|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-342 |
2.64e-156 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 441.84 E-value: 2.64e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 239 GGSYLNAQRIS--ELEFETSLGVVEAKPQTEIEFGSACELLLRPQHIQ-ASYEQDSAIS--VLEQQFMGDHCRYVIE-AH 312
Cdd:COG3842 238 EANLLPGTVLGdeGGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRlSPEGPENGLPgtVEDVVFLGSHVRYRVRlGD 317
|
330 340 350
....*....|....*....|....*....|....
gi 490872517 313 GQKLLA----TSSEALEVGMPVNVKVDTKGVLAF 342
Cdd:COG3842 318 GQELVVrvpnRAALPLEPGDRVGLSWDPEDVVVL 351
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-342 |
9.52e-121 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 351.68 E-value: 9.52e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MScALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMslncqtIDDGD-NWLPPE 78
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeIL------IGGRDvTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKlrKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 157 LLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADF 236
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 237 LGGGS--YLNAqRISELEFETSLGVVEAKPQTEIEFGSACELLLRPQHIQASYEQDSAIS--VLEQQFMGDHCRYVIEAH 312
Cdd:COG3839 234 IGSPPmnLLPG-TVEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEatVEVVEPLGSETLVHVRLG 312
|
330 340 350
....*....|....*....|....*....|..
gi 490872517 313 GQKLLA--TSSEALEVGMPVNVKVDTKGVLAF 342
Cdd:COG3839 313 GQELVArvPGDTRLRPGDTVRLAFDPERLHLF 344
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-335 |
4.94e-116 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 339.43 E-value: 4.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MScaLSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDdgdNWLPPEQR 80
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---TNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRppSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 239 GGSYLNAQRISElefETSLGVVEAKPQTEIEFGSAcELLLRPQHIQASYEQDS----AISVLEQQFMGDHCRYVIEAHG- 313
Cdd:COG1118 236 CVNVLRGRVIGG---QLEADGLTLPVAEPLPDGPA-VAGVRPHDIEVSREPEGentfPATVARVSELGPEVRVELKLEDg 311
|
330 340 350
....*....|....*....|....*....|
gi 490872517 314 -QKLL-------ATSSEALEVGMPVNVKVD 335
Cdd:COG1118 312 eGQPLeaevtkeAWAELGLAPGDPVYLRPR 341
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-342 |
4.80e-110 |
|
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: 324.68 E-value: 4.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKNrgMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 239 GGSYLNAQRISELEFETSLGVVEAKPQTEiEFGSACELLLRPQHIQASYEQDSA----ISVLEQQFMGDHCRYVIEAH-- 312
Cdd:TIGR03265 237 EVNWLPGTRGGGSRARVGGLTLACAPGLA-QPGASVRLAVRPEDIRVSPAGNAAnlllARVEDMEFLGAFYRLRLRLEgl 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 490872517 313 -GQKLLA--TSSE----ALEVGMPVNVKVDTKGVLAF 342
Cdd:TIGR03265 316 pGQALVAdvSASEverlGIRAGQPIWIELPAERLRAF 352
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-219 |
3.88e-106 |
|
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: 309.45 E-value: 3.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGM 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLrgVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-283 |
9.71e-96 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 288.77 E-value: 9.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 2 SCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRN 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH----VPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGG 239
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490872517 240 GSYLNAQ---RISELEFETSLGVVEAKPQTEIEF--GSACELLLRPQHI 283
Cdd:PRK09452 248 INIFDATvieRLDEQRVRANVEGRECNIYVNFAVepGQKLHVLLRPEDL 296
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-238 |
6.96e-93 |
|
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: 276.43 E-value: 6.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGM 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-238 |
2.81e-92 |
|
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: 274.99 E-value: 2.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGMIF 86
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD----VPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 87 QDYALFPHLTVNQNVGFGLK------DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-210 |
2.13e-91 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 273.50 E-value: 2.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYES----QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlppeq 79
Cdd:COG1116 7 ALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLElrGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-317 |
7.88e-88 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 267.74 E-value: 7.88e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDNWLPP--EQRNI 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG------QIFIDGEDVTHRsiQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLgvPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGGG 240
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 241 SYLNAQR------ISELEFETSLGVVEAKPQTEIEFGsacellLRPQHIQASYEQDSA--ISVLEQQFMGDHCRYVIEAH 312
Cdd:PRK11432 241 NIFPATLsgdyvdIYGYRLPRPAAFAFNLPDGECTVG------VRPEAITLSEQGEESqrCTIKHVAYMGPQYEVTVDWH 314
|
....*
gi 490872517 313 GQKLL 317
Cdd:PRK11432 315 GQELL 319
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-317 |
1.39e-85 |
|
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: 261.27 E-value: 1.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 35 LLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQ 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAFGLKmrKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 113 KKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIF 192
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 193 VTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGGGSYLNAQRISELEFETSLGVVEAKPQT-----E 267
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDiytdvP 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 268 IEFGSACELLLRPQHIQASYEQDSAIS------VLEQQFMGDHCRYVIE-AHGQKLL 317
Cdd:TIGR01187 237 VEKDQPLHVVLRPEKIVIEEEDEANSSnaiighVIDITYLGMTLEVHVRlETGQKVL 293
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-211 |
2.81e-85 |
|
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: 256.63 E-value: 2.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES----QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwlppEQR 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-------PGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLElqGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMN 211
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-238 |
1.66e-84 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 255.49 E-value: 1.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGMIF 86
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATR----VHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 87 QDYALFPHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRkhPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 165 SNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-252 |
2.25e-84 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 257.33 E-value: 2.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKY-ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RNIG 83
Cdd:COG1125 4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD----LDPVElrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLD--EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATvpRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG- 238
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGa 239
|
250
....*....|....*.
gi 490872517 239 --GGSYLNAQRISELE 252
Cdd:COG1125 240 drGLRRLSLLRVEDLM 255
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-219 |
1.95e-83 |
|
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: 251.79 E-value: 1.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSlncqtIDDGD-NWLPPEQRNIG 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY-----IGGRDvTDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKlrKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 162 EPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-238 |
1.31e-82 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 254.23 E-value: 1.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGMIFQDYALFPHLTVNQ 99
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN----LPPEKRGIAYVYQNYMLFPHKTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELIS 177
Cdd:NF040840 92 NIAFGLKlrKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 178 QIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:NF040840 172 EMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-238 |
2.83e-82 |
|
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: 249.56 E-value: 2.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLtCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGM 84
Cdd:cd03299 1 LKVENL-SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRkvDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-238 |
1.99e-81 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 252.45 E-value: 1.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGM 84
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-238 |
4.44e-79 |
|
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: 241.44 E-value: 4.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY-ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RN 81
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE----QDPVElrRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLD--EFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLkwPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFL 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
.
gi 490872517 238 G 238
Cdd:cd03295 237 G 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-238 |
4.09e-78 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 243.07 E-value: 4.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGMIFQDYALFPHLTVN 98
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHARDRKVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVGFGLKDLSDQQK------KEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK10851 93 DNIAFGLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 173 HELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:PRK10851 173 KELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
7-283 |
1.14e-76 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 239.51 E-value: 1.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLncqTIDDGD-NWLPPEQRNIGMI 85
Cdd:TIGR03258 8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLTGRI---AIADRDlTHAPPHKRGLALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 86 FQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:TIGR03258 85 FQNYALFPHLKVEDNVAFGLRaqKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 164 FSNIDTQVRHELISQIRKIFKK-QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGGGSY 242
Cdd:TIGR03258 165 LSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANI 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490872517 243 L--NAQRISE----LEFETSLGVVEA--KPQTEIEFGSACellLRPQHI 283
Cdd:TIGR03258 245 LpaIALGITEapglVDVSCGGAVIFAfgDGRHDGRDKLAC---IRPEHL 290
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-238 |
5.50e-75 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 230.80 E-value: 5.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTIleSLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGM 84
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA----LPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKD---LSDQQKKeKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRPglkLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 162 EPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-219 |
1.50e-74 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 229.10 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEhGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW--LPPEQRNIGMIFQDYALFPHLTVNQN 100
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 101 VGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIR 180
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 490872517 181 KIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-237 |
1.54e-73 |
|
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: 227.17 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTID-DGDNW--LPP 77
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG-------EILvDGQDItgLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 EQ-----RNIGMIFQDYALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIAR 149
Cdd:COG1127 75 KElyelrRRIGMLFQGGALFDSLTVFENVAFPLRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 150 SLAYKPDLLLLDEPFSNID---TQVRHELISQIRkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELyF 226
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDpitSAVIDELIRELR---DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-L 230
|
250
....*....|.
gi 490872517 227 HPSSKFVADFL 237
Cdd:COG1127 231 ASDDPWVRQFL 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-286 |
1.29e-72 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 228.96 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCaLSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDGD---NWLP 76
Cdd:PRK11650 1 MAG-LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSG-------EIWIGGrvvNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRNIGMIFQDYALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK11650 73 PADRDIAMVFQNYALYPHMSVRENMAYGLKIrgMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVA 234
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 235 DFLGGGSY-LNAQRISE--LEFETSLGVVEAKPQ-TEIEFGSACELLLRPQHIQAS 286
Cdd:PRK11650 233 SFIGSPAMnLLDGRVSAdgAAFELAGGIALPLGGgYRQYAGRKLTLGIRPEHIALS 288
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-331 |
2.00e-72 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 228.76 E-value: 2.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 12 CK-YESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRNIGMIFQDYA 90
Cdd:PRK11000 10 TKaYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 91 LFPHLTVNQNVGFGLK----DLSD-QQKKEKVQEMLELVHLDefgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:PRK11000 86 LYPHLSVAENMSFGLKlagaKKEEiNQRVNQVAEVLQLAHLL---DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 166 NIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGGGS---- 241
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKmnfl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 242 --YLNAQRISELEFETSLGV-----VEAkpqTEIEFGSACELLLRPQHIQASYEQDSAIS----VLEQqfMGDHCRYVIE 310
Cdd:PRK11000 243 pvKVTATAIEQVQVELPNRQqvwlpVEG---RGVQVGANMSLGIRPEHLLPSDIADVTLEgevqVVEQ--LGNETQIHIQ 317
|
330 340 350
....*....|....*....|....*....|.
