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-228 |
1.19e-66 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 211.16 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG-----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE---- 73
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 -RQVGFVFQH--YALFRhMTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDW-LAQRYPSELSGGQRQRIALAR 149
Cdd:TIGR04521 81 rKKVGLVFQFpeHQLFE-ETVYKDIAFG----PKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-240 |
2.35e-66 |
|
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: 209.66 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE----FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQV 76
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHY--ALFRHMTVFENVAFGLRVKPRRERpseaaiRAKVHELLSLVQLDW-LAQRYPSELSGGQRQRIALARALAV 153
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDR------EERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFV 233
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....*..
gi 490296977 234 YEFLGAA 240
Cdd:COG1124 236 RELLAAS 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-229 |
4.03e-66 |
|
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: 208.45 E-value: 4.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFVFQ 81
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVKPR------RERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGsglllaRARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-215 |
3.77e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 205.67 E-value: 3.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQV 76
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFGLRV--KPRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVtgKSRKE------IRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-224 |
7.49e-65 |
|
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: 205.11 E-value: 7.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHA-----DSGQVVLQGLDVASVG----ARE 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRhMTVFENVAFGLRVkpRRERPSEaAIRAKVHELLSLVQL-DWLAQR-YPSELSGGQRQRIALARAL 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRL--HGIKLKE-ELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 152 AVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlhISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-226 |
1.16e-64 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 205.09 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR-ERQVGFVFQ 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVKPRRERpseaAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDE----ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDLHIsTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-294 |
3.37e-64 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 204.33 E-value: 3.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFA----ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGArERQV 76
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 gfVFQHYALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRgvPKAER------RARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLnhgrveqvgSPqavydHP-RSAFV 233
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM---------SP-----GPgRIVER 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 234 YEfLGAANRldgtvsgngFVAHGAAQAIAVDADFAGpARAYVrphdleLAAPHARAQGIAA 294
Cdd:COG4525 219 LE-LDFSRR---------FLAGEDARAIKSDPAFIA-LREEL------LDIIFAQEEAEAA 262
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
9.20e-64 |
|
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: 200.32 E-value: 9.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ-VGFVFQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVafglrvkprrerpseaairakvhellslvqldwlaqrypsELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd03230 81 EPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-244 |
1.83e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 202.72 E-value: 1.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE----- 73
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRHMTVFENVAFGLRVkprrERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAV 153
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLEL----AGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFV 233
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
250
....*....|.
gi 490296977 234 YEFLGAANRLD 244
Cdd:PRK11153 238 REFIQSTLHLD 248
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-232 |
1.37e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 197.20 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQV 76
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFG-----------LRVKPRRERpseaairAKVHELLSLVQLDWLAQRYPSELSGGQRQRI 145
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDR-------ERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVeqvgspqaVY 225
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VF 227
|
....*..
gi 490296977 226 DHPRSAF 232
Cdd:COG3638 228 DGPPAEL 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-228 |
3.05e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 193.77 E-value: 3.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARerqVGFVFQH 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---IGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRH--MTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQvGSPQAVYDHP 228
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-276 |
6.23e-60 |
|
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: 200.90 E-value: 6.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF--GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD---SGQVVLQGLDV--ASVGARERQ 75
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLleLSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHY-ALFRHMTVFENVAFGLRVKprreRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:COG1123 85 IGMVFQDPmTQLNPVTVGDQIAEALENL----GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSafvy 234
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA---- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490296977 235 efLGAANRLDGTVSGNGFVAHGAAQAIAVD---ADFAGPARAYVR 276
Cdd:COG1123 237 --LAAVPRLGAARGRAAPAAAAAEPLLEVRnlsKRYPVRGKGGVR 279
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-345 |
4.65e-59 |
|
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: 194.18 E-value: 4.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 7 NLHKRFGEFAAldDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR------ERQVGFVF 80
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRvkprRERPSEAAIR-AKVHELLSLvqlDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMK----RARPSERRISfERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVyEFLGA 239
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL-AREDQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 240 ANRLDGTVSG----NGF----VAHGAAQAIAVDADFAGPARAYVRPHDLELAAPHARAQGIAADVR-RVVPL----GGSV 306
Cdd:TIGR02142 234 GSLIEGVVAEhdqhYGLtalrLGGGHLWVPENLGPTGARLRLRVPARDVSLALQKPEATSIRNILPaRVVEIedsdIGRV 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 490296977 307 RVELAArSGEVLEAELDRNAWRALALDVGDALTAVPRAV 345
Cdd:TIGR02142 314 GVVLES-GGKTLWARITRWARDELGIAPGTPVFAQIKAV 351
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-227 |
6.75e-59 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 190.09 E-value: 6.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQV 76
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFG-------LRVKPRRERPSEaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALAR 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRSLFGLFPKEE---KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
1.39e-58 |
|
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: 191.81 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHA---DSGQVVLQGLDVASVGARE-- 73
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 ----RQVGFVFQH-Y-ALFRHMTVFENVAFGLRVkprRERPSEAAIRAKVHELLSLVQLDW---LAQRYPSELSGGQRQR 144
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRI---HGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 145 IALARALAVEPKVLLLDEPFGALDAKVRK---ELrgwLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGR-VEQvGS 220
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAqilNL---LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRiVEE-GP 234
|
....*....
gi 490296977 221 PQAVYDHPR 229
Cdd:COG0444 235 VEELFENPR 243
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
4.02e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 184.63 E-value: 4.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVF 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFrHMTVFENVAFGLRVkpRRERPSEAAIRAKVHEL-LSLVQLDWLAQRypseLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG4619 81 QEPALW-GGTVRDNLPFPFQL--RERKFDRERALELLERLgLPPDILDKPVER----LSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-229 |
1.03e-56 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 184.21 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGArERQVgfVFQHYALFRHMTVFENVAF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GL-RVKPRRERPSEAAIrakVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELR 176
Cdd:TIGR01184 78 AVdRVLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 177 GWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV-YDHPR 229
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-229 |
3.99e-56 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 185.71 E-value: 3.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFA-------ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGA 71
Cdd:COG4608 8 LEVRDLKKHFpvrgGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 72 RE-----RQVGFVFQH-YA-LFRHMTVFENVAFGLRV---KPRRERpseaaiRAKVHELLSLVQLD-WLAQRYPSELSGG 140
Cdd:COG4608 88 RElrplrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIhglASKAER------RERVAELLELVGLRpEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 141 QRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDqeeaLEV----ADRIVVLNHGRVE 216
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIV 237
|
250
....*....|...
gi 490296977 217 QVGSPQAVYDHPR 229
Cdd:COG4608 238 EIAPRDELYARPL 250
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-237 |
4.81e-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: 4.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--------ER 74
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 QV-------GFVFQHYALFRHMTVFENVAFG-LRV--KPRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQR 144
Cdd:COG4598 89 QLqrirtrlGMVFQSFNLWSHMTVLENVIEApVHVlgRPKAE------AIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 145 IALARALAVEPKVLLLDEPFGALDAkvrkELRGWLRRLHDDL---HISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSP 221
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
250
....*....|....*.
gi 490296977 222 QAVYDHPRSAFVYEFL 237
Cdd:COG4598 239 AEVFGNPKSERLRQFL 254
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
2.04e-55 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 181.36 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL--------QGLDVASVGAR 72
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQVGFVFQHYALFRHMTVFENVAfglrvkprrERP------SEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIA 146
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLI---------EAPckvlglSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLhDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSpQAVYD 226
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFT 229
|
250
....*....|.
gi 490296977 227 HPRSAFVYEFL 237
Cdd:COG4161 230 QPQTEAFAHYL 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-225 |
2.28e-54 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 179.86 E-value: 2.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGE---FA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--- 72
Cdd:PRK13637 1 MSIKIENLTHIYMEgtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 -ERQVGFVFQH--YALFRHmTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDW--LAQRYPSELSGGQRQRIAL 147
Cdd:PRK13637 81 iRKKVGLVFQYpeYQLFEE-TIEKDIAFG----PINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-244 |
2.81e-54 |
|
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: 186.04 E-value: 2.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-----------GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAdSGQVVLQGLDVASVGA 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 72 RE-----RQVGFVFQH-YALF--RhMTVFENVAFGLRVKprRERPSEAAIRAKVHELLSLVQLD-WLAQRYPSELSGGQR 142
Cdd:COG4172 355 RAlrplrRRMQVVFQDpFGSLspR-MTVGQIIAEGLRVH--GPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDqeeaLEV----ADRIVVLNHGR-VEQ 217
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD----LAVvralAHRVMVMKDGKvVEQ 507
|
250 260
....*....|....*....|....*..
gi 490296977 218 vGSPQAVYDHPRSAFVYEFLGAANRLD 244
Cdd:COG4172 508 -GPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-210 |
4.71e-54 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 176.52 E-value: 4.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD---SGQVVLQGLDVASVGARERQVGF 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLRVK-PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTiGRAQR------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEvADRIVVL 210
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDL 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-223 |
1.65e-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: 176.09 E-value: 1.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG------AR 72
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQVGFVFQHYALFRHMTVFENVAFGLRVKPRRerpsEAAIRAKvhELLSLVQLDWLAQRYPSELSGGQRQRIALARALA 152
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGRR----DARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 153 VEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQA 223
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-229 |
4.50e-53 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 175.61 E-value: 4.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRV-------IAGLEHadSGQVVLQGLDVAS-----VG 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EGEILLDGEDIYDpdvdvVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 71 AReRQVGFVFQHYALFRhMTVFENVAFGLR---VKPRRErpseaaIRAKVHELLSLVQL-----DWLaQRYPSELSGGQR 142
Cdd:COG1117 90 LR-RRVGMVFQKPNPFP-KSIYDNVAYGLRlhgIKSKSE------LDEIVEESLRKAALwdevkDRL-KKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 143 QRIALARALAVEPKVLLLDEPFGALD----AKVrKELrgwLRRLHDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQV 218
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDpistAKI-EEL---ILELKKDYTI--VIVTHNMQQAARVSDYTAFFYLGELVEF 234
|
250
....*....|.
gi 490296977 219 GSPQAVYDHPR 229
Cdd:COG1117 235 GPTEQIFTNPK 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-215 |
1.73e-52 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 174.12 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGArERqvGFVFQH 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ER--GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAgvEKMQR------LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVL--NHGRV 215
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRV 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
1.82e-52 |
|
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: 171.46 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 hyalfrhmtvfenvafglrvkprrerpseaairakvheLLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-217 |
1.93e-52 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 173.66 E-value: 1.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL--------QGLDVASVGAR 72
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQVGFVFQHYALFRHMTVFENVAfglrvkprrERP------SEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIA 146
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLI---------EAPcrvlglSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDQEEALEVADRIVVLNHGR-VEQ 217
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHiVEQ 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-227 |
2.33e-52 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 173.25 E-value: 2.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQV 76
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFG-LRVKPR-----RERPSEAAIRAKvhELLSLVQLDWLAQRYPSELSGGQRQRIALARA 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrLGYKPTwrsllGRFSEEDKERAL--SALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-164 |
1.04e-51 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 168.60 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHMTVFENV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 96 AFGLRVKprreRPSEAAIRAKVHELLSLVQL-DWLAQR---YPSELSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:pfam00005 81 RLGLLLK----GLSKREKDARAEEALEKLGLgDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-224 |
1.53e-51 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 181.96 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFrHMTVFENVAFGlrvkpRRERPSEAAIRAkvhelLSLVQLDWLAQRYP-----------SELSGGQRQRIAL 147
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG-----DPDATDEEIIEA-----ARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlhISTIFVTHDqEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-213 |
2.73e-51 |
|
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: 169.64 E-value: 2.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARerqVGFVFQHYA 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 85 LFRHM--TVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03235 79 IDRDFpiSVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHG 213
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-215 |
5.25e-51 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 168.83 E-value: 5.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 20 DVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYALFRHMTVFENVAFGL 99
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 100 rvKPR-RERPSEaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGW 178
Cdd:cd03298 96 --SPGlKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 490296977 179 LRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-222 |
9.71e-51 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 168.45 E-value: 9.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG--EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ-VGFV 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVKPRRERPseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSE----IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 160 LDEPFGALDAKVRKELrgW-----LRRLHddlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:cd03263 157 LDEPTSGLDPASRRAI--WdlileVRKGR-----SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-214 |
1.64e-50 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 165.50 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 hyalfrhmtvfenvafglrvkprrerpseaairakvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-237 |
6.47e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 167.23 E-value: 6.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS----------VGAR 72
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQVGFVFQHYALFRHMTVFENVAFG-LRVKprrERPSEAAIrAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARAL 151
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVK---GEPKEEAT-ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 152 AVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIfVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSA 231
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
....*.
gi 490296977 232 FVYEFL 237
Cdd:PRK11264 239 RTRQFL 244
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-224 |
7.81e-50 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 167.18 E-value: 7.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVF 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGlrvkpR----RERPSEAAiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:COG4604 82 QENHINSRLTVRELVAFG-----RfpysKGRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-214 |
1.02e-48 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 161.40 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFrHMTVFENVafglrvkprrerpseaairakvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDLhiSTIFVTHDqEEALEVADRIVVLNHGR 214
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGK--TVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-215 |
1.69e-48 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 162.50 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAA----LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE----- 73
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLrkqvLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRHMTVFENVAFGLRVKPRRERpseAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAV 153
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQPNLSY---QEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQeEALEVADRIVVLNHGRV 215
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
3.58e-48 |
|
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: 161.77 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASvGARE--RQVGFVF 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYgvPGAER------RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSP 221
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
4.08e-48 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 161.11 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR-ERQVGFV 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVKPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD------REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRlHDDLHISTIFVTHDQEEALevADRIVVL 210
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELA--AARVLDL 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-228 |
3.02e-47 |
|
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: 159.63 E-value: 3.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFV 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENV--AFGLRVKPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:cd03218 81 PQEASIFRKLTVEENIlaVLEIRGLSKKER------EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHdDLHIStIFVT-HDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILK-DRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-224 |
3.39e-47 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 159.14 E-value: 3.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFV 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVKPRRERPseaAIRAKVHELLSlvQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRK---ARLERVYELFP--RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-215 |
8.27e-47 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 159.46 E-value: 8.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVvLQGldVASVGARERQVGFVFQH 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG--TAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRvkprrerpseAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLK----------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-240 |
8.81e-47 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 159.36 E-value: 8.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVG----- 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 ----------FVFQHYALFRHMTVFENV------AFGLRVKPRRERpseaAIRakvheLLSLVQLDWLAQ-RYPSELSGG 140
Cdd:PRK10619 86 qlrllrtrltMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARER----AVK-----YLAKVGIDERAQgKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 141 QRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
250 260
....*....|....*....|
gi 490296977 221 PQAVYDHPRSAFVYEFLGAA 240
Cdd:PRK10619 236 PEQLFGNPQSPRLQQFLKGS 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
1.98e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 164.42 E-value: 1.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG---ARERQVGFV 79
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:COG1129 85 HQELNLVPNLSVAENIFLG-REPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-219 |
2.01e-46 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 156.95 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 22 SLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYALFRHMTVFENVAFGLRv 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 102 kprrerPS---EAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGW 178
Cdd:TIGR01277 97 ------PGlklNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490296977 179 LRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-238 |
2.41e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 157.50 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS--VGARERQ-VG 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHMTVFENV--AFGLRVKPRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:COG1137 82 YLPQEASIFRKLTVEDNIlaVLELRKLSKKER------EERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHdDLHIStIFVT-HDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVY 234
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLK-ERGIG-VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVY 233
|
....