gi 490872517 311 AHGQK----------LLATSSEALEVGMPVN 331
Cdd:PRK11000 318 IPAIRqnlvyrqndvVLVEEGATFAIGLPPE 348
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-238 |
2.19e-70 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 219.10 E-value: 2.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIGM 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGL---KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 162 EPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHsrEEAFAF--ADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLG 238
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTH--EMGFARevADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-228 |
1.59e-69 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 225.55 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES-----QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW-LPPE 78
Cdd:COG1123 261 LEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQD--YALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRlhgLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 153 YKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-213 |
1.55e-68 |
|
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: 212.43 E-value: 1.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIGM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGlkdlsdqqkkekvqemlelvhldefgdryphqLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490872517 165 SNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-224 |
4.08e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 213.39 E-value: 4.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDNWLPPEQ--RNI 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV-----RVLGEDVARDPAEvrRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG1131 156 DEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-225 |
2.35e-67 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 211.04 E-value: 2.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNIG 83
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQ--DYALFpHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG1122 79 LVFQnpDDQLF-APTVEEDVAFGPEnlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
2.92e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 210.67 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKY----ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLP 76
Cdd:COG1136 1 MSPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS----LS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQR------NIGMIFQDYALFPHLTVNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIA 148
Cdd:COG1136 77 ERELarlrrrHIGFVFQFFNLLPELTALENVALPLllAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSrEEAFAFADKMAVMNHGVIE 216
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-224 |
1.86e-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: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY----ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIddGDNWLPPEQ 79
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDY--ALFPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:COG1124 79 RRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 157 LLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-224 |
2.80e-66 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 208.51 E-value: 2.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW-LPPEQRNIG 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-330 |
4.25e-66 |
|
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: 212.27 E-value: 4.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 24 SLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDN--WLPPEQRNIGMIFQDYALFPHLTVNQNV 101
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiFLPPHRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 102 GFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRK 181
Cdd:COG4148 99 LYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 182 IFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGGGSYLNAqRISELEFETSLGVVE 261
Cdd:COG4148 179 LRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA-TVAAHDPDYGLTRLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 262 AK------PQTEIEFGSACELLLRPQHIQASYEQDSAISVLEQ---------QFMGDHCRYVIEAHGQKLLAT----SSE 322
Cdd:COG4148 258 LGggrlwvPRLDLPPGTRVRVRIRARDVSLALEPPEGSSILNIlpgrvveiePADGGQVLVRLDLGGQTLLARitrrSAD 337
|
330
....*....|
gi 490872517 323 AL--EVGMPV 330
Cdd:COG4148 338 ELglAPGQTV 347
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-200 |
1.96e-65 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 205.41 E-value: 1.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPL---SSGIMSLNCQTIDDgdnwLPPEQRN 81
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA----LPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFGL-KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490872517 161 DEPFSNIDT----QVRHELISQIRkifkKQGVTAIFVTHSREEA 200
Cdd:COG4136 158 DEPFSKLDAalraQFREFVFEQIR----QRGIPALLVTHDEEDA 197
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-236 |
1.59e-64 |
|
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: 205.18 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 24 SLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQ---TIDDGDnwLPPEQRN-IGMIFQDYALFPHLTVNQ 99
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaAMSRKE--LRELRRKkISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELIS 177
Cdd:cd03294 122 NVAFGLevQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 178 QIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADF 236
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-217 |
3.76e-63 |
|
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: 200.42 E-value: 3.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYE----SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDNWLPPEQ- 79
Cdd:cd03257 2 LEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG------SIIFDGKDLLKLSRr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 ------RNIGMIFQDY--ALFPHLTVNQNVGFGL----KDLSDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVA 146
Cdd:cd03257 76 lrkirrKEIQMVFQDPmsSLNPRMTIGEQIAEPLrihgKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 147 IARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQ 217
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGkIVEE 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
3.81e-63 |
|
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: 208.99 E-value: 3.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQT--ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS---SGIMSLNCQTIDDgdnwL 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQR--NIGMIFQD--YALFPhLTVNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIAR 149
Cdd:COG1123 77 SEALRgrRIGMVFQDpmTQLNP-VTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
22-239 |
4.04e-63 |
|
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: 204.70 E-value: 4.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 22 SLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI--DDGDNWLPPEQRNIGMIFQDYALFPHLTVNQ 99
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENImkQSPVELREVRRKKIGMVFQQFALFPHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELIS 177
Cdd:TIGR01186 91 NTSLGPELLgwPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 178 QIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGG 239
Cdd:TIGR01186 171 ELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-215 |
7.42e-63 |
|
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: 198.91 E-value: 7.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIGM 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGL---KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 162 EPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHsrEEAFA--FADKMAVMNHGVI 215
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTH--EMGFAreVADRVIFMDDGRI 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-215 |
9.53e-63 |
|
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: 198.87 E-value: 9.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY----ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR 80
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISK----LSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 ------NIGMIFQDYALFPHLTVNQNV--GFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:cd03255 77 aafrrrHIGFVFQSFNLLPDLTALENVelPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 153 YKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVI 215
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-224 |
4.35e-61 |
|
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: 196.03 E-value: 4.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RN 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS----LSRRElaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFG-------LKDLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGryphlglFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
7.65e-61 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 195.47 E-value: 7.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MScALSIKDLTCKYE----SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwlP 76
Cdd:COG4525 1 MS-MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRniGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:COG4525 75 GADR--GVVFQKDALLPWLNVLDNVAFGLRlrGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-213 |
5.13e-60 |
|
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: 191.53 E-value: 5.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQT--ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimSLNCQTIDDGDNWLPPEQRNIG 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG--EVLVDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQ--DYALFpHLTVNQNVGFGLKDLSDQQK--KEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03225 79 LVFQnpDDQFF-GPTVEEEVAFGLENLGLPEEeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-198 |
1.17e-59 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.03 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 17 QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW-LPPEQRNIGMIFQDYALFPHL 95
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReIPYLRRRIGVVFQDFRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRH 173
Cdd:COG2884 95 TVYENVALPLRvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW 174
|
170 180
....*....|....*....|....*
gi 490872517 174 ELISQIRKIfKKQGVTAIFVTHSRE 198
Cdd:COG2884 175 EIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.97e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.46 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDN---WLPp 77
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigYVP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 eQRnigmiFQDYALFPhLTVNQNVGFGL-------KDLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS 150
Cdd:COG1121 82 -QR-----AEVDWDFP-ITVRDVVLMGRygrrglfRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEqYGSASE 223
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEE 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-229 |
2.62e-58 |
|
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: 188.17 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW-LPPEQ 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPS 229
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-228 |
2.35e-56 |
|
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: 184.58 E-value: 2.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-----ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW-LPPE 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQ--DYALFpHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNlgLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-224 |
2.47e-55 |
|
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: 180.82 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLppeQRNIGM 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA---RRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 163 PFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG4555 159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-228 |
5.97e-55 |
|
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: 182.18 E-value: 5.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP---LSSGIMSLNCQTIDDgdnwLPP 77
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLK----LSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 EQ------RNIGMIFQD-Y-ALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLD---EFGDRYPHQLSGGQQQ 143
Cdd:COG0444 78 KElrkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRihgGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 144 RVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*
gi 490872517 224 LYFHP 228
Cdd:COG0444 238 LFENP 242
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-238 |
2.89e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.04 E-value: 2.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ- 79
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA----LSEREl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 ----RNIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:COG1135 78 raarRKIGMIFQHFNLLSSRTVAENVALPLEiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFV 233
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
|
....*
gi 490872517 234 ADFLG 238
Cdd:COG1135 238 RRFLP 242
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-215 |
2.93e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.93 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RNI 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA----MPPPEwrRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHlTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 162 EPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-226 |
3.10e-54 |
|
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: 177.66 E-value: 3.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwlPPEQRNIgmIFQDYALFPHLTVNQ 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-----PGPDRMV--VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFG----LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHEL 175
Cdd:TIGR01184 74 NIALAvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490872517 176 ISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYF 226
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPF 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-237 |
7.24e-54 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 176.82 E-value: 7.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlpPEQRNI----G 83
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK----VDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFG---LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 161 DEPFSNIDTQVRHELIsQIRKIFKKQGVTAIFVTHsrEEAFA--FADKMAVMNHGVIEQYGSASELYFHPSSKFVADFL 237
Cdd:PRK09493 161 DEPTSALDPELRHEVL-KVMQDLAEEGMTMVIVTH--EIGFAekVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-224 |
9.07e-54 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 176.31 E-value: 9.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTIleSLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTiddgDNWLPPEQRNIGM 84
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLK---DLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGLGLNpglKLNAAQR-EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 162 EPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-224 |
2.89e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 175.63 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTID-DGDNWLPPEQRN 81
Cdd:COG3638 2 MLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFG-LKDLS---------DQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSL 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrLGRTStwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-224 |
1.04e-52 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 173.39 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRN--- 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG----LPPHERArag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELV-HLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-330 |
1.63e-52 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 176.84 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDN--WLPPEQRNIGMIFQDYALFPHLTVNQN 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 101 VGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIR 180
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 181 KIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYfhPSSKFVADFLGGGSYLNAQRISELE-----FET 255
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW--ASPDLPWLAREDQGSLIEGVVAEHDqhyglTAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 256 SLG-------VVEAKPQTEIEFG-SACELLLRPQHIQASyeqdSAISVLEQQFMG------DHCRYVIEAHGQKLLATSS 321
Cdd:TIGR02142 254 RLGgghlwvpENLGPTGARLRLRvPARDVSLALQKPEAT----SIRNILPARVVEiedsdiGRVGVVLESGGKTLWARIT 329
|
330
....*....|....*
gi 490872517 322 E------ALEVGMPV 330
Cdd:TIGR02142 330 RwardelGIAPGTPV 344
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-224 |
1.86e-52 |
|
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: 172.75 E-value: 1.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPL-----SSGIMSLNCQTIDDGDNWLPPEQ 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPhLTVNQNVGFGLKD---LSDQQKKEKVQEMLELVHL-DEFGDR-YPHQLSGGQQQRVAIARSLAYK 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLhgiKLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 155 PDLLLLDEPFSNID---TQVRHELISQIRKifkkqGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03260 160 PEVLLLDEPTSALDpisTAKIEELIAELKK-----EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
3.24e-52 |
|
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: 171.51 E-value: 3.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRNIGM 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 490872517 165 SNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEA 200
Cdd:COG4133 160 TALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-215 |
7.19e-52 |
|
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: 170.79 E-value: 7.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLP--PEQRNIg 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvPQRRSI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 mifqDYAlFPhLTVNQNVGFGL-------KDLSdQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:cd03235 80 ----DRD-FP-ISVRDVVLMGLyghkglfRRLS-KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 157 LLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-215 |
1.42e-51 |
|
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: 168.73 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDNWLPPEQ--RNI 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI-----KVLGKDIKKEPEEvkRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVgfglkdlsdqqkkekvqemlelvhldefgdryphQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 163 PFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03230 122 PTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
1.49e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 170.96 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MScaLSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKaVAGLLPL-SSGIMSLNCQTIDDGDNwlPPEQ 79
Cdd:COG4161 1 MS--IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETpDSGQLNIAGHQFDFSQK--PSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 ------RNIGMIFQDYALFPHLTVNQNV---GFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS 150
Cdd:COG4161 76 airllrQKVGMVFQQYNLWPHLTVMENLieaPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASeLYFHPSS 230
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQT 233
|
....*..
gi 490872517 231 KFVADFL 237
Cdd:COG4161 234 EAFAHYL 240
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-225 |
7.10e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 169.92 E-value: 7.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT--ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMSLNCQTIDDGDNWlppEQR- 80
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGkVTVDGLDTLDEENLW---EIRk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDyalfPH-----LTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:TIGR04520 78 KVGMVFQN----PDnqfvgATVEDDVAFGLENLgvPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELY 225
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-237 |
2.32e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 2.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKaVAGLLPL-SSGIMSLNCQTIDDGDNWLPPE---- 78
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMpRSGTLNIAGNHFDFSKTPSDKAirel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPHLTVNQNV--------GfglkdLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS 150
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLieapcrvlG-----LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASElYFHPSS 230
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQT 233
|
....*..
gi 490872517 231 KFVADFL 237
Cdd:PRK11124 234 EAFKNYL 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-224 |
5.26e-50 |
|
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: 166.97 E-value: 5.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLN-CQTIDDGDNWLPPEQRNI 82
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVGFG----------LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 153 YKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
19-195 |
1.43e-49 |
|
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: 165.19 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDD-GDNWLPPEQRNIGMIFQDYALFPHLTV 97
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGaSKKQLVQLRRRIGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGFGLK---DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHE 174
Cdd:TIGR02982 100 RQNVQMALElqpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179
|
170 180
....*....|....*....|.
gi 490872517 175 LISQIRKIFKKQGVTAIFVTH 195
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTH 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-215 |
2.50e-49 |
|
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: 164.20 E-value: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIddgdNWLPPEQRNIGMIFQDYALFPHLTVNQNVG 102
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----TAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 103 FGLK---DLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQI 179
Cdd:cd03298 93 LGLSpglKLTAEDR-QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 490872517 180 RKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-219 |
4.42e-49 |
|
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: 162.60 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRnigmi 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS----LSPKEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 86 fqdyalfphltvNQNVGFglkdlsdqqkkekVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:cd03214 72 ------------ARKIAY-------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 166 NIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-228 |
5.84e-49 |
|
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: 171.79 E-value: 5.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlSSGIMSLNCQTIDDGDNW-LPPEQRNIGMIFQD-YA-LFPHLT 96
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRaLRPLRRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNVGFGLK----DLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQV 171
Cdd:COG4172 381 VGQIIAEGLRvhgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 172 RHELISQIRKIFKKQGVTAIFVTHS----ReeafAFADKMAVMNHG-VIEQyGSASELYFHP 228
Cdd:COG4172 461 QAQILDLLRDLQREHGLAYLFISHDlavvR----ALAHRVMVMKDGkVVEQ-GPTEQVFDAP 517
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-227 |
6.34e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 165.19 E-value: 6.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYE--SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWlpPEQRNI 82
Cdd:PRK13635 6 IRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW--DVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQ--DYAlFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK13635 84 GMVFQnpDNQ-FVGATVQDDVAFGLENigVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELYFH 227
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-227 |
8.05e-49 |
|
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: 164.01 E-value: 8.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI-DDGDNWLPPEQRNI 82
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNV-------------GFGLkdLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIAR 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgrlgykptwrsLLGR--FSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFH 227
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-219 |
1.33e-48 |
|
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: 162.34 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 14 YESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqtiDDGDNWLPPEQRNIGMIFQDYALFP 93
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVN----DQSHTGLAPYQRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 94 HLTVNQNVGFGLK---DLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQ 170
Cdd:TIGR01277 84 HLTVRQNIGLGLHpglKLNAEQQ-EKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490872517 171 VRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-239 |
3.38e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 162.61 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MScALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDdGDNWLPPEQR 80
Cdd:PRK11264 1 MS-AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID-TARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NI-------GMIFQDYALFPHLTVNQNVGFG---LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS 150
Cdd:PRK11264 79 LIrqlrqhvGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGvTAIFVTHsrEEAFA--FADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTH--EMSFArdVADRAIFMDQGRIVEQGPAKALFADP 235
|
250
....*....|....*
gi 490872517 229 ----SSKFVADFLGG 239
Cdd:PRK11264 236 qqprTRQFLEKFLLQ 250
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-165 |
5.05e-48 |
|
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: 158.58 E-value: 5.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNIGMIFQDYALFPHLTVNQ 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 100 NVGFG--LKDLSDQQKKEKVQEMLELVHLDEFGDR----YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:pfam00005 79 NLRLGllLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-213 |
1.03e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 161.41 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwlPPEQRniG 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAER--G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490872517 162 EPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-224 |
1.07e-47 |
|
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: 160.92 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRN--- 81
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG----LPPHRIArlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQN---VGFGLKDLSDQqkKEKVQEMLELV-HLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENlllGAYARRDRAEV--RADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-224 |
1.21e-47 |
|
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: 159.98 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES--QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLppeQRNI 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA---RQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-213 |
1.38e-47 |
|
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: 157.79 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNIGMI 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP--LEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 86 FQdyalfphltvnqnvgfglkdlsdqqkkekvqemlelvhldefgdryphqLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:cd00267 79 PQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490872517 166 NIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd00267 110 GLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-224 |
1.58e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 170.40 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ-- 79
Cdd:COG2274 473 DIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ----IDPASlr 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFpHLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIA 148
Cdd:COG2274 549 RQIGVVLQDVFLF-SGTIRENITLGDPDATD----EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAH-RLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-228 |
5.17e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 161.82 E-value: 5.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 24 SLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ-----RNIGMIFQD-YA-LFPHLT 96
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG----LSGRElrplrRRMQMVFQDpYAsLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNVGFGLK---DLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:COG4608 114 VGDIIAEPLRihgLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 173 heliSQI----RKIFKKQGVTAIFVTHS----REeafaFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:COG4608 194 ----AQVlnllEDLQDELGLTYLFISHDlsvvRH----ISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-225 |
1.97e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 165.32 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY-ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPE--QR 80
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD----LDPAswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFpHLTVNQNVGFGLKDLSDQQkkekVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIAR 149
Cdd:COG4988 412 QIAWVPQNPYLF-AGTIRENLRLGRPDASDEE----LEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITH-RLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-225 |
2.32e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 159.06 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MScaLSIKDLTCKYESQTILES-----LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWL 75
Cdd:PRK13637 1 MS--IKIENLTHIYMEGTPFEKkaldnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQRNIGMIFQ--DYALFPHlTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLD--EFGDRYPHQLSGGQQQRVAIAR 149
Cdd:PRK13637 79 SDIRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLglSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
14-213 |
2.36e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 156.80 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 14 YESQTI----LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRN------IG 83
Cdd:NF038007 11 YITKTIktkvLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTN----LSYSQKIilrrelIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:NF038007 87 YIFQSFNLIPHLSIFDNVALPLKyrGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490872517 162 EPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSrEEAFAFADKMAVMNHG 213
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYI-NQKGTTIIMVTHS-DEASTYGNRIINMKDG 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-228 |
3.19e-46 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 160.42 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 32 IVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDN--WLPPEQRNIGMIFQDYALFPHLTVNQNVGFGLKDlS 109
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAK-S 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 110 DQQKKEKVQEMLELVHLDefgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVT 189
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490872517 190 AIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY----FHP 228
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWassaMRP 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-215 |
9.62e-46 |
|
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: 156.35 E-value: 9.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG----LPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 N---IGMIFQDYALFPHLTVNQNV-----------------GFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGG 140
Cdd:COG0411 77 ArlgIARTFQNPRLFPELTVLENVlvaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-224 |
1.53e-45 |
|
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: 154.84 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLN-----CQTIDdgdnwlppEQRN 81
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvREPRE--------VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIhaRLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-228 |
3.25e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 157.66 E-value: 3.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG--------IMSLNcqtiddgDNWLPPEQRNIGMIFQDYAL 91
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGrvlvdgqdLTALS-------EKELRKARRQIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 92 FPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:PRK11153 94 LSSRTVFDNVALPLElaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 170 QVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGSASELYFHP 228
Cdd:PRK11153 174 ATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQ-GTVSEVFSHP 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-224 |
3.72e-45 |
|
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: 162.24 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ-- 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD----LDEDDlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFpHLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIA 148
Cdd:COG4987 409 RRIAVVPQRPHLF-DTTLRENLRLARPDATD----EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITH-RLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
3.99e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 155.66 E-value: 3.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQT---ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDNwLPP 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG------QIIIDGDL-LTE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 E-----QRNIGMIFQDY-ALFPHLTVNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIAR 149
Cdd:PRK13650 74 EnvwdiRHKIGMVFQNPdNQFVGATVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-213 |
1.26e-44 |
|
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: 152.98 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQRN--- 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG----LPPHEIArlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNV----------GFGLKDLSDQQKK--EKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIAR 149
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-217 |
1.94e-44 |
|
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: 152.20 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNwlppEQR------NIGMIFQDYAL 91
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE----DARarlrarHVGFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 92 FPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQV 171
Cdd:COG4181 102 LPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490872517 172 RHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQ 217
Cdd:COG4181 182 GEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-224 |
3.92e-44 |
|
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: 151.52 E-value: 3.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR---N 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK----LPPHERaraG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFGLkDLSDQQKKEKVQEMLEL--VhLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:TIGR03410 77 IAYVPQGREIFPRLTVEENLLTGL-AALPRRSRKIPDEIYELfpV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-231 |
4.18e-44 |
|
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: 152.27 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES---------QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwL 75
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQ-----RNIGMIFQDY--ALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHL-DEFGDRYPHQLSGGQQQR 144
Cdd:TIGR02769 79 DRKQrrafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQYGSASE 223
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEECDVAQL 238
|
....*....
gi 490872517 224 LYF-HPSSK 231
Cdd:TIGR02769 239 LSFkHPAGR 247
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-213 |
4.91e-44 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 150.48 E-value: 4.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDD-GDNWLPPEQRNIGMIFQDYALFPHLTV 97
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRRIGVVFQDFRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHEL 175
Cdd:TIGR02673 97 YENVALPLEvrGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 490872517 176 IsQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:TIGR02673 177 L-DLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-239 |
6.77e-44 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 151.29 E-value: 6.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGI-----MSLNCQTIDDGDNWLPPE 78
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVriegkVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPhLTVNQNVGFGLKDLSDQQKK---EKVQEMLELVHL-DEFGDR---YPHQLSGGQQQRVAIARSL 151
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKeldEIVEESLKKAALwDEVKDRlhdSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 152 AYKPDLLLLDEPFSNID---TQVRHELISQIRKIFkkqgvTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDpiaTGKIEELIQELKKKY-----TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNP 234
|
250
....*....|.
gi 490872517 229 SSKFVADFLGG 239
Cdd:TIGR00972 235 KEKRTEDYISG 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-228 |
7.32e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 152.48 E-value: 7.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSL-----EVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW--LPPEQ 79
Cdd:PRK13634 5 FQKVEHRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkkLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQ--DYALFPHlTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEE-TVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-198 |
1.89e-43 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 148.92 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDNWLPPE-------Q 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSG------QVYLNGQETPPLNskkaskfR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RN-IGMIFQDYALFPHLTVNQN--VGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:TIGR03608 75 REkLGYLFQNFALIENETVEENldLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490872517 157 LLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSRE 198
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPE 195
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-240 |
6.04e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 149.18 E-value: 6.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 3 CALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTID---DGDNWLPPEQ 79
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpDRDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 R--------NIGMIFQDYALFPHLTVNQNVGFG----LKdLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAI 147
Cdd:COG4598 87 RrqlqrirtRLGMVFQSFNLWSHMTVLENVIEApvhvLG-RPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHsrEEAFA--FADKMAVMNHGVIEQYGSASELY 225
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTH--EMGFArdVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*
gi 490872517 226 FHPSSKFVADFLGGG 240
Cdd:COG4598 243 GNPKSERLRQFLSSS 257
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-224 |
7.44e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 156.09 E-value: 7.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY-ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--R 80
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD----LTLESlrR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFpHLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPHQ-----------LSGGQQQRVAIAR 149
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIRENIRYGRPDATD----EEVEEAAKAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-239 |
8.23e-43 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.65 E-value: 8.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKavagllplssgimSLN--CQTID----------DG 71
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLR-------------CLNrmNDLIPgarvegeillDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 72 DNWLPPEQ------RNIGMIFQDYALFPHlTVNQNVGFGLKD---LSDQQKKEKVQEMLELVHL-DEFGDR---YPHQLS 138
Cdd:COG1117 78 EDIYDPDVdvvelrRRVGMVFQKPNPFPK-SIYDNVAYGLRLhgiKSKSELDEIVEESLRKAALwDEVKDRlkkSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNID---TQVRHELISQIRKIFkkqgvTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEELILELKKDY-----TIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250 260
....*....|....*....|....
gi 490872517 216 EQYGSASELYFHPSSKFVADFLGG 239
Cdd:COG1117 232 VEFGPTEQIFTNPKDKRTEDYITG 255
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-215 |
1.82e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 147.90 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDGDNWLPPEQRNIGM 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKDlsdqQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490872517 165 SNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-228 |
2.66e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 147.68 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQT---------ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDG 71
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 72 DNwlppEQR--NIGMIFQD--YALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHL-DEFGDRYPHQLSGGQQQ 143
Cdd:COG4167 81 DY----KYRckHIRMIFQDpnTSLNPRLNIGQILEEPLRlntDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 144 RVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
....*
gi 490872517 224 LYFHP 228
Cdd:COG4167 237 VFANP 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-213 |
3.39e-42 |
|
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: 144.45 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES--QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGD-NWLppeQRN 81
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDlESL---RKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFpHLTVNQNVgfglkdlsdqqkkekvqemlelvhldefgdryphqLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490872517 162 EPFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHG 213
Cdd:cd03228 122 EATSALDPETEALILEALRAL--AKGKTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-198 |
1.22e-41 |
|
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: 144.47 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDD-GDNWLPPEQRNIGMIFQDYALFPHLTVN 98
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHElI 176
Cdd:cd03292 97 ENVAFALEvtGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE-I 175
|
170 180
....*....|....*....|..
gi 490872517 177 SQIRKIFKKQGVTAIFVTHSRE 198
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHAKE 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-215 |
1.13e-40 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 141.63 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDGDNWLPPEQR--NI 82
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG-------SILLNGKPIKAKERrkSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQD--YALFPHlTVNQNVGFGLKDLSDqqKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03226 74 GYVMQDvdYQLFTD-SVREELLLGLKELDA--GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 161 DEPFSNIDTqvRH-ELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03226 151 DEPTSGLDY--KNmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-239 |
1.96e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 146.33 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 24 SLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG---IMSLNCQTIDDGDnWLPPEQRNIGMIFQDYALFPHLTVNQN 100
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqvlIDGVDIAKISDAE-LREVRRKKIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 101 VGFG--LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQ 178
Cdd:PRK10070 127 TAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 179 IRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGG 239
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-223 |
3.36e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 141.83 E-value: 3.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnWLPPEQ-RNI 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD---WSPAELaRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYAL-FPhLTVNQNVGFGLKDLSDQQKKEK--VQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLA------Y 153
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
8-225 |
4.64e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 142.15 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYE------SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSL-NCQTIDDGDNWlppEQR 80
Cdd:PRK13633 8 KNVSYKYEsneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdGLDTSDEENLW---DIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 N-IGMIFQ--DYALFPHLtVNQNVGFGLKDLSDQQK--KEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK13633 85 NkAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEeiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 156 DLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
5.04e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.05 E-value: 5.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgDNwLPPEQRN 81
Cdd:PRK13632 7 MIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-EN-LKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDY-ALFPHLTVNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFaFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-231 |
8.49e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 141.36 E-value: 8.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 10 LTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTID--DGDNWlPPEQRNIGMIFQ 87
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQR-KAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 88 DY--ALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRhllSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 162 EPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI--EQYGSASELYFHPSSK 231
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSPAGR 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-224 |
6.36e-39 |
|
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: 138.29 E-value: 6.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTID----DGDNWLPPEQ 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRlfgeRRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 R-NIGMIfqDYALFPHLTVNQNV------GF----GL-KDLSDQQKkEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAI 147
Cdd:COG1119 77 RkRIGLV--SPALQLRFPRDETVldvvlsGFfdsiGLyREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-239 |
8.04e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 138.56 E-value: 8.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTID---DGDNWLPPEQRN 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 --------IGMIFQDYALFPHLTVNQNV---GFGLKDLSDQQKKEKVQEMLELVHLDEFG-DRYPHQLSGGQQQRVAIAR 149
Cdd:PRK10619 86 qlrllrtrLTMVFQHFNLWSHMTVLENVmeaPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTqvrhELISQIRKIFKK---QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYF 226
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|...