gi 490296977 235 efLG 238
Cdd:COG1137 234 --LG 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6-223 |
3.07e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 157.05 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFgefaalddvSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYAL 85
Cdd:PRK10771 12 HHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 86 FRHMTVFENVAFGLRvkprrerPS---EAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK10771 83 FSHLTVAQNIGLGLN-------PGlklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQA 223
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
3.60e-46 |
|
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: 154.51 E-value: 3.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG---ARERQVGFV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASprdARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQhyalfrhmtvfenvafglrvkprrerpseaairakvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-237 |
6.86e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 160.97 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG------ARERQ 75
Cdd:PRK10070 28 GLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelreVRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRHMTVFENVAFGLRVK--PRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAV 153
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFGMELAgiNAEER------REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFV 233
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
....
gi 490296977 234 YEFL 237
Cdd:PRK10070 262 RTFF 265
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
3.75e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 161.35 E-value: 3.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA---SVGARERQVGFV 79
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsPRDAIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRvKPRRERPSEAAIRAKVHEllslvqldwLAQRYP---------SELSGGQRQRIALARA 150
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLE-PTKGGRLDRKAARARIRE---------LSERYGldvdpdakvEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-229 |
4.13e-45 |
|
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: 154.37 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFVF 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRvkPRRERPSEAAIRAKVHELLSLvqldwLAQRYPS---ELSGGQRQRIALARALAVEPKV 157
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAY--ARRDRAEVRADLERVYELFPR-----LKERRRQragTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-215 |
8.92e-45 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 152.76 E-value: 8.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQH 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVKPRRERpseaairaKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK--------RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHisTIFV-THDQEEALEVADRIVVLNHGRV 215
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGI--TVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-219 |
1.07e-44 |
|
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: 152.91 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ-VG 77
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRrLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHMTVFENVAFGLR---VKPRrerpseaAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGlygLKGD-------ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-227 |
1.89e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 154.02 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERQVGF 78
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHY-ALFRHMTVFENVAFGLRvkpRRERPSEAAIRaKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFGLE---NIGVPREEMVE-RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-219 |
2.07e-44 |
|
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: 151.58 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGeLVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ-VGFVFQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVKprRERPSEAaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLK--GIPSKEV--KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDlhISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-215 |
2.28e-44 |
|
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: 151.79 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQV 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFGLRV--KPRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVtgVPPRE------IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-215 |
2.34e-44 |
|
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: 152.12 E-value: 2.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRF--GEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER------Q 75
Cdd:TIGR02211 5 ENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRHMTVFENVAFGLRVkpRRERPSEAAIRAKvhELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLI--GKKSVKEAKERAY--EMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEAlEVADRIVVLNHGRV 215
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEMKDGQL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.85e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 154.02 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFG-----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqGLDVASVGARERQ 75
Cdd:PRK13634 1 MDITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 -------VGFVFQ--HYALFRHmTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDW-LAQRYPSELSGGQRQRI 145
Cdd:PRK13634 80 lkplrkkVGIVFQfpEHQLFEE-TVEKDICFG----PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
...
gi 490296977 226 DHP 228
Cdd:PRK13634 235 ADP 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-215 |
3.25e-44 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 150.87 E-value: 3.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFA-ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGlDVASVGARERQVGFVFQH 82
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-KPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 --YALFRHmTVFENVAFGLRVKPRRErpseaairAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELDAGN--------EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHIStIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAV-IVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-222 |
1.83e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.02 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHkrF---GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQV 76
Cdd:COG1132 339 EIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFrHMTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLvqldwLAQRYPSE-------LSGGQRQRIALAR 149
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEA-----LPDGYDTVvgergvnLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlhISTIFVTHdQEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHE 559
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-225 |
2.10e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 151.42 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG---EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERQVG 77
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHY-ALFRHMTVFENVAFGLRVK--PRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENKgiPHEE------MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEaLEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-243 |
2.56e-43 |
|
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: 149.73 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFV 79
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVafgLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:TIGR04406 82 PQEASIFRKLTVEENI---MAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYefLGA 239
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY--LGE 235
|
....
gi 490296977 240 ANRL 243
Cdd:TIGR04406 236 QFRL 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
7-228 |
3.76e-43 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 152.72 E-value: 3.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 7 NLHKRFGEfaaLD-DVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG---LDVAS---VGARERQVGFV 79
Cdd:PRK11144 5 NFKQQLGD---LClTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEKRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRvkprrerPSEAAIRAKVHELLSLvqlDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK11144 82 FQDARLFPHYKVRGNLRYGMA-------KSMVAQFDKIVALLGI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-227 |
5.58e-43 |
|
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: 156.46 E-value: 5.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFV 79
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFrHMTVFENVAFGlrvkprRERPSEAAIRAkvheLLSLVQLDWLAQRYP-----------SELSGGQRQRIALA 148
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLG------RPDASDEELEA----ALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLhiSTIFVTHDqEEALEVADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
1.25e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 146.29 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG--EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:PRK13632 8 IKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHY-ALFRHMTVFENVAFGLrvKPRRERPSEaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGL--ENKKVPPKK--MKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALeVADRIVVLNHGRVEQVGSPQAV 224
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-249 |
1.52e-41 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 146.06 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG------ARERqV 76
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlytVRKR-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFQHYALFRHMTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLR---EHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPrSAFVYEF 236
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQF 242
|
250
....*....|...
gi 490296977 237 lgaanrLDGTVSG 249
Cdd:PRK11831 243 ------LDGIADG 249
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-215 |
1.82e-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: 145.23 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVV-LQGLDVASVGARE--RQVGFV 79
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWElrKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 --FQHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:COG1119 84 spALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
3.29e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 144.87 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVF 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRakvhELLSLVQLDWLAQRYPSELSGGQRQRIALARALA-------V 153
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVR----EALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 154 EPKVLLLDEPFGALDAK----VRKELRGWLRRlhddlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:COG4559 158 GPRWLFLDEPTSALDLAhqhaVLRLARQLARR-----GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-229 |
3.98e-41 |
|
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: 150.99 E-value: 3.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG----EFAALDDVSLDFPAGELVALLGPSGCGKT----TLLRVIAGLEHADSGQVVLQGLDVASVGARE- 73
Cdd:COG4172 7 LSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 -----RQVGFVFQH--YALFRHMTVFENVAFGLRVKprrERPSEAAIRAKVHELLSLVQLDWLAQR---YPSELSGGQRQ 143
Cdd:COG4172 87 rrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLH---RGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 144 RIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDqeeaL----EVADRIVVLNHGRVEQVG 219
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LgvvrRFADRVAVMRQGEIVEQG 239
|
250
....*....|
gi 490296977 220 SPQAVYDHPR 229
Cdd:COG4172 240 PTAELFAAPQ 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-240 |
1.53e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 143.06 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-----EHADSGQVVLQGLDVAS--VGARE-- 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdVDPIEvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRHMTVFENVAFGLR----VKPRRERPSEAAIRAKVHELLSLVQlDWLaQRYPSELSGGQRQRIALAR 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKlnglVKSKKELDERVEWALKKAALWDEVK-DRL-NDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
250
....*....|.
gi 490296977 230 SAFVYEFLGAA 240
Cdd:PRK14267 241 HELTEKYVTGA 251
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-245 |
7.04e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 142.55 E-value: 7.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVgareRQVGFVF 80
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPEDR----RRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAF-----GLrvkprrerpSEAAIRAKVHELLSLVQL-DWLAQRYpSELSGGQRQRIALARALAVE 154
Cdd:COG4152 78 EERGLYPKMKVGEQLVYlarlkGL---------SKAEAKRRADEWLERLGLgDRANKKV-EELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD-HPRSAFV 233
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRqFGRNTLR 226
|
250
....*....|..
gi 490296977 234 YEFLGAANRLDG 245
Cdd:COG4152 227 LEADGDAGWLRA 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
9.91e-40 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 140.92 E-value: 9.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGlrvkprRE-------RPSEAAiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARAL 151
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYG------RSpwlslwgRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 152 AVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-215 |
1.85e-39 |
|
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: 139.26 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 14 EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFrHMTV 91
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFGLRVKpRRERPSEAAIRAKVHEllslvqldwLAQRYP-----------SELSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03245 95 RDNITLGAPLA-DDERILRAAELAGVTD---------FVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 161 DEPFGALD----AKVRKELRGWLRrlhddlHISTIFVTHDQeEALEVADRIVVLNHGRV 215
Cdd:cd03245 165 DEPTSAMDmnseERLKERLRQLLG------DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-244 |
1.90e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 142.03 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRF----GEFA------ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV-----ASVG 70
Cdd:PRK11308 9 IDLKKHYpvkrGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 71 ARERQVGFVFQH-YAlfrhmtvfenvafglRVKPRR------ERP-------SEAAIRAKVHELLSLVQLD-WLAQRYPS 135
Cdd:PRK11308 89 LLRQKIQIVFQNpYG---------------SLNPRKkvgqilEEPllintslSAAERREKALAMMAKVGLRpEHYDRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 136 ELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK11308 154 MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250 260
....*....|....*....|....*....
gi 490296977 216 EQVGSPQAVYDHPRSAFVYEFLGAANRLD 244
Cdd:PRK11308 234 VEKGTKEQIFNNPRHPYTQALLSATPRLN 262
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-215 |
2.65e-39 |
|
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: 138.81 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFVF 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVKPRRERPseaaIRAKVHELLSLvqLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRK----IPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-217 |
3.03e-39 |
|
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: 139.94 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG-----LDVASVGARERQVGFVFQ--HYALFRH 88
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqLDRKQRRAFRRDVQLVFQdsPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 89 MTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQL-DWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:TIGR02769 105 MTVRQIIGEPLR---HLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 168 DAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGR-VEQ 217
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQiVEE 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
5.23e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 139.07 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG-----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA--SVGARERQ 75
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYAL--FRHMTVFENVAFGL-RVKPRRERPS-EAAIRAKVHELLSLVQLDwLAQRYPSE---LSGGQRQRIALA 148
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLALAYrRGKRRGLRRGlTKKRRELFRELLATLGLG-LENRLDTKvglLSGGQRQALSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-227 |
8.70e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 138.73 E-value: 8.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQH-YALFRHMTVFE 93
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 94 NVAFGLRvkpRRERPSEAAIRaKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRK 173
Cdd:PRK13648 104 DVAFGLE---NHAVPYDEMHR-RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 174 ELRGWLRRLHDDLHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-226 |
9.96e-39 |
|
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: 137.75 E-value: 9.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFrHMTVFE 93
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 94 NVAFGLRVKPrRERPSEAAIRAKVHELlslvqLDWLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:cd03251 95 NIAYGRPGAT-REEVEEAARAANAHEF-----IMELPEGYDTVigergvkLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 167 LDAKVRKELRGWLRRLHDDlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:cd03251 169 LDTESERLVQAALERLMKN---RTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-229 |
1.34e-38 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 139.84 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER-----QVGFVFQH--YALFRHM 89
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TVFENVAFGLRV-KPRRERpseAAIRAKVHELLSLVQL-DWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:PRK15079 116 TIGEIIAEPLRTyHPKLSR---QEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 168 DAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-229 |
1.49e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 137.81 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV-GARERQVGFV-- 79
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFEN--VAFGLRVKPR-----------RERPSEAAIRAkvHELLSLVQLDWLAQRYPSELSGGQRQRIA 146
Cdd:PRK11300 86 FQHVRLFREMTVIENllVAQHQQLKTGlfsgllktpafRRAESEALDRA--ATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
...
gi 490296977 227 HPR 229
Cdd:PRK11300 244 NPD 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
2.72e-38 |
|
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: 143.75 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRF--GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVG 77
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFrHMTVFENVAFGlrvkprRERPSEAAIRAkvheLLSLVQLDWLAQRYP-----------SELSGGQRQRIA 146
Cdd:COG4987 413 VVPQRPHLF-DTTLRENLRLA------RPDATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELrgwLRRLHDDLHIST-IFVTHDqEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGRTvLLITHR-LAGLERMDRILVLEDGRIVEQGTHE 554
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
3.03e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.21 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKvhelLSLVQLDWLAQRYPSELSGGQRQRIALARALA------ 152
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAA----LAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 153 VEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-227 |
7.25e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 137.06 E-value: 7.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 14 EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL------QGLD-VASVGARERQVGFVFQ--HYA 84
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKkIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 85 LFRHmTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQL-DWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK13645 103 LFQE-TIEKDIAFG----PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-230 |
2.18e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 134.96 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRF---------GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARE 73
Cdd:COG4167 7 VRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGDYKYRC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQH--YALFRHMTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLdwL---AQRYPSELSGGQRQRIALA 148
Cdd:COG4167 87 KHIRMIFQDpnTSLNPRLNIGQILEEPLR---LNTDLTAEEREERIFATLRLVGL--LpehANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
..
gi 490296977 229 RS 230
Cdd:COG4167 242 QH 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
3.11e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 134.27 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-----EHADSGQVVLQGLDVASVGARE--RQ 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRHMTVFENVAFGLRVKprRERPSEAAIRAKVHELLSLVQL-DWLAQRYPS---ELSGGQRQRIALARAL 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLN--RLVKSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 152 AVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-224 |
4.65e-37 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 139.55 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQV-VLQG---LDVASVGARE 73
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 R-----QVGFVFQHYALFRHMTVFENV--AFGLrvkprrERPSEAAIRAKVHELLSLVQLDWLAQ----RYPSELSGGQR 142
Cdd:TIGR03269 360 RgrakrYIGILHQEYDLYPHRTVLDNLteAIGL------ELPDELARMKAVITLKMVGFDEEKAEeildKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 490296977 223 AV 224
Cdd:TIGR03269 514 EI 515
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
5.13e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.48 E-value: 5.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFV 79
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHY--ALFRhMTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFG----PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-219 |
5.89e-37 |
|
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: 132.40 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASvgARERQVGFVFQH 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--AARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGLRVK--PRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKglKKEE------ARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
1.30e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 138.27 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvGARerqVGFVFQHYA 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR---IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 85 LFRHMTVFENVAFGLR----VKPRRERPSEA------------------------AIRAKVHELLS---LVQLDWlaQRY 133
Cdd:COG0488 72 LDDDLTVLDTVLDGDAelraLEAELEELEAKlaepdedlerlaelqeefealggwEAEARAEEILSglgFPEEDL--DRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 134 PSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRlhddLHISTIFVTHDQEEALEVADRIVVLNHG 213
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHDRYFLDRVATRILELDRG 225
|
..