gi 490872517 227 HPSSKFVADFLGG 239
Cdd:PRK10619 242 NPQSPRLQQFLKG 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-231 |
1.81e-38 |
|
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: 136.52 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR---N 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK----LPMHKRarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 160 LDEPFSNIDTQVRHElISQIRKIFKKQGVtAIFVT-HSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSK 231
Cdd:cd03218 157 LDEPFAGVDPIAVQD-IQKIIKILKDRGI-GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-215 |
2.00e-38 |
|
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: 135.81 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDNWLPPEQ--RNI 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG------EITFDGKSYQKNIEalRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNvgFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03268 75 GALIEAPGFYPNLTAREN--LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 163 PFSNIDTqvrhELISQIRKIF---KKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03268 153 PTNGLDP----DGIKELRELIlslRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-228 |
2.09e-38 |
|
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: 143.29 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY----ESQTILESLSLEVEHGEIVCLLGASGCGKT-TLLkAVAGLLPLSSGIMS----LNCQTIDDgdnwL 75
Cdd:COG4172 7 LSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPDPAAHPSgsilFDGQDLLG----L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQ------RNIGMIFQD--YALFPHLTVNQNVGFGL---KDLSDQQKKEKVQEMLELVHLDEFG---DRYPHQLSGGQ 141
Cdd:COG4172 82 SERElrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLrlhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 142 QQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTH-----SReeafaFADKMAVMNHGVIE 216
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHdlgvvRR-----FADRVAVMRQGEIV 236
|
250
....*....|..
gi 490872517 217 QYGSASELYFHP 228
Cdd:COG4172 237 EQGPTAELFAAP 248
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-215 |
2.38e-38 |
|
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: 134.09 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDdgdNWLPPEQRN--I 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---FASPRDARRagI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIfqdyalfphltvnqnvgfglkdlsdqqkkekvqemlelvhldefgdrypHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03216 78 AMV-------------------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 163 PFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03216 109 PTAALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-219 |
1.30e-37 |
|
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: 133.86 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGeIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLppeQRNIGM 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---RRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 163 PFSNIDTQVRHELisqiRKIFKKQGVTAIFV--THSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03264 157 PTAGLDPEERIRF----RNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-223 |
2.08e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.47 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RNI 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA----WSPWElaRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYAL-FPhLTVNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLA------- 152
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRapHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 153 YKPDLLLLDEPFSNIDtqVRHELIS-QIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:COG4559 157 GGPRWLFLDEPTSALD--LAHQHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-239 |
1.42e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 132.27 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSgIMSLNCQTIDDGDNWLPPE-- 78
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGEVRLFGRNIYSPDvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 ----QRNIGMIFQDYALFPHLTVNQNVGFGLK--DLSDQQKK--EKVQEMLELVHL-DEFGDR---YPHQLSGGQQQRVA 146
Cdd:PRK14267 80 pievRREVGMVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKEldERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 147 IARSLAYKPDLLLLDEPFSNID---TQVRHELISQIRKIFkkqgvTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKKEY-----TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
250
....*....|....*.
gi 490872517 224 LYFHPSSKFVADFLGG 239
Cdd:PRK14267 235 VFENPEHELTEKYVTG 250
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-215 |
2.15e-36 |
|
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: 129.26 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnWLPPEQR-N 81
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ---WDPNELGdH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHlTVNQNVgfglkdlsdqqkkekvqemlelvhldefgdryphqLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 162 EPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHsREEAFAFADKMAVMNHGVI 215
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-219 |
2.42e-36 |
|
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: 130.48 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlppeQRNIGM 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTV-NQNVGFG-LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03269 75 LPEERGLYPKMKViDQLVYLAqLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 163 PFSNIDTqVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03269 155 PFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-215 |
3.01e-36 |
|
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: 130.57 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDNWLPPEQ--RNIGMIFQDYALFPHLTV 97
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVKEPAEarRRLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHEL 175
Cdd:cd03266 96 RENLEYfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490872517 176 ISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03266 176 REFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-228 |
3.93e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 130.53 E-value: 3.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR---N 81
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH----LPMHKRarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHLTVNQNVG--FGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILavLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 160 LDEPFSNID--TqvrhelISQIRKIF---KKQGVtAIFVT-HSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:COG1137 160 LDEPFAGVDpiA------VADIQKIIrhlKERGI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-240 |
8.04e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 131.49 E-value: 8.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI--DDGDNWLPPEQRNIGMIFQ--DYALFPHl 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK13641 102 TVLKDVEFGPKNFgfSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 173 HELIsQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP------------SSKFVADFLGGG 240
Cdd:PRK13641 182 KEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlkkhyldepaTSRFASKLEKGG 260
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
1.34e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 135.49 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDG--DNWlppeQR 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdaDSW----RD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHlTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEF------------GDRyPHQLSGGQQQRVAIA 148
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARPDASD----AEIREALERAGLDEFvaalpqgldtpiGEG-GAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHSREEAfAFADKMAVM 210
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-210 |
1.41e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.76 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlpP---EQRNIGMIFQDYALFPHLT 96
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS----PrdaQAAGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNV-------GFGLkdLSDQQKKEKVQEMLELVHLDEfgDryPHQ----LSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:COG1129 96 VAENIflgreprRGGL--IDWRAMRRRARELLARLGLDI--D--PDTpvgdLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490872517 166 NI-DTQVRHeLISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG1129 170 SLtEREVER-LFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-223 |
2.11e-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: 135.26 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 15 ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLncqtidDG---DNWlPPEQ--RNIGMIFQDY 89
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL------DGadlSQW-DREElgRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 ALFPHlTVNQNVG-FGlkDLSDqqkkEKVQEMLELVHLDEFGDRYP-----------HQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG4618 416 ELFDG-TIAENIArFG--DADP----EKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITH-RPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
1.48e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.50 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIG 83
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQ--DYALF-PhlTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK13639 82 IVFQnpDDQLFaP--TVEEDVAFGPLNlgLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 159 LLDEPFSNIDTQVrhelISQIRKIFK---KQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13639 160 VLDEPTSGLDPMG----ASQIMKLLYdlnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-225 |
1.68e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 126.19 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT--ILESLSLEVEHGEIVCLLGASGCGKTTLLKavagLLP----LSSGIMSLNCQTIDDGDnwLPPE 78
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVN----LIPrfydVDSGRILIDGHDVRDYT--LASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFpHLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAI 147
Cdd:cd03251 75 RRQIGLVSQDVFLF-NDTVAENIAYGRPGATR----EEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-229 |
1.83e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 128.67 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 24 SLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMSLNCQTIDDGDNWLPPEQRNIGMIFQD--YALFPHLTVNQN 100
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 101 VGFGLK----DLSDQQKKEKVQEMLELVHL-DEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHEL 175
Cdd:PRK15079 121 IAEPLRtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 176 ISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPS 229
Cdd:PRK15079 201 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
3.30e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 128.04 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-----ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSL----NCQTIDDGDNWL 75
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQRNI----------GMIFQ--DYALFPHlTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGG 140
Cdd:PRK13631 102 NPYSKKIknfkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGPVALgvKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELIsQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGS 220
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*...
gi 490872517 221 ASELYFHP 228
Cdd:PRK13631 260 PYEIFTDQ 267
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-240 |
5.25e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 125.39 E-value: 5.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDNWLPP----EQR 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDISLLPlharARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGL---KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 158 LLLDEPFSNIDTqvrhelIS--QIRKI---FKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKF 232
Cdd:PRK10895 159 ILLDEPFAGVDP------ISviDIKRIiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
....*...
gi 490872517 233 VadFLGGG 240
Cdd:PRK10895 233 V--YLGED 238
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-224 |
1.47e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.61 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlppeQRNIG 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 mifqdY-----ALFPHLTV-NQNVGFG-LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:COG4152 75 -----YlpeerGLYPKMKVgEQLVYLArLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 157 LLLLDEPFSNIDTqVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG4152 150 LLILDEPFSGLDP-VNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-239 |
1.62e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.12 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGImSLNCQTIDDGDNWLPPE------ 78
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEV-TITGSIVYNGHNIYSPRtdtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPhLTVNQNVGFGL--KDLSDQQK-KEKVQEMLELVHL-DEFGDRYpHQ----LSGGQQQRVAIARS 150
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLrlKGIKDKQVlDEAVEKSLKGASIwDEVKDRL-HDsalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 151 LAYKPDLLLLDEPFSNIDTqvrhelISQiRKIFK-----KQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK14239 163 LATSPKIILLDEPTSALDP------ISA-GKIEEtllglKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|....
gi 490872517 226 FHPSSKFVADFLGG 239
Cdd:PRK14239 236 MNPKHKETEDYISG 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-224 |
3.09e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.27 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RNIG 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT----TPSRElaKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFG--------LKdlsdQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGrfpyskgrLT----AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 156 DLLLLDEPFSNIDtqVRH--ELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG4604 155 DYVLLDEPLNNLD--MKHsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-230 |
7.24e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.94 E-value: 7.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYESQT--ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNIGMI 85
Cdd:PRK13648 11 KNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN--FEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 86 FQD-YALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:PRK13648 89 FQNpDNQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELYFHPSS 230
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-224 |
1.54e-32 |
|
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: 121.18 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYE-SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNIGMIF 86
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT--LDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 87 QDYALFpHLTVNQNVGFGLKDLSDQQkkekVQEMLELVHLDEFGDRYPHQ-----------LSGGQQQRVAIARSLAYKP 155
Cdd:cd03253 82 QDTVLF-NDTIGYNIRYGRPDATDEE----VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 156 DLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH-RLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-242 |
2.17e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.17 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS-----SGIMSLNCQTIDDGDnwLPPEQ 79
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMD--VIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHLTVNQNVGFGLK----DLSDQQKKEKVQEMLELVHL-DEFGDRY---PHQLSGGQQQRVAIARSL 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKlnrlVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 152 AYKPDLLLLDEPFSNIDTqvrhELISQIRKIF--KKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPS 229
Cdd:PRK14247 162 AFQPEVLLADEPTANLDP----ENTAKIESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
250
....*....|...
gi 490872517 230 SKFVADFLGGGSY 242
Cdd:PRK14247 238 HELTEKYVTGRLY 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-223 |
2.63e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RNI 82
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM----LSSRQlaRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVGFGLK-------DLSdQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYGRSpwlslwgRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 156 DLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-213 |
5.32e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.14 E-value: 5.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlpPEQ- 79
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS----PRDa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 --RNIGMIFQDYALFPHLTVNQNVGFGLKD-----LSDQQKKEKVQEMLElvhldEFG-----DRYPHQLSGGQQQRVAI 147
Cdd:COG3845 78 iaLGIGMVHQHFMLVPNLTVAENIVLGLEPtkggrLDRKAARARIRELSE-----RYGldvdpDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-228 |
8.23e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.61 E-value: 8.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLncqtidDGDNWLPPE-------QRNIGMIFQD-YA- 90
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY------QGQDLLKADpeaqkllRQKIQIVFQNpYGs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 91 LFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:PRK11308 105 LNPRKKVGQILEEPLLintSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 167 IDTQVRheliSQIRKIF----KKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGSASELYFHP 228
Cdd:PRK11308 185 LDVSVQ----AQVLNLMmdlqQELGLSYVFISHDLSVVEHIADEVMVMYLGrCVEK-GTKEQIFNNP 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
9.87e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 120.29 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYE-SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNIG 83
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQ--DYALFPHlTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13652 82 LVFQnpDDQIFSP-TVEQDIAFGPINlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-200 |
1.11e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 118.73 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNwlppEQR------NIGMIFQDYAL 91
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE----EARaklrakHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 92 FPHLTVNQNVGFG--LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:PRK10584 100 IPTLNALENVELPalLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190
....*....|....*....|....*....|.