gi 490296977 214 RV 215
Cdd:COG0488 226 KL 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-224 |
2.39e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 139.23 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA--SVGARERQVGFVFQHYALFrHMTVFE 93
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPADLRRNIGYVPQDPRLF-YGTLRD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 94 NVAFGlRVKPRRERPSEAAIRAKVHELlslvqldwlAQRYPS-----------ELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:TIGR03375 558 NIALG-APYADDEEILRAAELAGVTEF---------VRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 163 PFGALD----AKVRKELRGWLRrlhddlHISTIFVTHDQeEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:TIGR03375 628 PTSAMDnrseERFKDRLKRWLA------GKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-210 |
2.72e-36 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 130.99 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHY 83
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 84 ALFRHmTVFENVAFGLRVkpRRERPSEAAIRAkvhellSLVQL---DWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQI--RNQQPDPAIFLD------DLERFalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEaLEVADRIVVL 210
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-228 |
4.80e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 131.73 E-value: 4.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF---------GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG-----LDVAS 68
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplakLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 69 VGARERQVGFVFQHY--ALFRHMTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLD-WLAQRYPSELSGGQRQRI 145
Cdd:PRK10419 84 RKAFRRDIQMVFQDSisAVNPRKTVREIIREPLR---HLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV--EQVGSPQA 223
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKL 240
|
....*
gi 490296977 224 VYDHP 228
Cdd:PRK10419 241 TFSSP 245
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-222 |
1.02e-35 |
|
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: 129.97 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFrHMTVFENV 95
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLF-DGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGlrvKPRRERPS--EAAIRAKVHELLSLV--QLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKV 171
Cdd:cd03249 98 RYG---KPDATDEEveEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 172 RKELRGWLRRLHDDlhISTIFVTHdQEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:cd03249 175 EKLVQEALDRAMKG--RTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHD 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-227 |
3.28e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 129.86 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFG-----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS------V 69
Cdd:PRK13649 1 MGINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 70 GARERQVGFVFQ--HYALFRHmTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDW-LAQRYPSELSGGQRQRIA 146
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEE-TVLKDVAFG----PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 490296977 227 H 227
Cdd:PRK13649 235 D 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-228 |
5.00e-35 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 128.35 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-----EHADSGQVVLQGLDVAS-----VGAR 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSprtdtVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 eRQVGFVFQHYALFRhMTVFENVAFGLRVKPRRERpseAAIRAKVHEllSLVQL---DWLAQRYPSE---LSGGQRQRIA 146
Cdd:PRK14239 86 -KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDK---QVLDEAVEK--SLKGAsiwDEVKDRLHDSalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
..
gi 490296977 227 HP 228
Cdd:PRK14239 237 NP 238
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-207 |
5.24e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.01 E-value: 5.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGE----FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGA----RERQ 75
Cdd:PRK11629 9 DNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAkaelRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRHMTVFENVAFGLRVKprRERPSEAAIRAkvHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIG--KKKPAEINSRA--LEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 156 KVLLLDEPFGALDAKVRK---ELRGWLRRLHddlhiSTIF--VTHDqeeaLEVADRI 207
Cdd:PRK11629 165 RLVLADEPTGNLDARNADsifQLLGELNRLQ-----GTAFlvVTHD----LQLAKRM 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-225 |
5.40e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.05 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG----ARERqVGFVFQH-----YALFr 87
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdIRNK-AGMVFQNpdnqiVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 88 hmtVFENVAFG---LRVKPRRerpseaaIRAKVHELLSLVQLdWLAQRY-PSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK13633 103 ---VEEDVAFGpenLGIPPEE-------IRERVDESLKKVGM-YEYRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-232 |
6.02e-35 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 128.51 E-value: 6.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG-----LDVASVGARERQV-- 76
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 ----GFVFQHYALFRHMTVFENVAFGLRVKPRRERpSEAAIRAKVHELLSLVQLDwlAQR---YPSELSGGQRQRIALAR 149
Cdd:PRK11701 88 rtewGFVHQHPRDGLRMQVSAGGNIGERLMAVGAR-HYGDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPR 229
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
...
gi 490296977 230 SAF 232
Cdd:PRK11701 245 HPY 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-227 |
7.61e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 7.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----------------------GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVV 60
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 61 LQGlDVAS---VGArerqvGFVfqhyalfRHMTVFENVAFGLRV--KPRRErpseaaIRAKVHELLSLVQL-DWLAQ--- 131
Cdd:COG1134 85 VNG-RVSAlleLGA-----GFH-------PELTGRENIYLNGRLlgLSRKE------IDEKFDEIVEFAELgDFIDQpvk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 132 RYPSelsgGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLN 211
Cdd:COG1134 146 TYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|....*.
gi 490296977 212 HGRVEQVGSPQAVYDH 227
Cdd:COG1134 221 KGRLVMDGDPEEVIAA 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-226 |
7.75e-35 |
|
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: 127.60 E-value: 7.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG--EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--ERQVGF 78
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLVQL--DWLAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:cd03252 81 VLQENVLFNR-SIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 157 VLLLDEPFGALDAKVRKELrgwLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:cd03252 159 ILIFDEATSALDYESEHAI---MRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-224 |
9.15e-35 |
|
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: 133.72 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA--SVGARERQVGFVFQHYALFRHmTVFE 93
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 94 NVA-FGlrvKPRRERPSEAAIRAKVHEL-LSlvqldwLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:COG4618 425 NIArFG---DADPEKVVAAAKLAGVHEMiLR------LPDGYDTRigeggarLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 165 GALDAKVRKELRGWLRRLHDDlHISTIFVTHDQeEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
1.16e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 129.05 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFG-----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLD---------- 65
Cdd:PRK13651 1 MQIKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 66 ----------------VASVGARERQVGFVFQ--HYALFRHmTVFENVAFGlrvkPRR--ERPSEAAIRAKvhELLSLVQ 125
Cdd:PRK13651 81 ekvleklviqktrfkkIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFG----PVSmgVSKEEAKKRAA--KYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 126 LD--WLaQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEV 203
Cdd:PRK13651 154 LDesYL-QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEW 231
|
250
....*....|..
gi 490296977 204 ADRIVVLNHGRV 215
Cdd:PRK13651 232 TKRTIFFKDGKI 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-228 |
2.61e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 127.22 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 14 EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGA------RERqVGFVFQHY-ALF 86
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAktvwdiREK-VGIVFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 87 RHMTVFENVAFGL--RVKPRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK13640 98 VGATVGDDVAFGLenRAVPRPE------MIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 165 GALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEAlEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-226 |
5.28e-34 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 124.96 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 27 AGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvASVGARERQVGFVFQ--HYALFRHMTVFENVAFGL--RVK 102
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---ASPGKGWRHIGYVPQrhEFAWDFPISVAHTVMSGRtgHIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 103 PRReRPSEAAIRAkVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRL 182
Cdd:TIGR03771 82 WLR-RPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490296977 183 HDDLHiSTIFVTHDQEEALEVADRIVVLNhGRVEQVGSPQAVYD 226
Cdd:TIGR03771 160 AGAGT-AILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
7.00e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.07 E-value: 7.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNL-HKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFV 79
Cdd:PRK13652 4 IETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHY--ALFRhMTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK13652 84 FQNPddQIFS-PTVEQDIAFG----PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-238 |
1.06e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.46 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ-VGFVFQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENvafgLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:PRK13537 88 FDNLDPDFTVREN----LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 162 EPFGALDAKVR----KELRGWLRRLHddlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFL 237
Cdd:PRK13537 164 EPTTGLDPQARhlmwERLRSLLARGK-----TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIY 238
|
.
gi 490296977 238 G 238
Cdd:PRK13537 239 G 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-308 |
1.45e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.04 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYdhprsafvyeflg 238
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL------------- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 239 AANRLDGTVSGNGFV----AHGAAQAIAVDADFAGPARAYVRPHDLELAAPHARAqgiaadVRRVVPLGGSVRV 308
Cdd:PRK09536 228 TADTLRAAFDARTAVgtdpATGAPTVTPLPDPDRTEAAADTRVHVVGGGQPAARA------VSRLVAAGASVSV 295
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-214 |
1.52e-33 |
|
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: 122.96 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvgarerQVGFVFQhYALFRHMTVFENVA 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQ-EPWIQNGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 97 FGLRVKPRRERpseaairaKVHELLSLVQ-LDWLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:cd03250 88 FGKPFDEERYE--------KVIKACALEPdLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 169 AKVRKEL-----RGWLrrlhddLHIST-IFVTHdQEEALEVADRIVVLNHGR 214
Cdd:cd03250 160 AHVGRHIfenciLGLL------LNNKTrILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-220 |
2.80e-33 |
|
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: 129.45 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFG--EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQ--LDWLAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPlgLDTPIGENGVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDLhiSTIFVTHdQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQGR--TTLVIAH-RLSTIEKADRIVVMDDGRIVERGT 550
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
2.81e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.97 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADS---GQVVLQGLDVASVGARER----- 74
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARdirks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 --QVGFVFQHYALFRHMTVFENVAFGL-------RVKPRRERPSEaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRI 145
Cdd:PRK09984 85 raNTGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQ---KQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAvY 225
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-F 240
|
....*....
gi 490296977 226 DHPRSAFVY 234
Cdd:PRK09984 241 DNERFDHLY 249
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-221 |
5.72e-33 |
|
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: 122.34 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHkrFG---EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV--GARERQVG 77
Cdd:cd03253 1 IEFENVT--FAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFrHMTVFENVAFGlRVKPRRERPSEAAIRAKVHEllSLVQLdwlAQRYPSE-------LSGGQRQRIALARA 150
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYG-RPDATDEEVIEAAKAAQIHD--KIMRF---PDGYDTIvgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDdlHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSP 221
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-215 |
5.72e-33 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 129.07 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 13 GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGA------RERQVGFVFQHYALF 86
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 87 RHMTVFENVAF-----GLRVKPRRERpseaairakVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:PRK10535 99 SHLTAAQNVEVpavyaGLERKQRLLR---------AQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 162 EPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEvADRIVVLNHGRV 215
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-219 |
5.86e-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: 5.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----------------------GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVV 60
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 61 LQGLDVASVGArerQVGFvfqHYALfrhmTVFENVAFGLRVKPRrerpSEAAIRAKVHELLSLVQL-DWLAQRYpSELSG 139
Cdd:cd03220 81 VRGRVSSLLGL---GGGF---NPEL----TGRENIYLNGRLLGL----SRKEIDEKIDEIIEFSELgDFIDLPV-KTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 140 GQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHIStIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTV-ILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-210 |
7.01e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 11 RFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVlqgldvasvGARERQVGFVFQHYALFRHM- 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 -TVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:NF040873 72 lTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490296977 169 AKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEvADRIVVL 210
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-222 |
7.86e-33 |
|
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: 121.95 E-value: 7.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHmTVFEN 94
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 95 VAFGlRVKPRRERPSEAAIRAKVHELlslvqLDWLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:cd03254 97 IRLG-RPNATDEEVIEAAKEAGAHDF-----IMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 168 DAKVRKELRGWLRRLHDDL-------HISTIfvthdqeealEVADRIVVLNHGRVEQVGSPQ 222
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRtsiiiahRLSTI----------KNADKILVLDDGKIIEEGTHD 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-240 |
1.18e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.51 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 8 LHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTT----LLRVIAGlehadSGQVVLQGLDVASVGARE-----RQVGF 78
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllpvrHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQ--HYALFRHMTVFENVAFGLRVkpRRERPSEAAIRAKVHELLSLVQLD-WLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRV--HQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYE 235
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
....*
gi 490296977 236 FLGAA 240
Cdd:PRK15134 525 LLALS 529
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-237 |
1.51e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 122.08 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-EHADS-----GQVVLQGLDVASVGARE--RQVGFVFQHYALFR 87
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 88 HMTVFENVAFGLR---VKPRRErpseaaIRAKVHELLSLVQLdW--LAQRY---PSELSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK14246 104 HLSIYDNIAYPLKshgIKEKRE------IKKIVEECLRKVGL-WkeVYDRLnspASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFL 237
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-210 |
1.73e-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: 127.02 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERQVGFV 79
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHmTVFENVAFGLRVKPRRERpSEAAIRAKVHELLS-LVQ-LDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPDASDAEI-REALERAGLDEFVAaLPQgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLhiSTIFVTHDqEEALEVADRIVVL 210
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-215 |
1.92e-32 |
|
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: 119.24 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAA--LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVafglrvkprrerpseaairakvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03246 81 LPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLhDDLHISTIFVTHdQEEALEVADRIVVLNHGRV 215
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-231 |
3.16e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 121.74 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 7 NLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLE-----HADSGQVVLQG---LDVASVGARERQVGF 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGrsiFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRhMTVFENVAFGLRVK---PRRERPSEAAIRAKVHELLSLVQlDWLAQRyPSELSGGQRQRIALARALAVEP 155
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHklvPRKEFRGVAQARLTEVGLWDAVK-DRLSDS-PFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSA 231
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-214 |
9.52e-32 |
|
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: 119.08 E-value: 9.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF-------GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL----QGLDVASVGA 71
Cdd:COG4778 5 LEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 72 RE------RQVGFVFQHyalfrhmtvfenvafgLRVKPR-----------RER-PSEAAIRAKVHELLSLVQLD-WLAQR 132
Cdd:COG4778 85 REilalrrRTIGYVSQF----------------LRVIPRvsaldvvaeplLERgVDREEARARARELLARLNLPeRLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 133 YPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNH 212
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTP 227
|
..
gi 490296977 213 GR 214
Cdd:COG4778 228 FS 229
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-232 |
1.53e-31 |
|
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: 119.16 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL-----QGLDVASVGARERQV- 76
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 -----GFVFQHYALFRHMTVFENVAFGLRVKPRRERpSEAAIRAKVHELLSLVQLDwlAQRY---PSELSGGQRQRIALA 148
Cdd:TIGR02323 84 mrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGAR-HYGNIRATAQDWLEEVEID--PTRIddlPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....
gi 490296977 229 RSAF 232
Cdd:TIGR02323 241 QHPY 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-239 |
1.59e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.97 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFG-----------EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE 73
Cdd:PRK10261 316 VRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 -----RQVGFVFQ--HYALFRHMTVFENVAFGLRVkpRRERPSEAAiRAKVHELLSLVQL-DWLAQRYPSELSGGQRQRI 145
Cdd:PRK10261 396 lqalrRDIQFIFQdpYASLDPRQTVGDSIMEPLRV--HGLLPGKAA-AARVAWLLERVGLlPEHAWRYPHEFSGGQRQRI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
250
....*....|....
gi 490296977 226 DHPRSAFVYEFLGA 239
Cdd:PRK10261 553 ENPQHPYTRKLMAA 566
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-243 |
2.12e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.46 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFV 79
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVkprRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQI---RDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYefLGA 239
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY--LGE 237
|
....
gi 490296977 240 ANRL 243
Cdd:PRK10895 238 DFRL 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-215 |
3.50e-31 |
|
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: 117.82 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 9 HKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR-ERQVGFVF-QHYALF 86
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 87 RHMTVFEnvafGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:cd03267 108 WDLPVID----SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490296977 167 LDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-228 |
5.18e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.78 E-value: 5.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA------SVGARERQVGFVFQ--HYALFRHm 89
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQL-DWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK13641 102 TVLKDVEFG----PKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 169 AKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-215 |
5.74e-31 |
|
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: 116.11 E-value: 5.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL--EHADSGQVVLQGLDVASVGAReRQVGFVFQHYALFRHMTVFENV 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFR-KIIGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGlrvkprrerpseAAIRAkvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKEL 175
Cdd:cd03213 104 MFA------------AKLRG---------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490296977 176 RGWLRRLHDDlHISTIFVTHD-QEEALEVADRIVVLNHGRV 215
Cdd:cd03213 151 MSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-215 |
6.56e-31 |
|
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: 116.60 E-value: 6.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD---SGQVVLQGLdvasvgARERQ-----VGFVFQHYALFRHM 89
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ------PRKPDqfqkcVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TVFENVAFGLRVKPRRERPSeaAIRAKVHE--LLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSD--AIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 168 DAKVRKELRGWLRRL-HDDlhiSTIFVTHDQ--EEALEVADRIVVLNHGRV 215
Cdd:cd03234 175 DSFTALNLVSTLSQLaRRN---RIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-211 |
2.08e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.42 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLR-------VIAGLEHadSGQVVLQGL-----DVASVGARe 73
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKnlyapDVDPVEVR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQHYALFRHmTVFENVAFGLRV---KPRRERPSEAAIRAKVheLLSLVQlDWLAQRYPSeLSGGQRQRIALARA 150
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGARIngyKGDMDELVERSLRQAA--LWDEVK-DKLKQSGLS-LSGGQQQRLCIARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHIstIFVTHDQEEALEVADRIVVLN 211
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFN 224
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-222 |
2.56e-30 |
|
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: 121.60 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS--VGARERQVG 77
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHmTVFENVAFGLRVKPrrERPSEAAirakvhellSLVQLDWLAQRYP-------SE----LSGGQRQRIA 146
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPLTL--DEAWEAA---------RMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALD----AKVRKELrgwlrrlhDDLHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQ 222
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDnrtqAIVSESL--------ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYD 669
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-252 |
2.82e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.33 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG----LDVASVGARERQVG 77
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHY--ALFRHmTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:PRK13639 82 IVFQNPddQLFAP-TVEEDVAFG----PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDH-------- 227
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDietirkan 235
|
250 260
....*....|....*....|....*...
gi 490296977 228 ---PRSAFVYEFLgaaNRLDGTVSGNGF 252
Cdd:PRK13639 236 lrlPRVAHLIEIL---NKEDNLPIKMGY 260
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
17-220 |
3.59e-30 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 120.96 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHmTVFEN 94
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAElrARMALVPQDPVLFAA-SVMEN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 95 VAFGlRVKPRRERPSEAAIRAKVHELLSLvqldwLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:TIGR02204 434 IRYG-RPDATDEEVEAAARAAHAHEFISA-----LPEGYDTYlgergvtLSGGQRQRIAIARAILKDAPILLLDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 168 DAKVRKELRGWLRRLHDdlHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGS 220
Cdd:TIGR02204 508 DAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGT 557
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
3.79e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV-ASVGARERQVGFV 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENvafgLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK13536 120 PQFDNLDLEFTVREN----LLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 160 LDEPFGALDAKVR----KELRGWLRRlhddlHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYE 235
Cdd:PRK13536 196 LDEPTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIE 270
|
...
gi 490296977 236 FLG 238
Cdd:PRK13536 271 IYG 273
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-200 |
4.29e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.49 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE----FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGA------R 72
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaklR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQVGFVFQHYALFRHMTVFENVAFGLRVKPRRERPSeaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALA 152
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQS----RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 153 VEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEA 200
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-219 |
6.17e-30 |
|
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: 112.79 E-value: 6.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE--FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV-GARERQVGFV 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLeKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFrHMTVFENVafGLRvkprrerpseaairakvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03247 81 NQRPYLF-DTTLRNNL--GRR------------------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 160 LDEPFGALDAKVRKELrgwLRRLHDDLHIST-IFVTHdQEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03247 122 LDEPTVGLDPITERQL---LSLIFEVLKDKTlIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-224 |
1.22e-29 |
|
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: 118.75 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLE--HADSGQVV-------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 61 ---------------LQGLDVASVGARERQVGFVFQH-YALFRHMTVFENVafgLRVKPRRERPSEAAIRAKVhELLSLV 124
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNV---LEALEEIGYEGKEAVGRAV-DLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 125 QLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVA 204
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|
gi 490296977 205 DRIVVLNHGRVEQVGSPQAV 224
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
1.91e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 111.37 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRfgefAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFV- 79
Cdd:cd03215 6 EVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 --FQHYALFRHMTVFENVAFglrvkprrerpseaairakvhellslvqldwlaqryPSELSGGQRQRIALARALAVEPKV 157
Cdd:cd03215 82 edRKREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-228 |
2.37e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.93 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV----GAReRQVGFVFQH-YALFRHMTV 91
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsklqGIR-KLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKV 171
Cdd:PRK13644 96 EEDLAFG----PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 172 RKELRGWLRRLHDDLHiSTIFVTHDQEEaLEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:PRK13644 172 GIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-219 |
3.15e-29 |
|
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: 117.83 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHmTVFENV 95
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 A-FGLRVKPrrERPSEAAIRAKVHELLslvqldwlaQRYP-----------SELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:TIGR01842 413 ArFGENADP--EKIIEAAKLAGVHELI---------LRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDlHISTIFVTHdQEEALEVADRIVVLNHGRVEQVG 219
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
17-240 |
7.26e-29 |
|
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: 111.31 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD----SGQVVLQGLDVASVGARERQVGFVFQHyalfrHMTVF 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQN-----PRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 93 eNVAFGLRVKPR-----RERPSEAAIRAKVHELL--SLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:TIGR02770 76 -NPLFTMGNHAIetlrsLGKLSKQARALILEALEavGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 166 ALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYEFLGAA 240
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAH 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-225 |
8.93e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.49 E-value: 8.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNL---HKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERQVG 77
Cdd:PRK13642 5 LEVENLvfkYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHY-ALFRHMTVFENVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLDWlAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGME---NQGIPREEMIKRVDEALLAVNMLDF-KTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-225 |
1.18e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE------RQVGFVFQ--HYALFRH 88
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 89 mTVFENVAFGLRVKPRRERPSEAaIRAKVHELLSLVQLDWlaQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEK-IAAEKLEMVGLADEFW--EKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 169 AKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-215 |
1.56e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.35 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-----RQVGFVFQHYALFRHMTV 91
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFGLRVKPrrerPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDakv 171
Cdd:PRK10908 97 YDNVAIPLIIAG----ASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490296977 172 rKELRGWLRRLHDDLH---ISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK10908 170 -DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-215 |
6.18e-28 |
|
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: 108.71 E-value: 6.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--ERQVGFVFQHYALFRHmTVFENV 95
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGLRVKPRrERPSEAAIRAKVHELLSLVQL--DWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDA---- 169
Cdd:cd03248 109 AYGLQSCSF-ECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAeseq 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490296977 170 KVRKELRGWLRRlhddlhiSTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:cd03248 188 QVQQALYDWPER-------RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-220 |
9.03e-28 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 114.45 E-value: 9.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAA--LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--ERQVG 77
Cdd:TIGR01846 455 AITFENIRFRYAPDSPevLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHmTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLvqldwLAQRYPSE-------LSGGQRQRIALARA 150
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALC-NPGAPFEHVIHAAKLAGAHDFISE-----LPQGYNTEvgekganLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELrgwLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALI---MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGR 674
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
1.94e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.17 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFA-ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARE--RQVG 77
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKlrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQH--YALFRhMTVFENVAFGlrvkPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFG----AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
2.40e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.55 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE-----FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL----------EHADSGQVVLQGLDVA 67
Cdd:PRK13631 22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 68 SVGARE--------RQVGFVFQ--HYALFRHmTVFENVAFG---LRVKPrrerpSEAAIRAKVHelLSLVQLDW-LAQRY 133
Cdd:PRK13631 102 NPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKK-----SEAKKLAKFY--LNKMGLDDsYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 134 PSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLrrLHDDLHISTIFV-THDQEEALEVADRIVVLNH 212
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI--LDAKANNKTVFViTHTMEHVLEVADEVIVMDK 251
|
250
....*....|...
gi 490296977 213 GRVEQVGSPQAVY 225
Cdd:PRK13631 252 GKILKTGTPYEIF 264
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-228 |
4.38e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.12 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTllrVIAGLEH---ADSGQVVLQGLDVASVGAR--ERQVGFVFQHYALFRHmTVF 92
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 93 ENVAFGLRVKPRRERPSeAAIRAKVHELLSLVQLDWLAQRYP--SELSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMA-AAKAANAHDFIMEFPNGYDTEVGEkgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 171 VRKELRGWlRRLHDdlhISTIFVTHdQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:TIGR00958 652 CEQLLQES-RSRAS---RTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-224 |
5.82e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.18 E-value: 5.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--ERQVGFVFQ 81
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGlrvkprrERPSEAAI-------RAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVE 154
Cdd:PRK10575 93 QLPAAEGMTVRELVAIG-------RYPWHGALgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
7.36e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.04 E-value: 7.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADS-----GQVVLQGLDV----ASVGAR 72
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQVGFVFQHYALFRhMTVFENVAFGLRV---KPRRERPS--EAAIRAKvhELLSLVQLDwlAQRYPSELSGGQRQRIAL 147
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDivESALKDA--DLWDEIKHK--IHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVL--NHGRVEQV---GSPQ 222
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTK 241
|
250
....*....|....*
gi 490296977 223 AVYDHPRSAFVYEFL 237
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-226 |
1.08e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.87 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNL-HKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLdvasVGARER-----QVG 77
Cdd:COG4586 23 ALKGLfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----VPFKRRkefarRIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVF-QHYALFRHMTVFENvaFGL-----RVkprrerpSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARAL 151
Cdd:COG4586 99 VVFgQRSQLWWDLPAIDS--FRLlkaiyRI-------PDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 152 AVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQE--EALevADRIVVLNHGRVeqvgspqaVYD 226
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRI--------IYD 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-215 |
1.29e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 4 TVRNLHKRfgefAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERQvGFVF- 80
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRA-GIAYv 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 ----QHYALFRHMTVFENVAF--------GLRVKPRRERpsEAAirAKVHELLSLvqldwlaqRYPS------ELSGGQR 142
Cdd:COG1129 333 pedrKGEGLVLDLSIRENITLasldrlsrGGLLDRRRER--ALA--EEYIKRLRI--------KTPSpeqpvgNLSGGNQ 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-225 |
4.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.25 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 14 EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS------VGARERQVGFVFQhyalFR 87
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 88 HMTVFE-NVAFGLRVKPRRERPSEAAIRAKVHELLslVQLDW---LAQRYPSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK13646 95 ESQLFEdTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFsrdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
4.83e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqGLDVasvgarerQVGFVFQH 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFR-HMTVFENVafglrvkpRRERP--SEAAIRAkvheLLSlvqlDWL-----AQRYPSELSGGQRQRIALARALAVE 154
Cdd:COG0488 387 QEELDpDKTVLDEL--------RDGAPggTEQEVRG----YLG----RFLfsgddAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 155 PKVLLLDEPFGALDAKVRKEL-------RGWLrrlhddlhistIFVTHDqEEALE-VADRIVVLNHGRVE 216
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALeealddfPGTV-----------LLVSHD-RYFLDrVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-225 |
5.24e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.70 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 11 RFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVG--ARERQVGFVFQ--HYA 84
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGllALRQQVATVFQdpEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 85 LFrHMTVFENVAFGLRvkprRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK13638 90 IF-YTDIDSDIAFSLR----NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 165 GALDAKVRKELRGWLRRL-HDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVY 225
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIvAQGNHV--IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-221 |
1.19e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 103.22 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLE--HADSGQVVLQGLDVASVGARERQ---VGFV 79
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAragIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFEnvaFgLRV---KPRRERPSEAAIRAKVHELLSLVQLDW-LAQRYPSE-LSGGQRQRIALARALAVE 154
Cdd:COG0396 83 FQYPVEIPGVSVSN---F-LRTalnARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHdQEEALE--VADRIVVLNHGRVEQVGSP 221
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDyiKPDFVHVLVDGRIVKSGGK 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-175 |
1.89e-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: 107.06 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRF-GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFrHMTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLVQ--LDWLAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
170
....*....|....*....
gi 490296977 157 VLLLDEPFGALDAKVRKEL 175
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADEL 510
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-220 |
2.90e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.64 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 14 EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA--SVGARERQVGFVFQHYALFRHmTV 91
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQ--LDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:PRK11176 434 ANNIAYARTEQYSREQIEEAARMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490296977 170 KVRKELRGWLRRLHDDlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PRK11176 514 ESERAIQAALDELQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVERGT 561
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-214 |
4.23e-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: 105.68 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-EHAD-SGQVVLQGLDVASVGARERQ---VG 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGTwDGEIYWSGSPLKASNIRDTEragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYP-SELSGGQRQRIALARALAVEPK 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-220 |
7.37e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 105.80 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLhkRFG----EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVgARER---Q 75
Cdd:TIGR03796 478 VELRNI--TFGysplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanS 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRHmTVFENVAFGLRVKPRrERPSEAAIRAKVHELLSLvqldwLAQRYPSEL-------SGGQRQRIALA 148
Cdd:TIGR03796 555 VAMVDQDIFLFEG-TVRDNLTLWDPTIPD-ADLVRACKDAAIHDVITS-----RPGGYDAELaegganlSGGQRQRLEIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELRGWLRRlhddLHISTIFVTHdQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-220 |
1.24e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 105.21 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV--GARERQVGFVFQHYALFRHmTVFEN 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 95 VAFGLRvkprrerpsEAAIRAKVHELLSLVQLDWLAQRYP-----------SELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:TIGR01193 568 LLLGAK---------ENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDlhiSTIFVTHdqeeALEVA---DRIVVLNHGRVEQVGS 220
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK---TIIFVAH----RLSVAkqsDKIIVLDHGKIIEQGS 691
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-221 |
1.42e-24 |
|
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: 105.48 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFA--ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV-ASVGARERQVGF 78
Cdd:TIGR01257 928 GVCVKNLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHMTVFENVAFGLRVKPRRERPSEAAIRAkvheLLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVL 158
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHDDLHIstIFVTHDQEEALEVADRIVVLNHGRVEQVGSP 221
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSGRTI--IMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-223 |
1.46e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 104.82 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERqVGFVF 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIATRRR-VGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVA-----FGLrvkprrerpSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:NF033858 346 QAFSLYGELTVRQNLElharlFHL---------PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 156 KVLLLDEPFGALDAKVRKELrgWlrRLHDDLhiS-----TIFV-THDQEEAlEVADRIVVLNHGRVEQVGSPQA 223
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMF--W--RLLIEL--SredgvTIFIsTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-214 |
2.18e-24 |
|
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: 96.75 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVvlqgldvasvgarerqvgfvfqh 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 yalfrhmTVFENVAFGlrvkprrerpseaairakvhellslvqldwlaqrYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03221 58 -------TWGSTVKIG----------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLhistIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYPGTV----ILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-169 |
2.98e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.41 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERqvgfvf 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHY-----ALFRHMTVFENVAFGLRVKPRRERPSEAAIRAkvhellslVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:PRK13539 75 CHYlghrnAMKPALTVAENLEFWAAFLGGEELDIAAALEA--------VGLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170
....*....|....