gi 490872517 170 QVRHELISQIRKIFKKQGVTAIFVTHSREEA 200
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
2.58e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQT---ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWlpP 77
Cdd:PRK13642 1 MNKILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 EQRNIGMIFQDY-ALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13642 79 LRRKIGMVFQNPdNQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-239 |
3.07e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 118.23 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPE----QR 80
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaiklRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGLKDLSDQQKKEK---VQEMLELVHL-DEFGDRY---PHQLSGGQQQRVAIARSLAY 153
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIkkiVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 154 KPDLLLLDEPFSNID---TQVRHELISQIrkifkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSS 230
Cdd:PRK14246 171 KPKVLLMDEPTSMIDivnSQAIEKLITEL-----KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
....*....
gi 490872517 231 KFVADFLGG 239
Cdd:PRK14246 246 ELTEKYVIG 254
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-239 |
3.27e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 118.71 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDNwLPPEQRN----- 81
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG------EILFDGEN-IPAMSRSrlytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 ---IGMIFQDYALFPHLTVNQNVGFGLKD---LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK11831 83 rkrMSMLFQSGALFTDMNVFDNVAYPLREhtqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 156 DLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKfVAD 235
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQ 241
|
....
gi 490872517 236 FLGG 239
Cdd:PRK11831 242 FLDG 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-225 |
7.32e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 118.19 E-value: 7.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDdGDNWLPPE----------QRNIGMIFQ-- 87
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG------QTIV-GDYAIPANlkkikevkrlRKEIGLVFQfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 88 DYALFPHlTVNQNVGFGLKDLSD--QQKKEKVQEMLELVHL-DEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK13645 100 EYQLFQE-TIEKDIAFGPVNLGEnkQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 165 SNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
7.62e-31 |
|
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: 114.84 E-value: 7.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYEsqtiLESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRNIG 83
Cdd:cd03215 4 VLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---PRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIF-----QDYALFPHLTVNQNVGFglkdlsdqqkkekvqemlelvhldefgdryPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03215 77 IAYvpedrKREGLVLDLSVAENIAL------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-225 |
8.42e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYES--QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAG-LLPLSSGIMSLNCQTIDDGDNWLPPEQR 80
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDY-ALFPHLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK13640 85 KVGIVFQNPdNQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-215 |
9.69e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 122.67 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGD-NWLPPE--QRNI 82
Cdd:TIGR03375 467 RNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSV-----LLDGVDiRQIDPAdlRRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFpHLTVNQNVGFGLKDLSDQQkkekVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSL 151
Cdd:TIGR03375 542 GYVPQDPRLF-YGTLRDNIALGAPYADDEE----ILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVI 215
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-225 |
1.01e-30 |
|
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: 116.48 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYES---QTILESLSLEVEHGEIVCLLGASGCGKTTllkaVAGLL-----PLSSGImslncqTIDDGD------ 72
Cdd:cd03249 3 FKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLerfydPTSGEI------LLDGVDirdlnl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 73 NWLppeQRNIGMIFQDYALFPhLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQ 141
Cdd:cd03249 73 RWL---RSQIGLVSQEPVLFD-GTIAENIRYGKPDATD----EEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 142 QQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSA 221
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTH 221
|
....
gi 490872517 222 SELY 225
Cdd:cd03249 222 DELM 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-224 |
2.20e-30 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 120.68 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCqtiddGDNWL------PPEQ----RNIGMIFQDY 89
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRV-----GDEWVdmtkpgPDGRgrakRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 ALFPHLTVNQNV--GFGLkDLSDQQKKEKVQEMLELVHLDE-----FGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:TIGR03269 375 DLYPHRTVLDNLteAIGL-ELPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-224 |
2.20e-30 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 120.92 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 15 ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlpPEQ--RNIGMIFQDYALF 92
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD----RETfgKHIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 93 PHlTVNQNVG-FGlkdlsDQQKKEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:TIGR01842 405 PG-TVAENIArFG-----ENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-215 |
2.98e-30 |
|
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: 114.61 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYESQTI--LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSlncqtIDDGDNW-LPPE--QRNI 82
Cdd:cd03245 6 RNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-----LDGTDIRqLDPAdlRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFpHLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSL 151
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAPLADD----ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVI 215
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-237 |
3.65e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.20 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlSSGIMSLNCQTIDdgdNW----LPPEQRNIGMIFQD--YAL 91
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLH---NLnrrqLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 92 FPHLTVNQNVGFGL----KDLSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:PRK15134 376 NPRLNVLQIIEEGLrvhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 167 IDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGSASELYFHPSSKFVADFL 237
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQ-GDCERVFAAPQQEYTRQLL 526
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-195 |
4.20e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.60 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKY----ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTID--DGDNW 74
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtlDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 75 LPPEQRNIGMIFQDYALFPHLTVNQNV-------GFGLKdlsdqQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAI 147
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVevpavyaGLERK-----QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISqIRKIFKKQGVTAIFVTH 195
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTH 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
6.30e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.22 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGL-LPLSSGIMSLNCQTIDDGDNWLppe 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDY--ALFPhLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13647 78 RSKVGLVFQDPddQVFS-STVWDDVAFGPVNmgLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISqIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-200 |
1.53e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.94 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 14 YESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDGDNwlppeqRNIGMIFQDYAL-- 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAGG------ARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 92 -FPhLTVNQNVGFG-------LKDLSDQQKKEkVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:NF040873 69 sLP-LTVRDLVAMGrwarrglWRRLTRDDRAA-VDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490872517 164 FSNIDTQVR---HELISQIRkifkKQGVTAIFVTHSREEA 200
Cdd:NF040873 147 TTGLDAESReriIALLAEEH----ARGATVVVVTHDLELV 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-195 |
1.63e-29 |
|
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: 112.07 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRNIGM 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR---DEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKDLSDQQKKekVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:TIGR01189 78 LGHLPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|.
gi 490872517 165 SNIDTQVRHELISQIRKIFKKQGVtAIFVTH 195
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGI-VLLTTH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-206 |
1.76e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.37 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLT-CKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDdgdnwLPPEQRni 82
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------RIA-----RPAGAR-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 gMIF--Q----------DYALFPHLTvnqnvgfglKDLSDQQkkekVQEMLELVHLDEFGDRY------PHQLSGGQQQR 144
Cdd:COG4178 428 -VLFlpQrpylplgtlrEALLYPATA---------EAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADK 206
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGH-RSTLAAFHDR 552
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-225 |
3.20e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.72 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 14 YESQTIlESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI--DDGDNWLPPEQRNIGMIFQ--DY 89
Cdd:PRK13646 18 YEHQAI-HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKDKYIRPVRKRIGMVFQfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 ALFPHlTVNQNVGFGLKDLS---DQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:PRK13646 97 QLFED-TVEREIIFGPKNFKmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 167 IDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-224 |
3.69e-29 |
|
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: 112.19 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 13 KYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG---IMSLNCQTIDDgdNWLppeQRNIGMIFQDY 89
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlVDGHDLALADP--AWL---RRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 ALFpHLTVNQNVGFGLKDLSdqqkKEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03252 86 VLF-NRSIRDNIALADPGMS----MERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
4.46e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 117.08 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYE-SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDNWLPPE---QR 80
Cdd:TIGR02868 335 LELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSSLDQdevRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFpHLTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIAR 149
Cdd:TIGR02868 410 RVSVCAQDAHLF-DTTVRENLRLARPDATD----EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHS 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-215 |
6.47e-29 |
|
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: 111.21 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP---LSSGIMSLNCQTIDDgDNWlppeQRNIGMIFQDYALFPHL 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP-DQF----QKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGL-----KDLSDQQKKEKV-QEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:cd03234 97 TVRETLTYTAilrlpRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490872517 170 QVRHELISQIRKIFKKqGVTAIFVTHS-REEAFAFADKMAVMNHGVI 215
Cdd:cd03234 177 FTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-237 |
9.49e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 111.67 E-value: 9.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSS-----GIMSLNCQTIDDGDNWLPPE 78
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPhLTVNQNVGFGLKdLSDQQKKEKVQEMLELVHLD-EFGDRYPHQ-------LSGGQQQRVAIARS 150
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVK-IVGWRPKLEIDDIVESALKDaDLWDEIKHKihksaldLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVM--NHGVIEQ---YGSASELY 225
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQlveFGLTKKIF 244
|
250
....*....|..
gi 490872517 226 FHPSSKFVADFL 237
Cdd:PRK14258 245 NSPHDSRTREYV 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-224 |
1.02e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 116.48 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLT-CKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSsGIMSLNCQTIDDgdnwLPPEQ--RN 81
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRE----LDPESwrKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFpHLTVNQNVGFGLKDLSDQQkkekVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARS 150
Cdd:PRK11174 425 LSWVGQNPQLP-HGTLRDNVLLGNPDASDEQ----LQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-213 |
2.65e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.82 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCA-LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGdnwLPPEQ 79
Cdd:PRK13537 3 MSVApIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR---ARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHLTVNQNVG-----FGLkdlSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLvfgryFGL---SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKqGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
3.39e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT-ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIG 83
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQ--DYALFPhLTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13636 86 MVFQdpDNQLFS-ASVYQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-225 |
5.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILES-----LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI--DDGDNWLP 76
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRNIGMIFQ--DYALFPHlTVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVAIARSL 151
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNfgVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISqirkIFKK---QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMT----LFKKlhqSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-228 |
7.97e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.18 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDD-GDNWLPPEQRNIGMIFQD-YA-LFPHLT 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNVGFGLKD---LSDQQKKEKVQEMLELVHL-DEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK10261 420 VGDSIMEPLRVhglLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 173 HELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-213 |
8.73e-28 |
|
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: 107.56 E-value: 8.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ-----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLN------CQTiddgdN 73
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgsiayvSQE-----P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 74 WLPPEqrnigmifqdyalfphlTVNQNVGFGLKdlSDQQKKEKVqemLELVHLDEFGDRYPHQ-----------LSGGQQ 142
Cdd:cd03250 76 WIQNG-----------------TIRENILFGKP--FDEERYEKV---IKACALEPDLEILPDGdlteigekginLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 143 QRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQ-IRKIFKKqGVTAIFVTHsREEAFAFADKMAVMNHG 213
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLN-NKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-225 |
1.45e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLN--CQTIDDGDNWLPPEQRNIGMIFQ--DYALFPHl 95
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGLKD--LSDQQKKEKVQEMLELVHLD-EFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK13643 101 TVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 173 HELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13643 181 IEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-219 |
1.67e-27 |
|
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: 107.23 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIddgdnWLPpeqrNIGM 84
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLL----GLGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQdyalfPHLTVNQNVGFG--LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03220 94 GFN-----PELTGRENIYLNgrLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 163 PFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-225 |
2.42e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.17 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIGM 84
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQD--YALFpHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK13638 82 VFQDpeQQIF-YTDIDSDIAFSLRNLgvPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIFkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
2.46e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILE-----SLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMslncqtIDDGD-NWLPP 77
Cdd:COG1101 2 LELKNLSKTFNPGTVNEkraldGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGsIL------IDGKDvTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 EQR--NIGMIFQDYAL--FPHLTVNQNV--------GFGLKDLSDQQKKEKVQEMLELVHL-------DEFGdryphQLS 138
Cdd:COG1101 76 YKRakYIGRVFQDPMMgtAPSMTIEENLalayrrgkRRGLRRGLTKKRRELFRELLATLGLglenrldTKVG-----LLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQvRHELISQI-RKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-215 |
2.87e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.63 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQT-----ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPE--- 78
Cdd:PRK13651 5 VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEkvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 -------------------QRNIGMIFQ--DYALFPHlTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDE-FGDRYP 134
Cdd:PRK13651 85 eklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMgvSKEEAKKRAAKYIELVGLDEsYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 135 HQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHElisqIRKIFK---KQGVTAIFVTHSREEAFAFADKMAVMN 211
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKE----ILEIFDnlnKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 490872517 212 HGVI 215
Cdd:PRK13651 240 DGKI 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-195 |
4.38e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.44 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQRN--IGMIFQDYALFPHLT 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHE 174
Cdd:PRK11629 104 ALENVAMPLliGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|.