gi 490296977 156 KVLLLDEPFGALDA 169
Cdd:PRK13539 147 PIWILDEPTAALDA 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-214 |
4.12e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.70 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-EHAD-SGQVVLQGLDVASVGARERQ---VGFVF 80
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELQASNIRDTEragIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLRVKPRReRPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK13549 89 QELALVKELSVLENIFLGNEITPGG-IMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 161 DEPFGALDAkvrKELRGWLRRLHD--DLHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:PRK13549 168 DEPTASLTE---SETAVLLDIIRDlkAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-170 |
1.17e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 96.66 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV-GARERQVGFVFQ 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFglrvkprrERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLD 161
Cdd:TIGR01189 81 LPGLKPELSALENLHF--------WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 490296977 162 EPFGALDAK 170
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-252 |
1.48e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.86 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKT----TLLRVI--AGLEhADSGQVVL-----QGLDVA 67
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLrrrsrQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 68 SVGARERQ------VGFVFQH--YALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSG 139
Cdd:PRK10261 92 EQSAAQMRhvrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 140 GQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVG 219
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260 270
....*....|....*....|....*....|...
gi 490296977 220 SPQAVYDHPRSAFVYEFLGAANRLdGTVSGNGF 252
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQL-GAMKGLDY 283
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-224 |
1.86e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 101.74 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERqvgfVFQH 82
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA----VCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YA---------LFRHMTVFENVAF-----GLRvkpRRERpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALA 148
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFfgrlfGQD---AAER------RRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 149 RALAVEPKVLLLDEP-----------FGALDAKVRKELRGwlrrlhddlhISTIFVTHDQEEAlEVADRIVVLNHGRVEQ 217
Cdd:NF033858 149 CALIHDPDLLILDEPttgvdplsrrqFWELIDRIRAERPG----------MSVLVATAYMEEA-ERFDWLVAMDAGRVLA 217
|
....*..
gi 490296977 218 VGSPQAV 224
Cdd:NF033858 218 TGTPAEL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-214 |
2.51e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.37 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR---ERQVGFVFQH 82
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK11288 88 LHLVPEMTVAENLYLG-QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHIsTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-224 |
3.02e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.98 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 12 FGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHM 89
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TVFENVAFG------LRVKPRRErPSEAAIRAkvhelLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK10253 97 TVQELVARGryphqpLFTRWRKE-DEEAVTKA-----MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-250 |
3.23e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.26 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD---SGQVVLQGLDVASVGARE-- 73
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKEln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 ----RQVGFVFQH--YALFRHMTVFENVAFGLRVKPRRERPS--EAAIRakvheLLSLVQLDWLAQR---YPSELSGGQR 142
Cdd:PRK09473 93 klraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEafEESVR-----MLDAVKMPEARKRmkmYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
250 260 270
....*....|....*....|....*....|....
gi 490296977 223 AVYDHPRSAFVYEFLGAANRLDG------TVSGN 250
Cdd:PRK09473 248 DVFYQPSHPYSIGLLNAVPRLDAegesllTIPGN 281
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-220 |
3.94e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.42 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGAR--ERQVGFVFQHYALFRHmTVFEN 94
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 95 VAFGlRVKPRRERPSEAAIRAKVHELL--SLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVR 172
Cdd:PRK13657 429 IRVG-RPDATDEEMRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 173 KELRGWLRRLhddLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PRK13657 508 AKVKAALDEL---MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-215 |
5.23e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLH-KRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFV- 79
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrlgVAYIp 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 --FQHYALFRHMTVFENVAFGLRVKPRRERP---SEAAIRAKVHELLSlvQLDwlaQRYPSE------LSGGQRQRIALA 148
Cdd:COG3845 340 edRLGRGLVPDMSVAENLILGRYRRPPFSRGgflDRKAIRAFAEELIE--EFD---VRTPGPdtparsLSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 149 RALAVEPKVLLLDEPFGALD----AKVRKELRGwLRrlhdDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLE-LR----DAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-233 |
1.07e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.95 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAS-VGAR--ERQVGFV 79
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKimREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLRVKPRRERPSEAairAKVHELLSLVQlDWLAQRyPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERI---KWVYELFPRLH-ERRIQR-AGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLhiSTIF-VTHDQEEALEVADRIVVLNHGRV--EQVGSPQAVYDHPRSAFV 233
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQG--MTIFlVEQNANQALKLADRGYVLENGHVvlEDTGDALLANEAVRSAYL 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-217 |
1.27e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 98.74 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV--GARERQVGFVFQHYALFrHMTVFENV 95
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtqASLRAAIGIVPQDTVLF-NDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGlRVKPRRERPSEAAIRAKVHELLSLvqldwLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:COG5265 453 AYG-RPDASEEEVEAAARAAQIHDFIES-----LPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 169 AKVRKELRGWLRRL---HDDLHI----STIfvTHdqeealevADRIVVLNHGR-VEQ 217
Cdd:COG5265 527 SRTERAIQAALREVargRTTLVIahrlSTI--VD--------ADEILVLEAGRiVER 573
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-228 |
2.42e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvgarERQVGFVFQH 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------KLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALfrHMTVFENVAFGLRVKPrrerpseAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK09544 76 LYL--DTTLPLTVNRFLRLRP-------GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHgRVEQVGSPQAVYDHP 228
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-215 |
3.81e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG-ARERQVG--FV 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENVAFGLrvkPRRERPSEaairaKVHELLSL--VQLDWLAQryPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL---PKRQASMQ-----KMKQLLAAlgCQLDLDSS--AGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-220 |
5.59e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.84 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAG-LEHADSGQVVLQGLDVASVGARERQVGFVFQHYALFrHMTVFEN 94
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 95 VAFGlrvkprRERPSEAAI-----RAKVHELLSLVQ--LDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:PRK11174 443 VLLG------NPDASDEQLqqaleNAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 168 DAKVRKELRGWLRRLHDDLhiSTIFVTHdQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-222 |
8.71e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.43 E-value: 8.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF--GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVA--SVGARERQVGF 78
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVAFGlrvkprrerpSEAAIRAKVHELLSLVQLDWLAQRYPS----------ELSGGQRQRIALA 148
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLLA----------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELrgwLRRLHDD-LHISTIFVTHdQEEALEVADRIVVLNHGRVEQVGSPQ 222
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQI---LELLAEHaQNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQ 558
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-210 |
2.17e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL-QGLDVAsvgarerqvgFVFQH-YalFRHMTVFENV 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------FLPQRpY--LPLGTLREAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFglrvkPRRERP-SEAAIRakvhELLSLVQLDWLAQRY------PSELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:COG4178 447 LY-----PATAEAfSDAELR----EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490296977 169 AKVRKELrgwLRRLHDDLHIST-IFVTHdQEEALEVADRIVVL 210
Cdd:COG4178 518 EENEAAL---YQLLREELPGTTvISVGH-RSTLAAFHDRVLEL 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-224 |
3.46e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD---SGQVVLQGLdvaSVGARERQV--GFVFQHYALFRHMTVF 92
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAisAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 93 ENVAFGLRVK-PRRERPSEAaiRAKVHELLSLVQLDWLAQ-------RYPSeLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:TIGR00955 118 EHLMFQAHLRmPRRVTKKEK--RERVDEVLQALGLRKCANtrigvpgRVKG-LSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 165 GALDAKVRKELRGWLRRLHDDLhiSTIFVTHDQ--EEALEVADRIVVLNHGRVEQVGSP-QAV 224
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKG--KTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPdQAV 255
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-213 |
3.55e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 94.30 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 7 NLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQ---VGFVFQHY 83
Cdd:PRK10762 9 GIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 84 ALFRHMTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK10762 89 NLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 164 FGAL-DA------KVRKELRgwlrrlhdDLHISTIFVTHDQEEALEVADRIVVLNHG 213
Cdd:PRK10762 169 TDALtDTeteslfRVIRELK--------SQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-215 |
4.53e-21 |
|
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: 89.51 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGleHAD----SGQVVLQGLDVASVGARERQ--- 75
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGEDITDLPPEERArlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 76 VGFVFQHYALFRhmtvfenvafGLRVKprrerpseaairakvhELLslvqldwlaqRYPSE-LSGGQRQRIALARALAVE 154
Cdd:cd03217 79 IFLAFQYPPEIP----------GVKNA----------------DFL----------RYVNEgFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 155 PKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEV-ADRIVVLNHGRV 215
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-228 |
5.21e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.00 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRF----GEF-----AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARE 73
Cdd:PRK15112 7 VRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 74 RQVGFVFQ--HYALFRHMTVFENVAFGLRVKPRRERPS-EAAIRAkvhellSLVQLDWL---AQRYPSELSGGQRQRIAL 147
Cdd:PRK15112 87 QRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQrEKQIIE------TLRQVGLLpdhASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
.
gi 490296977 228 P 228
Cdd:PRK15112 241 P 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-221 |
5.61e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 89.86 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF--GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVAfglrvkPRRERPSEAAIRA--KVHeLLSLVQ-----LDWLAQRYPSELSGGQRQRIALARAL 151
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLD------PFGEYSDEELWQAleRVG-LKEFVEslpggLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 152 AVEPKVLLLDEPFGALD----AKVRKELRGWLRrlhddlHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSP 221
Cdd:cd03244 155 LRKSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-245 |
5.65e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.01 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVAFGlRVKPRRERPSEAAIRAKVHE-LLSLvqldwlAQRYPSE-------LSGGQRQRIALARA 150
Cdd:PRK10789 394 VSQTPFLFSD-TVANNIALG-RPDATQQEIEHVARLASVHDdILRL------PQGYDTEvgergvmLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 151 LAVEPKVLLLDEPFGALDAK----VRKELRGWLRRlhddlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRtehqILHNLRQWGEG-------RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
250 260
....*....|....*....|..
gi 490296977 227 HP---RSAFVYEFLGAAnrLDG 245
Cdd:PRK10789 539 QSgwyRDMYRYQQLEAA--LDD 558
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-170 |
5.82e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 19 DDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYA-LFRHMTVFENVAF 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPgIKTELTALENLRF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 98 GLRVkprRERPSEAAIrakvHELLSLVQL----DWLAqrypSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:PRK13538 98 YQRL---HGPGDDEAL----WEALAQVGLagfeDVPV----RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-239 |
7.14e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 91.73 E-value: 7.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE----FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL----EHADSGQVVLQGLDVASVGARER 74
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 Q------VGFVFQH--YALFRHMTVFENVAFGLRV------KPRRERpseaAIrakvhELLSLVQLDWLAQR---YPSEL 137
Cdd:PRK11022 84 RnlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVhqggnkKTRRQR----AI-----DLLNQVGIPDPASRldvYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 138 SGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQ 217
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250 260
....*....|....*....|..
gi 490296977 218 VGSPQAVYDHPRSAFVYEFLGA 239
Cdd:PRK11022 235 TGKAHDIFRAPRHPYTQALLRA 256
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-213 |
1.04e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.93 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG---ARERQVGFV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMTVFENV---------AFGLRV---KPRRERPSEAAIRAKVHellslVQLDWLAqrypSELSGGQRQRIAL 147
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrhltkkVCGVNIidwREMRVRAAMMLLRVGLK-----VDLDEKV----ANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHG 213
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-239 |
5.00e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 19 DDVSLDFPAGELVALLGPSGCGKT-TLLRVIAGLE-------HAD---SGQVVLQGLDVASVGARERQVGFVFQH----- 82
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvvypSGDirfHGESLLHASEQTLRGVRGNKIAMIFQEpmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 -------------YALFRHMtvfenvafglrvkpRRErpseaAIRAKVHELLSLVQLDWLAQR---YPSELSGGQRQRIA 146
Cdd:PRK15134 106 nplhtlekqlyevLSLHRGM--------------RRE-----AARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
250
....*....|...
gi 490296977 227 HPRSAFVYEFLGA 239
Cdd:PRK15134 247 APTHPYTQKLLNS 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-235 |
7.56e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.30 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 21 VSLDFPAGELVALLGPSGCGKTTLLRVIAGLEhADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHMTVFENVAFG 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 99 LRVKPRrerpsEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARA-LAVEP------KVLLLDEPFGALDakV 171
Cdd:PRK03695 94 QPDKTR-----TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLD--V 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 172 RKElrGWLRRLHDDL---HISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAFVYE 235
Cdd:PRK03695 167 AQQ--AALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFG 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-237 |
8.92e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 90.78 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRF--GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvgarerQVGFVF 80
Cdd:TIGR00957 637 ITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHyALFRHMTVFENVAFGLRVKPRRerpseaaIRAKVHELLSLVQLDWLAQRYPSE-------LSGGQRQRIALARALAV 153
Cdd:TIGR00957 706 QQ-AWIQNDSLRENILFGKALNEKY-------YQQVLEACALLPDLEILPSGDRTEigekgvnLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 154 EPKVLLLDEPFGALDAKVRKEL-------RGWLRrlhddlHISTIFVTHDQeEALEVADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIfehvigpEGVLK------NKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
250
....*....|.
gi 490296977 227 hpRSAFVYEFL 237
Cdd:TIGR00957 851 --RDGAFAEFL 859
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-220 |
1.45e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.42 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAG-LEHADSGQVVLQGlDVASVgareRQVGFVFqhyalfrHMTVFENVA 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRG-SVAYV----PQVSWIF-------NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 97 FGLRVKPrrERPSEAA-IRAKVHELlslvqlDWLAQRYPSEL-------SGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PLN03232 701 FGSDFES--ERYWRAIdVTALQHDL------DLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 169 AKVRKELrgWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PLN03232 773 AHVAHQV--FDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-218 |
1.91e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 1 MGITVRNLHKRFgefaaLDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLE--HADSGQVVLQGLDvasvgarerqvgf 78
Cdd:COG2401 34 FGVELRVVERYV-----LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 vfqhyaLFRHMTVFENVafglrvkPRRERPSEAAirakvhELLSLVQLD--WLAQRYPSELSGGQRQRIALARALAVEPK 156
Cdd:COG2401 96 ------FGREASLIDAI-------GRKGDFKDAV------ELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQE--EALEvADRIVVLNHGRVEQV 218
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDviDDLQ-PDLLIFVGYGGVPEE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-214 |
1.16e-18 |
|
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: 86.91 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqGLDVasvgarerQVGFVFQ- 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVKP--RRERPSEAAIRAkvhelLSLVQLDwlAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:TIGR03719 394 RDALDPNKTVWEEISGGLDIIKlgKREIPSRAYVGR-----FNFKGSD--QQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 160 LDEPFGALDAKVrkelrgwLRRLhddlhistifvthdqEEALEV-ADRIVVLNHGR 214
Cdd:TIGR03719 467 LDEPTNDLDVET-------LRAL---------------EEALLNfAGCAVVISHDR 500
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-214 |
1.38e-18 |
|
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: 86.53 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvGARerqVGFVFQHYALFRHMTVFENVAF 97
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP------GIK---VGYLPQEPQLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GLRVK----------------PRRERPSEAAIRAKV---------HELLSLVQLDWLAQRYP------SELSGGQRQRIA 146
Cdd:TIGR03719 92 GVAEIkdaldrfneisakyaePDADFDKLAAEQAELqeiidaadaWDLDSQLEIAMDALRCPpwdadvTKLSGGERRRVA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAkvrkELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGR 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-213 |
1.58e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 83.15 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 15 FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQV-----VLQGLDVASVGARER-QVGFVFQHYALFrH 88
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRySVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 89 MTVFENVAFGLRV-KPRRERPSEAAIRAKVHELLSLVQLDWLAQRyPSELSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:cd03290 93 ATVEENITFGSPFnKQRYKAVTDACSLQPDIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 168 DAKVRKEL--RGWLRRLHDDLHiSTIFVTHdQEEALEVADRIVVLNHG 213
Cdd:cd03290 172 DIHLSDHLmqEGILKFLQDDKR-TLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-215 |
5.15e-18 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 81.15 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 10 KRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD---SGQVVLQGLDVASVGAR-ERQVGFVFQHYAL 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 86 FRHMTVFENVAFglrvkprrerpseaAIRAKVHELLSLVqldwlaqrypselSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:cd03233 95 FPTLTVRETLDF--------------ALRCKGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 166 ALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQ--EEALEVADRIVVLNHGRV 215
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLK-TTTFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-220 |
5.91e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 85.56 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 13 GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAG-LEHADSGQVVLQGlDVASVGarerQVGFVFqhyalfrHMTV 91
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG-TVAYVP----QVSWIF-------NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFGLRVKPRR-ERPSEAAIRAKVHELLSLVQLDWLAQRyPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:PLN03130 696 RDNILFGSPFDPERyERAIDVTALQHDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 171 V---------RKELRGWLRrlhddlhistIFVThDQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PLN03130 775 VgrqvfdkciKDELRGKTR----------VLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-210 |
6.42e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHkrfgefAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASvGARERQVGFVFQH 82
Cdd:PRK15056 14 VTWRNGH------TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVF-ENVA----FGLRVKPRRERPSEaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKV 157
Cdd:PRK15056 87 EEVDWSFPVLvEDVVmmgrYGHMGWLRRAKKRD---RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 158 LLLDEPFGALDAKVRKELRGWLRRLHDDLhiSTIFV-THDQEEALEVADRIVVL 210
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEG--KTMLVsTHNLGSVTEFCDYTVMV 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-215 |
9.00e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 84.23 E-value: 9.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGlDVasVGARERQvgfvfqh 82
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DL--IVARLQQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 yALFRHM--TVFENVAFGL-----------RVKPRRER-PSEAAIR--AKVHELLS--------------LVQLDWLAQR 132
Cdd:PRK11147 74 -DPPRNVegTVYDFVAEGIeeqaeylkryhDISHLVETdPSEKNLNelAKLQEQLDhhnlwqlenrinevLAQLGLDPDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 133 YPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAkvrkELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNH 212
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDR 228
|
...
gi 490296977 213 GRV 215
Cdd:PRK11147 229 GKL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-168 |
9.57e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.01 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqGLDVasvgarerQVGFVFQ- 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGL---RVKpRRERPSEAAIRA----------KVhellslvqldwlaqrypSELSGGQRQRIALA 148
Cdd:PRK11819 396 RDALDPNKTVWEEISGGLdiiKVG-NREIPSRAYVGRfnfkggdqqkKV-----------------GVLSGGERNRLHLA 457
|
170 180
....*....|....*....|
gi 490296977 149 RALAVEPKVLLLDEPFGALD 168
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-215 |
1.82e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHkrfGE-FAaldDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER-QVGFVF 80
Cdd:PRK15439 269 LTVEDLT---GEgFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 -----QHYALFRHMTVFENVA------FGLRVKPRRERpseaAIRAKVHELLS--LVQLDWLAQRypseLSGGQRQRIAL 147
Cdd:PRK15439 343 lpedrQSSGLYLDAPLAWNVCalthnrRGFWIKPAREN----AVLERYRRALNikFNHAEQAART----LSGGNQQKVLI 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-212 |
2.13e-17 |
|
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: 78.35 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqgldvasvgARERQVGFVFQH-YalfrhmtvfenVA 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQRpY-----------LP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 97 FG-LRvkprrerpseaairakvhELLSlvqldwlaqrYP--SELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVrk 173
Cdd:cd03223 77 LGtLR------------------EQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES-- 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 490296977 174 ELRgwLRRLHDDLHISTIFVTHdQEEALEVADRIVVLNH 212
Cdd:cd03223 127 EDR--LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-168 |
2.54e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.22 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV-ASVGARERQVGFVFQ 81
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENVAFGLRVkprrerpSEAAIraKVHELLSLVQLDWLAQrYPSE-LSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHF-------SPGAV--GITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLL 151
|
....*...
gi 490296977 161 DEPFGALD 168
Cdd:PRK13540 152 DEPLVALD 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-224 |
2.97e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.64 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 16 AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD--------SGQVVLQGLDVASVG----ARERQV------- 76
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprlARLRAVlpqaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 77 GFVFqhyalfrhmTVFENVAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALA---- 152
Cdd:PRK13547 95 AFAF---------SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 153 -----VEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-168 |
2.98e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.51 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 23 LDF--PAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGlDVASVGARERQVGFVFQHYALFRHMTVFENVAF--G 98
Cdd:PRK13543 30 LDFhvDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-KTATRGDRSRFMAYLGHLPGLKADLSTLENLHFlcG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 99 LRVKPRRERPSEAairakvhelLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK13543 109 LHGRRAKQMPGSA---------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-169 |
3.84e-17 |
|
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: 78.69 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV-GARERQVGFVFQHY 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 84 ALFRHMTVFENVAFGLRVKPrrerpseaaiRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHS----------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
....*.
gi 490296977 164 FGALDA 169
Cdd:cd03231 153 TTALDK 158
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-212 |
3.90e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.77 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 55 DSGQVVLQGLDVASVGARERQVGF--VFQHYALFrHMTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLV--QLDWLA 130
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFsiVSQEPMLF-NMSIYENIKFG-KEDATREDVKRACKFAAIDEFIESLpnKYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 131 QRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHdQEEALEVADRIVVL 210
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVF 1431
|
..
gi 490296977 211 NH 212
Cdd:PTZ00265 1432 NN 1433
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-218 |
7.12e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRfgEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV-------------ASVGA 71
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgmAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 72 RERQVGFvFQHYALFRHMTVFENV-------AFGLrVKPRRERPSEAAIRakvhELLSLvQLDWLAQRYpSELSGGQRQR 144
Cdd:PRK09700 346 SRRDNGF-FPNFSIAQNMAISRSLkdggykgAMGL-FHEVDEQRTAENQR----ELLAL-KCHSVNQNI-TELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVEQV 218
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-223 |
7.73e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-RQ-VGFVFQHYALFRHmTVFENV 95
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQgVAMVQQDPVVLAD-TFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGLRVkprrerpSEaairAKVHELLSLVQLDWLAQRYP-----------SELSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK10790 436 TLGRDI-------SE----EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 165 GALDAKVRKELRGWLRRLHDdlHISTIFVTHDQEEALEvADRIVVLNHGRVEQVGSPQA 223
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQ 560
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-214 |
2.28e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.83 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADS--GQVVLQGLDVASVGARE-RQVGFVF-- 80
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDsEALGIVIih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGlrvkprRERPS-------EAAIRAKvhELLSLVQLDWLAQRYPSELSGGQRQRIALARALAV 153
Cdd:NF040905 85 QELALIPYLSIAENIFLG------NERAKrgvidwnETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-214 |
2.48e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.77 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 6 RNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV---ASVGARERQVGFVFQH 82
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFGlRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK10982 82 LNLVLQRSVMDNMWLG-RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGR 214
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-209 |
9.94e-16 |
|
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: 75.52 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 10 KRFGEFAaLDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVvlqGLDVASVGARERQVGFVFQhyalfrhM 89
Cdd:cd03237 8 KTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYE-------G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TVfenvafglrvkprRERPSEAAIRAKVH-----ELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:cd03237 77 TV-------------RDLLSSITKDFYTHpyfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490296977 165 GALDAKVRKELRGWLRRLHDDlHISTIFVT-HDQEEALEVADRIVV 209
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAEN-NEKTAFVVeHDIIMIDYLADRLIV 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-221 |
1.15e-15 |
|
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: 74.76 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEF--AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGF 78
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFRHmTVFENVafglrvkPRRERPSEAAIRA--KVHEllslvqldwlaqrYPSELSGGQRQRIALARALAVEPK 156
Cdd:cd03369 87 IPQDPTLFSG-TIRSNL-------DPFDEYSDEEIYGalRVSE-------------GGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSP 221
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTN---STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-231 |
1.47e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.51 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 19 DDVSLDFPAGELVALLGPSGCGKT----TLLRVI-AGLEHAdSGQVVLQGLDVASVGARERQVGFVFQH----YALFRHM 89
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPCALRGRKIATIMQNprsaFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TvfenvAFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:PRK10418 99 H-----THARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 170 KVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSA 231
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
1.72e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARER-QVGFVF-----QHYALFRHMTV 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVA---------FGLRVKPRRERpseaairAKVHELLSLVQLdwlaqRYPS------ELSGGQRQRIALARALAVEPK 156
Cdd:PRK10762 348 KENMSltalryfsrAGGSLKHADEQ-------QAVSDFIRLFNI-----KTPSmeqaigLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 157 VLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-169 |
3.89e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 28 GELVALLGPSGCGKTTLLRVIAGLEHADS--GQVVLQGLDVASvgARERQVGFVFQHYALFRHMTVFENVAFG--LRVKP 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 104 RRERPSEAAIRAKVHELLSLVQLD--WLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCEntIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-196 |
5.24e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvGARerqVGFVFQHYALFRHMTVFENVAF 97
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP------GIK---VGYLPQEPQLDPEKTVRENVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GLR-VKPRRERPSE---------------AAIRAKV---------HELLSLVQLDWLAQRYP------SELSGGQRQRIA 146
Cdd:PRK11819 94 GVAeVKAALDRFNEiyaayaepdadfdalAAEQGELqeiidaadaWDLDSQLEIAMDALRCPpwdakvTKLSGGERRRVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAkvrkELRGWLRRLHDDLHISTIFVTHD 196
Cdd:PRK11819 174 LCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
6.82e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 21 VSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG--LDVASVGARERQvGFVF-----QHYALFRHMTVFE 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRA-GIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 94 NVAFGLRvkpRRERPSEAAIRAKVHELLSLVQLDWLAQRYPS------ELSGGQRQRIALARALAVEPKVLLLDEPFGAL 167
Cdd:PRK11288 351 NINISAR---RHHLRAGCLINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 168 DAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-213 |
8.64e-15 |
|
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: 71.89 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD--SGQVVLQGLDVASvgARERQVGFVFQHYALFRHMTVFENV 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK--NFQRSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFglrvkprrerpsEAAIRAkvhellslvqldwlaqrypseLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKEL 175
Cdd:cd03232 101 RF------------SALLRG---------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490296977 176 RGWLRRLHDdlHISTIFVTHDQEEA--LEVADRIVVLNHG 213
Cdd:cd03232 148 VRFLKKLAD--SGQAILCTIHQPSAsiFEKFDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-220 |
9.75e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVlqgldvasvgaRERQVGFVFQHyALFRHMTVFENVAF 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GlrvkpRRERPSEAAIRAKVHELLSLVQLdwLAQRYPSE-------LSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:PTZ00243 744 F-----DEEDAARLADAVRVSQLEADLAQ--LGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490296977 171 V---------RKELRGWLRRLhddlhistifVTHdQEEALEVADRIVVLNHGRVEQVGS 220
Cdd:PTZ00243 817 VgervveecfLGALAGKTRVL----------ATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-215 |
1.48e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.62 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 2 GITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCgkttllrviAGLEHADSGQVVlqGLDVasvGARE-RQVGFVF 80
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAHV*--GPDA---GRRPwRF*TWCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENVAFGLR----------VKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARA 150
Cdd:NF000106 79 NRRALRRTIG*HRPVR*GRResfsgrenlyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 151 LAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-209 |
1.68e-14 |
|
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: 74.44 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 7 NLHKRFGEFaalddvSLDFPAGEL-----VALLGPSGCGKTTLLRVIAGLEHADSGQVVLQgLDVAsvgarerqvgFVFQ 81
Cdd:COG1245 346 DLTKSYGGF------SLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS----------YKPQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENvafgLRvkprrerpseAAIRAKV------HELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:COG1245 409 YISPDYDGTVEEF----LR----------SANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVV 209
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-214 |