gi 490872517 175 LISQIRKIFKKQGVTAIFVTH 195
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTH 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-195 |
5.40e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 106.11 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNW-LPPEQRNIGMIFQDYALFPHLTVN 98
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFLRRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVGFGL--KDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRhELI 176
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS-EGI 176
|
170
....*....|....*....
gi 490872517 177 SQIRKIFKKQGVTAIFVTH 195
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATH 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-195 |
7.29e-27 |
|
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: 105.27 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRNIGM 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---DSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKDLSDQQkkekVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRFWHADHSDEQ----VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 490872517 165 SNIDTQVRHELISQIRKiFKKQGVTAIFVTH 195
Cdd:cd03231 154 TALDKAGVARFAEAMAG-HCARGGMVVLTTH 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-215 |
8.14e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYEsqtiLESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPE--QRN 81
Cdd:COG1129 256 VLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS---PRDaiRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQD---YALFPHLTVNQNV---------GFGLkdLSDQQKKEKVQEMLELVHLdefgdRYPH------QLSGGQQQ 143
Cdd:COG1129 329 IAYVPEDrkgEGLVLDLSIRENItlasldrlsRGGL--LDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 144 RVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE-LAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-228 |
8.60e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 106.80 E-value: 8.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnWLPPEQRnIGMIFQD--YALFPHLTV 97
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-YSYRSQR-IRMIFQDpsTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGFGLK---DLSDQQKKEKVQEMLELVHL-DEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRH 173
Cdd:PRK15112 107 SQILDFPLRlntDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 174 ELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-213 |
1.82e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.78 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES------QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLL--PLSSGIMSLNCQTIDDgDNWlp 76
Cdd:cd03213 4 LSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDK-RSF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 peQRNIGMIFQDYALFPHLTVNQNVGFGLKdLSdqqkkekvqemlelvhldefgdryphQLSGGQQQRVAIARSLAYKPD 156
Cdd:cd03213 81 --RKIIGYVPQDDILHPTLTVRETLMFAAK-LR--------------------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 157 LLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHS-REEAFAFADKMAVMNHG 213
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
1.87e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.48 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMS--------LNCQTIDDGD 72
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShiellgrtVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 73 nwLPPEQRNIGMIFQDYALFPHLTVNQNVGFG-----------LKDLSDQQKKEKVQEmLELVHLDEFGDRYPHQLSGGQ 141
Cdd:PRK09984 81 --IRKSRANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQA-LTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 142 QQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSA 221
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
...
gi 490872517 222 SEL 224
Cdd:PRK09984 238 QQF 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-218 |
4.15e-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: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLplssgimslncqTIDDGDNWLPPEQRnIGMIF 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL------------EPDSGEVSIPKGLR-IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 87 QDYALFPHLTVNQNVGFGLKDLSD-QQKKEKVQEML---------------ELVHLDE---------------FGDRYPH 135
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRAlEAELEELEAKLaepdedlerlaelqeEFEALGGweaearaeeilsglgFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 136 Q----LSGGQQQRVAIARSLAYKPDLLLLDEPfSN---IDTqvrhelISQIRKIFKKQGVTAIFVTHSREeaF--AFADK 206
Cdd:COG0488 148 RpvseLSGGWRRRVALARALLSEPDLLLLDEP-TNhldLES------IEWLEEFLKNYPGTVLVVSHDRY--FldRVATR 218
|
250
....*....|..
gi 490872517 207 MAVMNHGVIEQY 218
Cdd:COG0488 219 ILELDRGKLTLY 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-224 |
4.80e-26 |
|
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: 103.46 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGD-NWLppeQRNIGMIFQDYALFPHlTV 97
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrKSL---RSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGFGlkdlSDQQKKEKVQEMLELVHLDEFGDRYP-----------HQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:cd03254 94 MENIRLG----RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 167 IDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03254 170 IDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-229 |
4.85e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.96 E-value: 4.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlSSGIMS----LNCQTIDDgdnwLP 76
Cdd:PRK09473 13 LDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGgsatFNGREILN----LP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRN------IGMIFQD--YALFPHLTVNQNVGFGL---KDLSDQQKKEKVQEMLELVHLDEFGDR---YPHQLSGGQQ 142
Cdd:PRK09473 88 EKELNklraeqISMIFQDpmTSLNPYMRVGEQLMEVLmlhKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 143 QRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSAS 222
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
....*..
gi 490872517 223 ELYFHPS 229
Cdd:PRK09473 248 DVFYQPS 254
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-215 |
7.39e-26 |
|
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: 103.18 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 13 KYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqtiddgdNWLPPEQRN-----IGMIF- 86
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA--------GLVPWKRRKkflrrIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 87 QDYALFPHLTVNQnvGFGLK----DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03267 102 QKTQLWWDLPVID--SFYLLaaiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-223 |
1.02e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 13 KYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQT---IDdgdnwlppeqrnIGMIFQdy 89
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalLE------------LGAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 alfPHLTVNQNVGFG--LKDLSDQQKKEKVQEMLELVHLDEFGDRyP-HQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:COG1134 101 ---PELTGRENIYLNgrLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 167 IDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:COG1134 177 GDAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-196 |
2.37e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.10 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQ----- 79
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEAchylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 -RNigmifqdyALFPHLTVNQNVGF-----GLKDLSdqqkkekVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:PRK13539 80 hRN--------AMKPALTVAENLEFwaaflGGEELD-------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490872517 154 KPDLLLLDEPFSNIDtqvRH--ELISQIRKIFKKQGVTAIFVTHS 196
Cdd:PRK13539 145 NRPIWILDEPTAALD---AAavALFAELIRAHLAQGGIVIAATHI 186
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-220 |
6.29e-25 |
|
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: 100.26 E-value: 6.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-ImslncqTIDDGD-NWLPPEQ- 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGsI------LIDGVDiSKIGLHDl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 -RNIGMIFQDYALFPHlTVNQNVgfglkDLSDQQKKEKVQEMLELVHLDEFGDRYPHQL-----------SGGQQQRVAI 147
Cdd:cd03244 77 rSRISIIPQDPVLFSG-TIRSNL-----DPFGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGS 220
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-219 |
7.79e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 7.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG--------IMSLNCQTIDdgdnwlp 76
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtvlvagddVEALSARAAS------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 peqRNIGMIFQDYALFPHLTVNQNVGFGLK------DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS 150
Cdd:PRK09536 77 ---RRVASVPQDTSLSFEFDVRQVVEMGRTphrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 151 LAYKPDLLLLDEPFSNIDT--QVRH-ELISQIrkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDInhQVRTlELVRRL----VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-206 |
9.74e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 9.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ--RNI 82
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST----LKPEIyrQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHlTVNQNVGFGLkdlsdQQKKEKVQEMLELVHLDEFG------DRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPW-----QIRNQQPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490872517 157 LLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEaFAFADK 206
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADK 206
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-198 |
1.12e-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: 97.52 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGImslncqtiddgdnwlppeqrnigm 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 ifqdyalfphLTVNQNVGFGlkdlsdqqkkekvqemlelvhldefgdrYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03221 57 ----------VTWGSTVKIG----------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|....
gi 490872517 165 SNIDTQVRHELISQIRKiFKKqgvTAIFVTHSRE 198
Cdd:cd03221 99 NHLDLESIEALEEALKE-YPG---TVILVSHDRY 128
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-217 |
1.22e-24 |
|
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: 100.68 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimSLNCQTIDDGDNWL----PPEQR 80
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHG--TATYIMRSGAELELyqlsEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NI-----GMIFQDYA--LFPHLTVNQNVGFGLKDLSDQQK---KEKVQEMLELVHLDEFG-DRYPHQLSGGQQQRVAIAR 149
Cdd:TIGR02323 82 RLmrtewGFVHQNPRdgLRMRVSAGANIGERLMAIGARHYgniRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQ 217
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGrVVES 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-252 |
1.84e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 103.73 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTL---LKAVAGLLPLSSGI-----MSLNCQTID------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIiyhvaLCEKCGYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 70 ------------DGDNWLPPE------QRNIGMIFQ-DYALFPHLTVNQNVGFGLKDLSdQQKKEKVQEMLELVHLDEFG 130
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 131 DRYPH---QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKM 207
Cdd:TIGR03269 160 HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490872517 208 AVMNHGVIEQYGSASELyfhpsskfVADFLGGGSYLNAQRISELE 252
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECEVEVG 276
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-239 |
1.92e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGI----------MSLNCQTIDdgdnw 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkvtfhgKNLYAPDVD----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 75 lPPE-QRNIGMIFQDYALFPHlTVNQNVGFGLKDLSDQ-QKKEKVQEMLELVHL-DEFGDRYPHQ---LSGGQQQRVAIA 148
Cdd:PRK14243 86 -PVEvRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgDMDELVERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 149 RSLAYKPDLLLLDEPFSNID---TQVRHELISQIrkifkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIE---QYG--- 219
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDpisTLRIEELMHEL-----KEQYTIIIVTHNMQQAARVSDMTAFFNVELTEgggRYGylv 238
|
250 260
....*....|....*....|...
gi 490872517 220 --SASELYFH-PSSKFVADFLGG 239
Cdd:PRK14243 239 efDRTEKIFNsPQQQATRDYVSG 261
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-217 |
2.85e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimSLNCQTIDDGDNWL----PPEQR 80
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAG--EVHYRMRDGQLRDLyalsEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NI-----GMIFQDYA--LFPHLTVNQNVGFGLKDLSDQ---QKKEKVQEMLELVHLDEfgDR---YPHQLSGGQQQRVAI 147
Cdd:PRK11701 85 RLlrtewGFVHQHPRdgLRMQVSAGGNIGERLMAVGARhygDIRATAGDWLERVEIDA--ARiddLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQ 217
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVES 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-219 |
3.47e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 97.38 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLppeQRNI 82
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDyalfPHL---TVNQNVGfglkdlsdqqkkekvqemlelvhldefgdrypHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03247 78 SVLNQR----PYLfdtTLRNNLG--------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-233 |
7.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLncQTIDDGD-NWLPPEQRNIGMIFQD-YALFPHLTV 97
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDfSKLQGIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGFGLKDL--SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHEL 175
Cdd:PRK13644 96 EEDLAFGPENLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 176 ISQIRKIFKKqGVTAIFVTHSREEAFAfADKMAVMNHGVIEQYGSASELYFHPSSKFV 233
Cdd:PRK13644 176 LERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-206 |
1.06e-23 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 95.68 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 15 ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLncqtiddgdnwlpPEQRNIGMIFQDyALFPH 94
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------PEGEDLLFLPQR-PYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 LTvnqnvgfgLKDLSdqqkkekvqemlelvhldefgdRYP--HQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:cd03223 78 GT--------LREQL----------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....
gi 490872517 173 HelisQIRKIFKKQGVTAIFVTHsREEAFAFADK 206
Cdd:cd03223 128 D----RLYQLLKELGITVISVGH-RPSLWKFHDR 156
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-195 |
1.71e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlppEQRNigm 84
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-----DEYH--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 ifQDYALFPH-------LTVNQNVGFGLKdLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK13538 74 --QDLLYLGHqpgikteLTALENLRFYQR-LHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490872517 158 LLLDEPFSNIDTQ---VRHELISQirkiFKKQGVTAIFVTH 195
Cdd:PRK13538 151 WILDEPFTAIDKQgvaRLEALLAQ----HAEQGGMVILTTH 187
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
1.76e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnWLPPE-- 78
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD---WQTAKim 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELV-HLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 158 LLLDEP---FSNIDTQVRHELISQIRkifkKQGVTAIFVTHSREEAFAFADKMAVMNHG--VIEQYGSA 221
Cdd:PRK11614 159 LLLDEPslgLAPIIIQQIFDTIEQLR----EQGMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGDA 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-222 |
1.86e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 101.35 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRnIGMIFQ 87
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATRRR-VGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 88 DYALFPHLTVNQNVGFG--LKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:NF033858 347 AFSLYGELTVRQNLELHarLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 166 NIDTQVR----HELISQIRkifkKQGVTaIFV-THSREEAfAFADKMAVMNHG----------VIEQYGSAS 222
Cdd:NF033858 427 GVDPVARdmfwRLLIELSR----EDGVT-IFIsTHFMNEA-ERCDRISLMHAGrvlasdtpaaLVAARGAAT 492
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-251 |
2.09e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.09 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY--ESQTI--LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSL--------NCQTIDDGD 72
Cdd:PRK10261 13 LAVENLNIAFmqEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrSRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 73 NWLPPEQR----NIGMIFQD--YALFPHLTVNQNVGFGLK---DLSDQQKKEKVQEMLELVHLDE---FGDRYPHQLSGG 140
Cdd:PRK10261 93 QSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlhqGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGS 220
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
250 260 270
....*....|....*....|....*....|.
gi 490872517 221 ASELYFHPSSKFVADFLGGGSYLNAQRISEL 251
Cdd:PRK10261 253 VEQIFHAPQHPYTRALLAAVPQLGAMKGLDY 283
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
2.10e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.51 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIddgdNWLPP--- 77
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC----ARLTPaka 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 78 EQRNIGMIFQDYALFPHLTVNQNVGFGLKdlSDQQKKEKVQEML-EL-VHLDefgdryPHQLSG----GQQQRVAIARSL 151
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKENILFGLP--KRQASMQKMKQLLaALgCQLD------LDSSAGslevADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-213 |
2.43e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.98 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQ-RNIG 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG----LPGHQiARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MI--FQDYALFPHLTVNQNV----------GF--GLKDL-----SDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQR 144
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIENLlvaqhqqlktGLfsGLLKTpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
2.59e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.39 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP--------LSSGiMSLNCQTIDDgd 72
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEG-EELQASNIRD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 73 nwlpPEQRNIGMIFQDYALFPHLTVNQN-------VGFGLKDlsDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRV 145
Cdd:PRK13549 79 ----TERAGIAIIHQELALVKELSVLENiflgneiTPGGIMD--YDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 146 AIARSLAYKPDLLLLDEPFSNIdTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-218 |
4.34e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcQTIddgdnwlppeqrNIGM 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETV------------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALF-PHLTVNQNvgfgLKDLSDQQKKEKVQEMLELvhldeFG------DRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG0488 383 FDQHQEELdPDKTVLDE----LRDGAPGGTEQEVRGYLGR-----FLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKiFKkqGvTAIFVTHSREeaF--AFADKMAVMNHGVIEQY 218
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDD-FP--G-TVLLVSHDRY--FldRVATRILEFEDGGVREY 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-213 |
1.28e-22 |
|
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: 98.36 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP--------LSSGiMSLNCQTIDDgdnwlp 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiYWSG-SPLKASNIRD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRNIGMIFQDYALFPHLTVNQNVGFGLK------DLSDQQKKEKVQEMLELVHLDEFGDRYP-HQLSGGQQQRVAIAR 149
Cdd:TIGR02633 75 TERAGIVIIHQELTLVPELSVAENIFLGNEitlpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-228 |
1.56e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS-----SGIMSLNCQTIDDGDnwl 75
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHAS--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 ppEQR-------NIGMIFQD--YALFPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELvhLDEFGDR--------YPHQLS 138
Cdd:PRK15134 83 --EQTlrgvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNC--LDRVGIRqaakrltdYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQY 218
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250
....*....|
gi 490872517 219 GSASELYFHP 228
Cdd:PRK15134 239 NRAATLFSAP 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-224 |
1.63e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLkavaGLL-----PlSSGIMSLNCQTIDDgdnWlp 76
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLtrawdP-QQGEILLNGQPIAD---Y-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQ---RNIGMIFQDYALFPHlTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEF-------------GDRyphQLSGG 140
Cdd:PRK11160 408 SEAalrQAISVVSQRVHLFSA-TLRDNLLLAAPNASD----EALIEVLQQVGLEKLleddkglnawlgeGGR---QLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGS 220
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
|
....
gi 490872517 221 ASEL 224
Cdd:PRK11160 557 HQEL 560
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-224 |
1.80e-22 |
|
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: 98.25 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTI--LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqTIDDGDNWLPPEQRNI 82
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD--GHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHlTVNQNVGFGLKDlsdQQKKEKVQEMLELVHLDEFGDRYP---HQ--------LSGGQQQRVAIARSL 151
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTE---QADRAEIERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-228 |
1.82e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTidDGDNW--LPPEQR------NIGMIFQD--YALF 92
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEF--NGQDLqrISEKERrnlvgaEVAMIFQDpmTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 93 PHLTVNQNVGFGLKDLSDQQKKEKVQ---EMLELVHLDEFGDR---YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHQGGNKKTRRQraiDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 167 IDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-214 |
1.87e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 2 SCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDGDNWLPPEQR- 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-------KITVLGVPVPARARl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 ---NIGMIFQDYALFPHLTVNQN-VGFGLK-DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK13536 112 araRIGVVPQFDNLDLEFTVRENlLVFGRYfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 156 DLLLLDEPFSNIDTQVRHELISQIRKIFKKqGVTAIFVTHSREEAFAFADKMAVMNHGV 214
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-215 |
2.64e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.59 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGlLP---LSSGIMSLNCQTIDDgdnwLPPEQR- 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITD----LPPEERa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 --NIGMIFQDYALFPHLTVNQ-----NVGFglkdlsdqqkkekvqemlelvhldefgdryphqlSGGQQQRVAIARSLAY 153
Cdd:cd03217 76 rlGIFLAFQYPPEIPGVKNADflryvNEGF----------------------------------SGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 154 KPDLLLLDEPFSNIDTqVRHELISQIRKIFKKQGVTAIFVTHsREEAFAF--ADKMAVMNHGVI 215
Cdd:cd03217 122 EPDLAILDEPDSGLDI-DALRLVAEVINKLREEGKSVLIITH-YQRLLDYikPDRVHVLYDGRI 183
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-225 |
2.74e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 16 SQTILESLSLEVEHGEIVCLLGASGCGKTTllkaVAGLL-----PlSSGIMSLNCQTIDDGDN-WLppeQRNIGMIFQDY 89
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST----VAALLqnlyqP-TGGQVLLDGVPLVQYDHhYL---HRQVALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 ALFPHlTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLL 158
Cdd:TIGR00958 565 VLFSG-SVRENIAYGLTDTPD----EEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 159 LLDEPFSNIDTQVRHeLISQIRkifKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:TIGR00958 640 ILDEATSALDAECEQ-LLQESR---SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-220 |
2.79e-22 |
|
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: 92.86 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslnCQTIDDGDNWLPPEQ--- 79
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG-----KIEIDGIDISTIPLEdlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHlTVNQNVgfglkDLSDQQKKEKVQEMLELvhlDEFGDryphQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03369 82 SSLTIIPQDPTLFSG-TIRSNL-----DPFDEYSDEEIYGALRV---SEGGL----NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGS 220
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEF--TNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-247 |
3.73e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGI-----MSLNCQTIDDGDNWLPpE 78
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLE-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPhLTVNQNVGFGLKDLSDQQKKE---KVQEMLELVHL-DEFGDRY---PHQLSGGQQQRVAIARSL 151
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEfrgVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKqgVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSK 231
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
250
....*....|....*...
gi 490872517 232 FVADFLGG--GSYLNAQR 247
Cdd:PRK14271 257 ETARYVAGlsGDVKDAKR 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-224 |
7.73e-22 |
|
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: 96.35 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYE-SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGD--------NWL 75
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhtlrqfiNYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQrnigMIFQDyalfphlTVNQNVGFGLKDLSDQqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQR 144
Cdd:TIGR01193 554 PQEP----YIFSG-------SILENLLLGAKENVSQ---DEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKqgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-224 |
1.77e-21 |
|
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: 95.27 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPE--QRNIGMIFQDYALFpHL 95
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD----VTQAslRAAIGIVPQDTVLF-ND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPHQ-----------LSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:COG5265 447 TIAYNIAYGRPDASE----EEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 165 SNIDTQVRHELISQIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:COG5265 523 SALDSRTERAIQAALREV--ARGRTTLVIAH-RLSTIVDADEILVLEAGRIVERGTHAEL 579
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-230 |
2.12e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.68 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlsSGIMSLNCQTIDDGDNWLPPEQR--NIGMIFQD--YALFPHLTVN 98
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILP--AGVRQTAGRVLLDGKPVAPCALRgrKIATIMQNprSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVGFGLKDLSDQQKKEKVQEMLELVHLDEFG---DRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHEL 175
Cdd:PRK10418 100 THARETCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 176 ISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHPSS 230
Cdd:PRK10418 180 LDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-247 |
5.88e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.31 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYE--SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGdnwLPPEQRNIGM 84
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---LDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFyaQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 163 PFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHSREEAFAFADKMAVMNHGvieqygsasELYFHPSSKFVADFLGGGSY 242
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQG---------RLYCSGTPLFLKNCFGTGFY 1156
|
....*
gi 490872517 243 LNAQR 247
Cdd:TIGR01257 1157 LTLVR 1161
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-276 |
1.07e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDL-TCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqtiddgdNWLPPEQR---- 80
Cdd:COG4586 23 ALKGLfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL--------GYVPFKRRkefa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 -NIGMIF-QDYALFPHLTVNQNvgFGLK----DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:COG4586 95 rRIGVVFgQRSQLWWDLPAIDS--FRLLkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL--YFHPSSKF 232
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELkeRFGPYKTI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490872517 233 VADFlgggsylnAQRISELEFETSLGVVEAKPQT-EIEFGSACEL 276
Cdd:COG4586 253 VLEL--------AEPVPPLELPRGGEVIEREGNRvRLEVDPRESL 289
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-224 |
1.20e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLppEQRNIGMI 85
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 86 FQDYALFPHLTVNQNVGFG-------LKDLSdQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGrypwhgaLGRFG-AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-236 |
1.26e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP---LSSGIMSLNCQTIDdgdnwlPPEQRNI-GMIFQDYALFP 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPID------AKEMRAIsAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 94 HLTVNQNVGFGL-----KDLSDQQKKEKVQEMLELVHLDE-----FGDRYPHQ-LSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:TIGR00955 113 TLTVREHLMFQAhlrmpRRVTKKEKRERVDEVLQALGLRKcantrIGVPGRVKgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 163 PFSNIDTQVRHELISQIRKIFKKqGVTAIFVTHS-REEAFAFADKMAVMNHGVIEQYGSASELyfhpsSKFVADF 236
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA-----VPFFSDL 261
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-304 |
1.51e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 92.64 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 6 SIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSgimsLNCQTIDDGDNWLPPEQRNIGMI 85
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 86 FQDYALFPHLTVNQNVGFGL-----KDLSDQQK---KEKVQEMLELVHLDE--FGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSllrlpKSLTKQEKilvAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 156 DLLLLDEPFSNIDTQVRHELISQIRKIFKKQG--VTAIFVTHSReeAFAFADKMAVMNHG--VIEQYGSASELYFHpSSK 231
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKtiVTSMHQPSSR--VYQMFDSVLVLSEGrcLFFGKGSDAMAYFE-SVG 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 232 FVADF-LGGGSYLN--AQRISELEfetslGVVE-AKPQTEIEFGSACELLLRPQhIQASYEQDSaISVLEQQFMGDH 304
Cdd:PLN03211 303 FSPSFpMNPADFLLdlANGVCQTD-----GVSErEKPNVKQSLVASYNTLLAPK-VKAAIEMSH-FPQANARFVGSA 372
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-223 |
2.18e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.74 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlSSGIMSLNCQTIDDgdnWLPPEQ-RNIGMIFQDYALFPHLTVN 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSD---WSAAELaRHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVGFGLKDLSDQQKKEKVQEML-ELVHLDEFGDRYPHQLSGGQQQRVAIARSL-----AYKPD--LLLLDEPFSNIDtq 170
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 171 VRHE--LISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:COG4138 166 VAQQaaLDRLLRE-LCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-215 |
3.66e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYES-QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGdnwlpPEQ 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-----LQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQ----DYAlFPHLT-----VNQNVGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS 150
Cdd:PRK15056 78 NLVAYVPQseevDWS-FPVLVedvvmMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 151 LAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADkMAVMNHGVI 215
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-215 |
4.12e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.86 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYES-QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgdnwLPPEQR-- 80
Cdd:COG3845 257 VLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG----LSPRERrr 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 -NIGMIFQD---YALFPHLTVNQNVGFGLKDLSDQQK-----KEKVQEM-LELVhlDEFGDRYPH------QLSGGQQQR 144
Cdd:COG3845 333 lGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPPFSRggfldRKAIRAFaEELI--EEFDVRTPGpdtparSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNID----TQVRHELISQirkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-195 |
4.93e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGL--LPLSSGIMSLNCQTIDDgdnwLPPEQR-- 80
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILE----LSPDERar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 -NIGMIFQDYALFPHLTV--------NQNVGfglKDLSDQQKKEKVQEMLELVHLDE-FGDRYPHQ-LSGGQQQRVAIAR 149
Cdd:COG0396 77 aGIFLAFQYPVEIPGVSVsnflrtalNARRG---EELSAREFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490872517 150 SLAYKPDLLLLDEPFSNID---TQVRHELISQIRkifkKQGVTAIFVTH 195
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDidaLRIVAEGVNKLR----SPDRGILIITH 198
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-213 |
9.32e-20 |
|
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: 86.33 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAG-LLPLSSGIMslncqtIDDGDNWL-----PPEQ------RNIGMIFQ 87
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSIL------VRHDGGWVdlaqaSPREilalrrRTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 88 dyalF----PHLTVNQNVGFGLKDL--SDQQKKEKVQEMLELVHLDE-FGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:COG4778 101 ----FlrviPRVSALDVVAEPLLERgvDREEARARARELLARLNLPErLWDLPPATFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490872517 161 DEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:COG4778 177 DEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-213 |
1.04e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQrNIGM 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL-GIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQN--VG-------FGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK09700 85 IYQELSVIDELTVLENlyIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 156 DLLLLDEPFSNIdTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK09700 165 KVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-224 |
1.49e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 10 LTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLplssgimslncqTIDDGDNWLPPEQ---------- 79
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM------------TPAHGHVWLDGEHiqhyaskeva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHLTVNQNVGFGL---KDLSDQQKKEK---VQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARGRyphQPLFTRWRKEDeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-199 |
6.22e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 17 QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslnCQTIDDGDNWLPPEqrnigmifqdyalfphLT 96
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV-----AGCVDVPDNQFGRE----------------AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNVGfglkdlSDQQKKEKVqEMLELVHLdefGD-----RYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQV 171
Cdd:COG2401 102 LIDAIG------RKGDFKDAV-ELLNAVGL---SDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*...