1.99e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.76 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 14 EFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEH----ADSGQVVLQGLDVASVGARER-QVGFVFQHYALFRH 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 89 MTVFENVAFGLRVKPRRERP---SEAAIRAKVHEL------LSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLL 159
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPdgvSREEYAKHIADVymatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 160 LDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQ--EEALEVADRIVVLNHGR 214
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILD-TTPLVAIYQcsQDAYELFDKVIVLYEGY 288
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-213 |
2.87e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 72.20 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvgarerQVGFVFQhYALFRHMTVFENVAF 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQ-FSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GLRVKPRRERpseAAIRAkvhellslVQLDWLAQRYPSE-----------LSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:cd03291 121 GVSYDEYRYK---SVVKA--------CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 167 LDAKVRKEL-RGWLRRLHDDLhiSTIFVTHDQEEaLEVADRIVVLNHG 213
Cdd:cd03291 190 LDVFTEKEIfESCVCKLMANK--TRILVTSKMEH-LKKADKILILHEG 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-228 |
2.91e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 13 GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLE------HADsgQVVLQGLDVASVGARERQ------VGFVF 80
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwhvTAD--RFRWNGIDLLKLSPRERRkiigreIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QH--YALFRHMTVFENVAFGLrvkPRRE-------RPSEAAIRAKvhELLSLVQL---DWLAQRYPSELSGGQRQRIALA 148
Cdd:COG4170 96 QEpsSCLDPSAKIGDQLIEAI---PSWTfkgkwwqRFKWRKKRAI--ELLHRVGIkdhKDIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 149 RALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHP 228
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-208 |
3.64e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.39 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqgldvasvgARERQVGFVFQ- 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALF-RHMTVFENVAfglrvKPRRERPSEAAIRAKVHELLsLVQLDwlAQRYPSELSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK15064 391 HAYDFeNDLTLFDWMS-----QWRQEGDDEQAVRGTLGRLL-FSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLhistIFVTHDQEEALEVADRIV 208
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKYEGTL----IFVSHDREFVSSLATRII 506
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-213 |
2.60e-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: 71.09 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGldvasvgarerQVGFVFQhYALFRHMTVFENVAF 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQ-TSWIMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GLRVKPRRERpseAAIRAkvhellslVQLDWLAQRYPSE-----------LSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:TIGR01271 510 GLSYDEYRYT---SVIKA--------CQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490296977 167 LDAKVRKELrgWLRRLHDDLHISTIFVTHDQEEALEVADRIVVLNHG 213
Cdd:TIGR01271 579 LDVVTEKEI--FESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-213 |
6.82e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAglEHADSGqVVLQGLDVASVGAR----ERQVGFVFQHYALFRHMTVFE 93
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPLdssfQRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 94 NVAFGLRVKprreRPSEAAIRAK---VHELLSLVQLDWLAQRY---PSE-LSGGQRQRIALARALAVEPKVLL-LDEPFG 165
Cdd:TIGR00956 856 SLRFSAYLR----QPKSVSKSEKmeyVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490296977 166 ALDAKVRKELRGWLRRLHDdlHISTIFVTHDQEEA--LEVADRIVVLNHG 213
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLAD--HGQAILCTIHQPSAilFEEFDRLLLLQKG 979
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
19-216 |
1.17e-12 |
|
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: 66.09 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 19 DDVSLDFPAGeLVALLGPSGCGKTTLLRVI-AGL--EHADSGQVVLQGLDVASVGARERQVGFVFQH-----YALFRHMT 90
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEALkYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 91 VFENVAFglrvkprrerpseaairakVHEllslVQLDWLAQRYPSELSGGQRQ------RIALARALAVEPKVLLLDEPF 164
Cdd:cd03240 93 ILENVIF-------------------CHQ----GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490296977 165 GALDA-KVRKELRGWLRRLHDDLHISTIFVTHDqEEALEVADRIVvlnhgRVE 216
Cdd:cd03240 150 TNLDEeNIEESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY-----RVE 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-209 |
1.71e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 7 NLHKRFGEFaalddvSLDFPAGEL-----VALLGPSGCGKTTLLRVIAGLEHADSGQVVLQgLDVAsvgarerqvgFVFQ 81
Cdd:PRK13409 345 DLTKKLGDF------SLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS----------YKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 HYALFRHMTVFENvafgLRvkprrerpseaAIRAKV------HELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEP 155
Cdd:PRK13409 408 YIKPDYDGTVEDL----LR-----------SITDDLgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHD---QEealEVADRIVV 209
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDiymID---YISDRLMV 526
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-223 |
2.33e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 67.90 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 21 VSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVG-ARERQVgF--VFQHYALFRHMtvfenvaF 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNrEAYRQL-FsaVFSDFHLFDRL-------L 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GLRvkprrerpsEAAIRAKVHELLSLVQLD---WLAQRYPS--ELSGGQRQRIALARALAVEPKVLLLDE-------PFg 165
Cdd:COG4615 423 GLD---------GEADPARARELLERLELDhkvSVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEwaadqdpEF- 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 166 aldakvRK----ELRGWLRRlhddLHISTIFVTHDqEEALEVADRIVVLNHGRVEQVGSPQA 223
Cdd:COG4615 493 ------RRvfytELLPELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAA 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-221 |
2.81e-12 |
|
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: 68.05 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFrhmtvfeNV 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF-------SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGLRVKPRRERPSE----AAIRAKVHELLSLV--QLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEevwwALELAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 170 KVRKELRGWLRRLHDDLHISTIfvTHDQEEALEVAdRIVVLNHGRVEQVGSP 221
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTI--AHRLNTIMDYT-RVIVLDKGEVAEFGAP 1503
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-228 |
4.36e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.36 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRF----GEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEH------ADsgQVVLQGLDVASVGARER 74
Cdd:PRK15093 6 IRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtAD--RMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 75 Q------VGFVFQHYAlfRHMTVFENVAFGL---------------RVKPRRERpseaAIrakvhELLSLVQL---DWLA 130
Cdd:PRK15093 84 RklvghnVSMIFQEPQ--SCLDPSERVGRQLmqnipgwtykgrwwqRFGWRKRR----AI-----ELLHRVGIkdhKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 131 QRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVL 210
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260
....*....|....*....|.
gi 490296977 211 NHGR-VEQVGSPQAVY--DHP 228
Cdd:PRK15093 233 YCGQtVETAPSKELVTtpHHP 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-232 |
1.15e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 29 ELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHMTVFEnvafglrVKPRRE 106
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGTVRFN-------IDPFSE 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 107 RPS----EAAIRAKVHELLSLVQLDWLAQRYP--SELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRgwlR 180
Cdd:PLN03232 1336 HNDadlwEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ---R 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490296977 181 RLHDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAF 232
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-212 |
1.34e-11 |
|
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: 62.01 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 28 GELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFqhyalfrhmtvfenvafglrvkprrer 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 108 pseaairakvhellslvqldwlaQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELR-----GWLRRL 182
Cdd:smart00382 55 -----------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLL 111
|
170 180 190
....*....|....*....|....*....|
gi 490296977 183 HDDLHISTIFVTHDQEEALEVADRIVVLNH 212
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-224 |
5.52e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.18 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE--FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADsGQVVLQGLDVASVGARE--RQVGF 78
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKwrKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFrhmtvfeNVAFGLRVKPRRERPSEAAIRAKVHELLSLV------QLDWLAQRYPSELSGGQRQRIALARALA 152
Cdd:cd03289 82 IPQKVFIF-------SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490296977 153 VEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAV 224
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD---CTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-232 |
5.67e-11 |
|
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: 64.26 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDV-ASVGARERQVGFVFQHYALFRHMTVFENV 95
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGLRVkprRERPSEAAIRAKVHELLSLvQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKEL 175
Cdd:TIGR01257 2034 YLYARL---RGVPAEEIEKVANWSIQSL-GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 176 RGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQavydHPRSAF 232
Cdd:TIGR01257 2110 WNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ----HLKSKF 2161
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-175 |
5.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.04 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVgaRERQVGFVFQHYALFRHMTVFENVAF 97
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 98 GLRVkprreRPSEAAIRAKVHELlslvQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKEL 175
Cdd:PRK13541 94 WSEI-----YNSAETLYAAIHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-198 |
5.90e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 5 VRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQV-VLQGLDVAsvgarerqvgfVFQHY 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhCGTKLEVA-----------YFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 84 --ALFRHMTVFENVAFGlrvkprrerPSEAAIRAKVHELLSLVQlDWL----AQRYP-SELSGGQRQRIALARALAVEPK 156
Cdd:PRK11147 391 raELDPEKTVMDNLAEG---------KQEVMVNGRPRHVLGYLQ-DFLfhpkRAMTPvKALSGGERNRLLLARLFLKPSN 460
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490296977 157 VLLLDEPFGALDAKVRkELrgwLRRLHDDLHISTIFVTHDQE 198
Cdd:PRK11147 461 LLILDEPTNDLDVETL-EL---LEELLDSYQGTVLLVSHDRQ 498
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-214 |
7.32e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFA-ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGF--V 79
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFsaV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 80 FQHYALFRHMtvfenvafglrVKPRRERPSEAAI-----RAKVHELLSLVQLDWLAQRypseLSGGQRQRIALARALAVE 154
Cdd:PRK10522 403 FTDFHLFDQL-----------LGPEGKPANPALVekwleRLKMAHKLELEDGRISNLK----LSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 155 PKVLLLDEPFGALDAKVRK----ELRGWLRRLHddlhiSTIF-VTHDqEEALEVADRIVVLNHGR 214
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRRefyqVLLPLLQEMG-----KTIFaISHD-DHYFIHADRLLEMRNGQ 526
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-219 |
9.50e-11 |
|
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: 60.03 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLlrviaglehadsgqvVLQGLDVAsvgARERQVGFVfqhYALFRHMTVFenva 96
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEGLYAS---GKARLISFL---PKFSRNKLIF---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 97 fglrvkprrerpseaairakVHELLSLVQ--LDWLA-QRYPSELSGGQRQRIALARALAVEPK--VLLLDEPFGALDAKV 171
Cdd:cd03238 65 --------------------IDQLQFLIDvgLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 172 RKELRGWLRRLHDDLHiSTIFVTHDqEEALEVADRIVVLNHGRVEQVG 219
Cdd:cd03238 125 INQLLEVIKGLIDLGN-TVILIEHN-LDVLSSADWIIDFGPGSGKSGG 170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
86-230 |
1.75e-10 |
|
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: 62.34 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 86 FRHMTVFENVAF--GLRVKPRRERPSEAAIRAKVHELLSL--VQLDWLA-QRYPSELSGGQRQRIALARALAVE-PKVL- 158
Cdd:TIGR00630 433 VSELSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLGFLidVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGlTGVLy 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 159 LLDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDqEEALEVADRIVVL-----NH-GRVEQVGSPQAVYDHPRS 230
Cdd:TIGR00630 513 VLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVEHD-EDTIRAADYVIDIgpgagEHgGEVVASGTPEEILANPDS 588
|
|
| TOBE_3 |
pfam12857 |
TOBE-like domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
287-343 |
3.08e-10 |
|
TOBE-like 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 sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 432835 Cd Length: 59 Bit Score: 55.33 E-value: 3.08e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 287 ARAQGIAADVRRVVPLGGSVRVELAAR-SGEVLEAELDRNAWRALALDVGDALTAVPR 343
Cdd:pfam12857 2 PAGGGIPATVRRIRRVGPIVRLELERLdTGELIEIELPRDRFRELGLAEGETVRLRPR 59
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-220 |
3.15e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGleHAD----SGQVVLQGLDVASVGARER-QVG 77
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERaHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 --FVFQhYALfrHMTVFENVAFgLRVKPRRERPSEAAIRAK-------VHELLSLVQLD--WLaQRYPSE-LSGGQRQRI 145
Cdd:CHL00131 86 ifLAFQ-YPI--EIPGVSNADF-LRLAYNSKRKFQGLPELDplefleiINEKLKLVGMDpsFL-SRNVNEgFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQeEALE--VADRIVVLNHGRVEQVGS 220
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQ-RLLDyiKPDYVHVMQNGKIIKTGD 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-195 |
6.83e-10 |
|
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: 60.53 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 20 DVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqgldvasvgARERQVGFVFQHyALFRHMTVFENVAFGL 99
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR-PYMTLGTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 100 RVKPRRERpseaAIRAKVHE-LLSLVQLDWLAQR---------YPSELSGGQRQRIALARALAVEPKVLLLDEPFGAlda 169
Cdd:TIGR00954 540 SSEDMKRR----GLSDKDLEqILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA--- 612
|
170 180
....*....|....*....|....*.
gi 490296977 170 kVRKELRGWLRRLHDDLHISTIFVTH 195
Cdd:TIGR00954 613 -VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-243 |
7.04e-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: 60.69 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGE--FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADsGQVVLQGLDVASVGARE--RQVGF 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwrKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 79 VFQHYALFrhmtvfeNVAFGLRVKPrRERPSEAAIRAKVHEllslVQLDWLAQRYPSE-----------LSGGQRQRIAL 147
Cdd:TIGR01271 1297 IPQKVFIF-------SGTFRKNLDP-YEQWSDEEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 148 ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDlhiSTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDH 227
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN---CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
250
....*....|....*.
gi 490296977 228 pRSAFvYEFLGAANRL 243
Cdd:TIGR01271 1442 -TSLF-KQAMSAADRL 1455
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-216 |
7.82e-10 |
|
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: 59.84 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGL-EHADSGQVVLQGLDVA---SVGARERQVGFV---FQHYALFRHMT 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDirnPAQAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 91 VFENVAFG-LRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRYP-SELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:TIGR02633 356 VGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 169 AKVRKELRGWLRRLHDDlHISTIFVTHDQEEALEVADRIVVLNHGRVE 216
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-241 |
8.63e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHmtvfeNV 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFSG-----TV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 AFGLrvKPRRERPS----EAAIRAKVHELL--SLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGAL-- 167
Cdd:PLN03130 1330 RFNL--DPFNEHNDadlwESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdv 1407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490296977 168 --DAKVRKELRgwlrrlhDDLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRSAF--VYEFLGAAN 241
Cdd:PLN03130 1408 rtDALIQKTIR-------EEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFskMVQSTGAAN 1478
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-212 |
8.75e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 20 DVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVL---QGLDVASVGARERQVGFVFQHYALFRHmTVFENVA 96
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 97 FGLRVKPRRERPSE----------------AAIRAK----------------------------------------VHEL 120
Cdd:PTZ00265 482 YSLYSLKDLEALSNyynedgndsqenknkrNSCRAKcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 121 LSLV--QLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHdQE 198
Cdd:PTZ00265 562 VSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-RL 640
|
250
....*....|....
gi 490296977 199 EALEVADRIVVLNH 212
Cdd:PTZ00265 641 STIRYANTIFVLSN 654
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-219 |
2.45e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLE--HADSGQVVLQGLDVASVGARERQVGFVF 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 81 QHYALFRHMTVFENvAFGLR-----VKPRRERPS------EAAIRAKVhELLSLVQlDWLAQRYPSELSGGQRQRIALAR 149
Cdd:PRK09580 82 MAFQYPVEIPGVSN-QFFLQtalnaVRSYRGQEPldrfdfQDLMEEKI-ALLKMPE-DLLTRSVNVGFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVA-DRIVVLNHGRVEQVG 219
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-208 |
2.89e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG-------------LDVASV 69
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpaLPQPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 70 -----GARErqvgfvfqhyalFRHMTVFENVAfglrvkprRERPSEAAIrAKVHELLSLVQ-----------LDWLA--- 130
Cdd:PRK10636 82 eyvidGDRE------------YRQLEAQLHDA--------NERNDGHAI-ATIHGKLDAIDawtirsraaslLHGLGfsn 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 131 ---QRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLhistIFVTHDQEEALEVADRI 207
Cdd:PRK10636 141 eqlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVDKI 216
|
.
gi 490296977 208 V 208
Cdd:PRK10636 217 I 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
3-210 |
3.82e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.27 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSlDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVAsvgarerqvgfvfqh 82
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 yalfrhmtvfenvafglrVKPRRerpseaairakvhellslvqldwlaqrypSELSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03222 65 ------------------YKPQY-----------------------------IDLSGGELQRVAIAAALLRNATFYLFDE 97
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490296977 163 PFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEALEVADRIVVL 210
Cdd:cd03222 98 PSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-170 |
9.35e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEhadSGQVVlQGlDVASVGARERQ------VGFVFQHYALFRHMTV 91
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK---TGGYI-EG-DIRISGFPKKQetfariSGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFGLRVKPRRERPSEAAIRAkVHELLSLVQLDWLAQR---YP--SELSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:PLN03140 971 RESLIYSAFLRLPKEVSKEEKMMF-VDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
....
gi 490296977 167 LDAK 170
Cdd:PLN03140 1050 LDAR 1053
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-200 |
1.03e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGlEH--ADSGQVVLQGLDVAS---VGARERQVG 77
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHpqGYSNDLTLFGRRRGSgetIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYAL-FRHMTVFENV-------AFGL-RVKPRRERpseaairAKVHELLSLVQLD-WLAQRYPSELSGGQrQRIAL 147
Cdd:PRK10938 340 YVSSSLHLdYRVSTSVRNVilsgffdSIGIyQAVSDRQQ-------KLAQQWLDILGIDkRTADAPFHSLSWGQ-QRLAL 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490296977 148 -ARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIFVTHDQEEA 200
Cdd:PRK10938 412 iVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-215 |
2.25e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 17 ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE-------------RQVGFvfqhY 83
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalvteerRSTGI----Y 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 84 A--------LFRHMTVFENvAFGLRVKPRRERPSEAAIrakvhellslvqlDWLAQRYPSE------LSGGQRQRIALAR 149
Cdd:PRK10982 339 AyldigfnsLISNIRNYKN-KVGLLDNSRMKSDTQWVI-------------DSMRVKTPGHrtqigsLSGGNQQKVIIGR 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 150 ALAVEPKVLLLDEPFGALDAKVRKELRGWLRRL-HDDLHIstIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-196 |
2.55e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.48 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNlhkrFGEFAalDDVSLDFPAGeLVALLGPSGCGKTTLLRVIA-GLEHADSGQVVLQGlDVASVGARERQVGFVFQ 81
Cdd:COG0419 5 LRLEN----FRSYR--DTETIDFDDG-LNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRS-DLINVGSEEASVELEFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 82 H----YALFRH---------------MTVFENVaFGLRVKPRRERPSEAAIRAKVHELLSLVQLDWLAQRY--------- 133
Cdd:COG0419 77 HggkrYRIERRqgefaefleakpserKEALKRL-LGLEIYEELKERLKELEEALESALEELAELQKLKQEIlaqlsgldp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 134 PSELSGGQRQRIALARALAvepkvLLLDepFGALDAKVRKELRGWLRRLHddlhistiFVTHD 196
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-196 |
2.87e-08 |
|
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: 55.18 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 28 GELVALLGPSGCGKTTLLRVIAGLEhadsgqvvlqgldVASVGARERQVGF--VFQHYA---LFRHmtvFENVAFG-LRV 101
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGEL-------------KPNLGDYDEEPSWdeVLKRFRgteLQDY---FKKLANGeIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 102 --KPR-------------RERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:COG1245 163 ahKPQyvdlipkvfkgtvRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190
....*....|....*....|....*....|
gi 490296977 167 LDAKVRKELRGWLRRLHDDlHISTIFVTHD 196
Cdd:COG1245 243 LDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-215 |
5.92e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 19 DDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEH-ADSGQVVLQGLDV---ASVGARERQVGFVFQ---HYALFRHMTV 91
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVkirNPQQAIAQGIAMVPEdrkRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 92 FENVAFG-LRVKPRRERPSEAAirakvhELLSLVQ-LDWLAQRYPS------ELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK13549 359 GKNITLAaLDRFTGGSRIDDAA------ELKTILEsIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490296977 164 FGALDAKVRKElrgwLRRLHDDL---HISTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PRK13549 433 TRGIDVGAKYE----IYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-232 |
8.07e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARE--RQVGFVFQHYALFRHmTVFENV 95
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 96 afglrvkprreRPSEAAIRAKVHELLSLVQLdwlAQRYPSELSG--------------GQRQRIALARALAVE-PKVLLL 160
Cdd:PTZ00243 1405 -----------DPFLEASSAEVWAALELVGL---RERVASESEGidsrvleggsnysvGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490296977 161 DEPFGALDAKVRKELRGWLRRLHDDLHISTIfvTHDQEEaleVA--DRIVVLNHGRVEQVGSPQAVYDHPRSAF 232
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAYTVITI--AHRLHT---VAqyDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-196 |
1.02e-07 |
|
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: 52.37 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 28 GELVALLGPSGCGKTTLLRVIAG--------LEHADSGQVVLQGldvasvgarerqvgfvFQHYALFRHMTVFENVAFGL 99
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDE----------------FRGSELQNYFTKLLEGDVKV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 100 RVKPRRERPSEAAIRAKVHELLS----------LVQ---LDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:cd03236 90 IVKPQYVDLIPKAVKGKVGELLKkkdergkldeLVDqleLRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|
gi 490296977 167 LDAKVRKELRGWLRRLHDDLHiSTIFVTHD 196
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDN-YVLVVEHD 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-196 |
3.17e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 28 GELVALLGPSGCGKTTLLRVIAG--------LEHADSGQVVLqgldvasvgarERQVGFVFQHYalfrhmtvFENVAFG- 98
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVL-----------KRFRGTELQNY--------FKKLYNGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 99 LRV--KPR-------------RERPSEAAIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK13409 160 IKVvhKPQyvdlipkvfkgkvRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 490296977 164 FGALDAKVRKELRGWLRRLHDDlhISTIFVTHD 196
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEG--KYVLVVEHD 270
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-168 |
3.37e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqgldvaSVGARerqVGFVFQH 82
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL------DPNER---LGKLRQD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 83 YALFRHMTVFENVAFG----LRVKPRRER----P--SE--------------------AAIRAKvhELLSLVQLDwLAQR 132
Cdd:PRK15064 73 QFAFEEFTVLDTVIMGhtelWEVKQERDRiyalPemSEedgmkvadlevkfaemdgytAEARAG--ELLLGVGIP-EEQH 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 490296977 133 YP--SELSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK15064 150 YGlmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-216 |
5.90e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 12 FGEFAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLqgldvasvgARERQVGFVFQHYALF----- 86
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFAQHQLEFlrade 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 87 ---RHMTvfenvafglRVKPRRerpSEAAIRA----------KVHELlslvqldwlAQRYpselSGGQRQRIALARALAV 153
Cdd:PRK10636 393 splQHLA---------RLAPQE---LEQKLRDylggfgfqgdKVTEE---------TRRF----SGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490296977 154 EPKVLLLDEPFGALDAKVRKELRGWLRrlhdDLHISTIFVTHDQEEALEVADRIVVLNHGRVE 216
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-236 |
1.36e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 15 FAALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVvlqgldvasvgARERQVGFVFQHYALFRHMTVFEN 94
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 95 VAFGLRVK--PRRErpseaaIRAKVHELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVR 172
Cdd:PRK13546 106 IEFKMLCMgfKRKE------IKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 173 KELrgwLRRLHD--DLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHpRSAFVYEF 236
Cdd:PRK13546 180 QKC---LDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDF 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-215 |
1.49e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 20 DVSLDFPAGEL--------------VALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASVGARERQVGFVFQHYAL 85
Cdd:PLN03073 513 DASFGYPGGPLlfknlnfgidldsrIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 86 FRHMTVFENVAfglrvkprrerpsEAAIRAkvhELLSLVQLDWLAQRYPSELSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:PLN03073 593 LYMMRCFPGVP-------------EQKLRA---HLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490296977 166 ALDAKVRKELRGWLRRLHDDLhistIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:PLN03073 657 HLDLDAVEALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-208 |
1.60e-06 |
|
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: 47.35 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAglehadsgqvvlqgldvasvgarerqvgfvfqhYALFRHMTVfenvaf 97
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSA------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 98 GLRVKPRRERPSEAAIRAkvHELLSLVQLdwlaqrypselSGGQRQRIALARALA---VEPKVL-LLDEPFGALDAKVRK 173
Cdd:cd03227 52 TRRRSGVKAGCIVAAVSA--ELIFTRLQL-----------SGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 490296977 174 ELRGWLRRLHDdlHIST-IFVTHDqEEALEVADRIV 208
Cdd:cd03227 119 ALAEAILEHLV--KGAQvIVITHL-PELAELADKLI 151
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
13-243 |
1.79e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 13 GEFA-ALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQG-LDVASVGArerqvgfvfqhyALFRHMT 90
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsAALIAISS------------GLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 91 VFENVAF-GLRVKPRRERPSEaaIRAKVHELLSLVQldWLAQRYPSeLSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:PRK13545 102 GIENIELkGLMMGLTKEKIKE--IIPEIIEFADIGK--FIYQPVKT-YSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490296977 170 KVRKELrgwLRRLHD--DLHISTIFVTHDQEEALEVADRIVVLNHGRVEQVGSPQAVYDHPRsafvyEFLGAANRL 243
Cdd:PRK13545 177 TFTKKC---LDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-----EFLKKYNQM 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
138-168 |
2.61e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.61e-06
10 20 30
....*....|....*....|....*....|.
gi 490296977 138 SGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-208 |
3.27e-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: 47.64 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTL----------LRVIAG--------LEHADSGQV-VLQGLDVA------SVGAR 72
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESlsayarqfLGQMDKPDVdSIEGLSPAiaidqkTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 73 ERQ-VGFVFQHYALFRhmtvfenVAFglrvkprrerpSEAAIRAKVHELLSlVQLDWLA-QRYPSELSGGQRQRIALARA 150
Cdd:cd03270 91 PRStVGTVTEIYDYLR-------LLF-----------ARVGIRERLGFLVD-VGLGYLTlSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 151 LAVEPKVLL--LDEPFGALDAKVRKELRGWLRRLHdDLHISTIFVTHDqEEALEVADRIV 208
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHD-EDTIRAADHVI 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-215 |
1.75e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHAD--SGQVVLQG--LDVASVG-ARERQVGFVFQ---HYALFRHM 89
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGkeVDVSTVSdAIDAGLAYVTEdrkGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 90 TVFEN--------VAFGLRVKPRRERPSEAAIRAKvhellslvqldwLAQRYPS------ELSGGQRQRIALARALAVEP 155
Cdd:NF040905 356 DIKRNitlanlgkVSRRGVIDENEEIKVAEEYRKK------------MNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 156 KVLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQEEALEVADRIVVLNHGRV 215
Cdd:NF040905 424 DVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-183 |
5.47e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 5.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490296977 137 LSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLH 183
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-218 |
1.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 137 LSGGQRQ------RIALARALAVEPKVLLLDEPFGALDAKVRKEL----RGWLRRlhddlhIS-TIFVTHDqEEALEVAD 205
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRK------IPqVIIVSHD-EELKDAAD 861
|
90
....*....|....*..
gi 490296977 206 RI--VVLNHG--RVEQV 218
Cdd:PRK03918 862 YVirVSLEGGvsKVEVV 878
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-232 |
1.20e-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: 42.97 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 3 ITVRNLHKRFGEF--AALDDVSLDFPAGELVALLGPSGCGKTTLLRVIAGLEHADSGQVVLQGLDVASV---GARERqVG 77
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 78 FVFQHYALFRHmtvfeNVAFGLRvkprrerPSEAAIRAKVHELLSLVQLDWLAQRYPSEL-----------SGGQRQRIA 146
Cdd:cd03288 99 IILQDPILFSG-----SIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 147 LARALAVEPKVLLLDEPFGALDAKVRKELRGWLRRLHDDLHISTIfvTHDQEEALEvADRIVVLNHGRVEQVGSPQAVYD 226
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI--AHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
....*.
gi 490296977 227 HPRSAF 232
Cdd:cd03288 244 QEDGVF 249
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-208 |
2.95e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 131 QRYPSELSGGQRQRIALARALAVEPK--VLLLDEPFGALDAKVRKELRGWLRRLHDDLHiSTIFVTHDqEEALEVADRIV 208
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRII 548
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-282 |
8.00e-04 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 36.65 E-value: 8.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490296977 241 NRLDGTVSGNGFVAHGAAQAIAVDADFAG-PARAYVRPHDLEL 282
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPELAGAEGsEVVAYVRPHDLEI 43
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-163 |
1.09e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 18 LDDVSLDFPAGELVALLGPSGCGKTTLL----------------------RVIAGLEHADSGQVVLQGL----------- 64
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkkeqpgnhDRIEGLEHIDKVIVIDQSPigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 65 -------------DVASvGAR-ERQVGFVfqhyaLFRH--------MTVFENVAFGLRVkPRrerpseaaIRAKVHELLS 122
Cdd:cd03271 91 ytgvfdeirelfcEVCK-GKRyNRETLEV-----RYKGksiadvldMTVEEALEFFENI-PK--------IARKLQTLCD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490296977 123 lVQLDWLAQRYPS-ELSGGQRQRIALARAL---AVEPKVLLLDEP 163
Cdd:cd03271 156 -VGLGYIKLGQPAtTLSGGEAQRIKLAKELskrSTGKTLYILDEP 199
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
89-210 |
1.39e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490296977 89 MTVFENVAFGLrvkprrerpSEAAIRAKVHELLSLvQLDWLAQRYP-SELSGGQRQRIALARAL---AVEPKVLLLDEPF 164
Cdd:PRK00635 771 MTAYEAEKFFL---------DEPSIHEKIHALCSL-GLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPT 840
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490296977 165 GALDAKVRKELRGWLRRLHDDLHiSTIFVTHDQeEALEVADRIVVL 210
Cdd:PRK00635 841 TGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNM-HVVKVADYVLEL 884
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
15-45 |
4.87e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 4.87e-03
10 20 30
....*....|....*....|....*....|.
gi 490296977 15 FAALDDVSLDFPAGeLVALLGPSGCGKTTLL 45
Cdd:pfam13476 6 FRSFRDQTIDFSKG-LTLITGPNGSGKTTIL 35
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-207 |
6.02e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 6.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490296977 136 ELSGGQRQRIALARALA---VEPK-VLLLDEPFGALDAKVRKELRGWLRRLHDDLH-ISTIFvthdQEEALEVADRI 207
Cdd:cd03272 158 QLSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKELSDGAQfITTTF----RPELLEVADKF 230
|
|
| |