gi 490872517 172 RHELISQIRKIFKKQGVTAIFVTHsREE 199
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATH-HYD 198
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-228 |
9.28e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.73 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT----ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlssgimslncqtiddgDNW------ 74
Cdd:COG4170 4 LDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK----------------DNWhvtadr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 75 ----------LPPEQR------NIGMIFQDyalfP--HLTVNQNVGFGLKDLSD------------QQKKEKVQEMLELV 124
Cdd:COG4170 68 frwngidllkLSPRERrkiigrEIAMIFQE----PssCLDPSAKIGDQLIEAIPswtfkgkwwqrfKWRKKRAIELLHRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 125 ----HLDEFgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRheliSQIRKIFKK----QGVTAIFVTHS 196
Cdd:COG4170 144 gikdHKDIM-NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQ----AQIFRLLARlnqlQGTSILLISHD 218
|
250 260 270
....*....|....*....|....*....|....*
gi 490872517 197 REEAFAFADKMAVMNHGVIEQYGSASELY---FHP 228
Cdd:COG4170 219 LESISQWADTITVLYCGQTVESGPTEQILkspHHP 253
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-197 |
3.02e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.53 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGdnwLPPEQRNIGM 84
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD---LCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFglkDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLY---DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|...
gi 490872517 165 SNIDTQVRHELISQIRKiFKKQGVTAIFVTHSR 197
Cdd:PRK13540 156 VALDELSLLTIITKIQE-HRAKGGAVLLTSHQD 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
3.24e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqtiddgdnwLPPEQR 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPH--LTVNQnvgfgLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK09544 68 RIGYVPQKLYLDTTlpLTVNR-----FLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 159 LLDEPFSNIDT--QVR-HELISQIRKIFkkqGVTAIFVTHSREEAFAFADKMAVMNH 212
Cdd:PRK09544 143 VLDEPTQGVDVngQVAlYDLIDQLRREL---DCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-215 |
3.44e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI---------DDGDNWLPpEQRNIGMIFQDYAL-- 91
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInalstaqrlARGLVYLP-EDRQSSGLYLDAPLaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 92 -FPHLTVNQNvGFGLKDLSDQQKKEKVQEML--ELVHLDEFGDRyphqLSGGQQQRVAIARSLAYKPDLLLLDEPFSNID 168
Cdd:PRK15439 361 nVCALTHNRR-GFWIKPARENAVLERYRRALniKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490872517 169 TQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK15439 436 VSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-219 |
7.61e-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: 80.38 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS---SGIMSLNCQTIDDGDNwlpPEQRNIGMIFQDYALFPH 94
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE---KYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 LTVNQNVGFGLKDLsdqqkkekvqemlelvhldefGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHE 174
Cdd:cd03233 98 LTVRETLDFALRCK---------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490872517 175 LISQIRKIFKKQGVTAIF-VTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03233 157 ILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-173 |
8.51e-18 |
|
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: 80.98 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDN-WLppeQRNIGMIFQDYALFPHlTV 97
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHkYL---HSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:cd03248 105 QDNIAYGLQSCSF----ECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
....*..
gi 490872517 167 IDTQVRH 173
Cdd:cd03248 181 LDAESEQ 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-215 |
1.93e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTID-----DG-DNwlppeqrNIGMIFQDY---A 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqDGlAN-------GIVYISEDRkrdG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 91 LFPHLTVNQNVGF-GLKDLSDQ----QKKEKVQEMLELVHLdeFGDRYPHQ------LSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK10762 341 LVLGMSVKENMSLtALRYFSRAggslKHADEQQAVSDFIRL--FNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 160 LDEPFSNIDTQVRHE---LISQirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK10762 419 LDEPTRGVDVGAKKEiyqLINQ----FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-228 |
2.14e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDG--DNWlppeQRN 81
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqlDSW----RSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHlTVNQNVGFGLKDLSDQQKKEKVQemLELVHLD----------EFGDRyPHQLSGGQQQRVAIARSL 151
Cdd:PRK10789 391 LAVVSQTPFLFSD-TVANNIALGRPDATQQEIEHVAR--LASVHDDilrlpqgydtEVGER-GVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQW--GEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-213 |
3.36e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSS--GIMSLN---CQ--TIDDGdnwlppEQRNIGMIFQDYALF 92
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDgevCRfkDIRDS------EALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 93 PHLTVNQNVgFglkdLSDQQKKEKV----------QEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:NF040905 91 PYLSIAENI-F----LGNERAKRGVidwnetnrraRELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 163 PFSNI---DTQVRHELISQirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:NF040905 166 PTAALneeDSAALLDLLLE----LKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-216 |
3.58e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 82.15 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDgDNWlpPEQRN-IGMIFQDYALFPHLtvnqnv 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-DNR--EAYRQlFSAVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 102 gFGLKDLSDQqkkEKVQEMLELVHLDE--------FGDRyphQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR- 172
Cdd:COG4615 422 -LGLDGEADP---ARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRr 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490872517 173 ---HELISQirkiFKKQGVTAIFVTHSrEEAFAFADKMAVMNHGVIE 216
Cdd:COG4615 495 vfyTELLPE----LKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-223 |
4.87e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlSSGIMSLNCQTIDDGD--------NWLPPEQRN-IGM-IFQDY 89
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSaaelarhrAYLSQQQTPpFAMpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 90 ALfpHLTVNQNVGFGLKDLSdqqkkekvqEMLELVHLDEFGDRYPHQLSGGQQQRVAIARS-LAYKPD------LLLLDE 162
Cdd:PRK03695 91 TL--HQPDKTRTEAVASALN---------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 163 PFSNID-TQVrhELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PRK03695 160 PMNSLDvAQQ--AALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-225 |
1.08e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.56 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQT---ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLssgiMSLNCQTIDDGDNWLPpeqr 80
Cdd:PLN03232 614 AISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH----AETSSVVIRGSVAYVP---- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFqdyalfpHLTVNQNVGFGLKDLSDQQKKE----KVQEMLELV---HLDEFGDRYPHqLSGGQQQRVAIARSLAY 153
Cdd:PLN03232 686 QVSWIF-------NATVRENILFGSDFESERYWRAidvtALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKiFKKQGVTAIFVThSREEAFAFADKMAVMNHGVIEQYGSASELY 225
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-220 |
1.19e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS--------SGIMSLNCQTIDDGD---- 72
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 73 ---NWLPPEQRNIGMIFQDYAL-----FPHLTVNQNVGFGLKDLSDQQkkekvqemLELVHLDEFGDRYPHQLSGGQQQR 144
Cdd:PRK13547 82 arlRAVLPQAAQPAFAFSAREIvllgrYPHARRAGALTHRDGEIAWQA--------LALAGATALVGRDVTTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 145 VAIARSLAY---------KPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK13547 154 VQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
....*
gi 490872517 216 EQYGS 220
Cdd:PRK13547 234 VAHGA 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-224 |
1.42e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.39 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLkavaGLL-----PlSSGIMSLNcqTIDDGDNWLPPEQRNIGMIFQDYALFPH 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLqrvfdP-QSGRILID--GTDIRTVTRASLRRNIAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 lTVNQNVGFGLKDLSDqqkkEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK13657 424 -SIEDNIRVGRPDATD----EEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 164 FSNID--TQVR-HELISQIRKifkkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK13657 499 TSALDveTEAKvKAALDELMK-----GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-224 |
1.75e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.45 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTI--LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwLPPEQRNI 82
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFpHLTVNQNVGFGLKDlsdQQKKEKVQEMLELVHLDEFGDRYPH-----------QLSGGQQQRVAIARSL 151
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYARTE---QYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-195 |
2.67e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.43 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlppEQRNIGM 84
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-----RSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFgLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHF-LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190
....*....|....*....|....*....|....*
gi 490872517 165 SNID----TQVRHELISQIRKifkkqGVTAIFVTH 195
Cdd:PRK13543 166 ANLDlegiTLVNRMISAHLRG-----GGAALVTTH 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-224 |
7.66e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 1 MSCALSIKDLTCKY-ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG--------IMSLNCQTIDDG 71
Cdd:PRK10790 337 QSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGeirldgrpLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 72 dnwlppeqrnIGMIFQDYALFPHlTVNQNVGFGlKDLSDqqkkEKVQEMLELVHLDEFGDRYP-----------HQLSGG 140
Cdd:PRK10790 417 ----------VAMVQQDPVVLAD-TFLANVTLG-RDISE----EQVWQALETVQLAELARSLPdglytplgeqgNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGS 220
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
....
gi 490872517 221 ASEL 224
Cdd:PRK10790 558 HQQL 561
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-255 |
1.30e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.03 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS------SGIMSLNCQTiddgdNWLPPEqrnigmifqdyalf 92
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkikhSGRISFSPQT-----SWIMPG-------------- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 93 phlTVNQNVGFGLKdlSDQQKKEKVqemLELVHLDEFGDRYPHQ-----------LSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:TIGR01271 502 ---TIKDNIIFGLS--YDEYRYTSV---IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 162 EPFSNIDTQVRHELI-SQIRKIFKKQgvTAIFVThSREEAFAFADKMAVMNHGVIEQYGSASELYfHPSSKFVADFLGGG 240
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFeSCLCKLMSNK--TRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQ-AKRPDFSSLLLGLE 649
|
250
....*....|....*..
gi 490872517 241 SY--LNAQRISELEFET 255
Cdd:TIGR01271 650 AFdnFSAERRNSILTET 666
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-224 |
1.73e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYES---QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlssgIMSLNCQTIDDGDNWLPpeqr 80
Cdd:PLN03130 614 AISIKNGYFSWDSkaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP----PRSDASVVIRGTVAYVP---- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFqdyalfpHLTVNQNVGFGLKdlSDQQKKEKVQEMLELVH---------LDEFGDRYPHqLSGGQQQRVAIARSL 151
Cdd:PLN03130 686 QVSWIF-------NATVRDNILFGSP--FDPERYERAIDVTALQHdldllpggdLTEIGERGVN-ISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRhelisqiRKIFKK------QGVTAIFVThSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVG-------RQVFDKcikdelRGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-224 |
2.68e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTI-LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRN-I 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ---PEDYRKlF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLtvnqnvgfgLKDLSDQQKKEKVQ---EMLELVH-LDEFGDRYPH-QLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK10522 400 SAVFTDFHLFDQL---------LGPEGKPANPALVEkwlERLKMAHkLELEDGRISNlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSrEEAFAFADKMAVMNHGVI-EQYGSASEL 224
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLsELTGEERDA 537
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-195 |
3.71e-15 |
|
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: 76.33 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 15 ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTID-DGDNWLPPEQRNIGM-IFQDYALF 92
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPaKGKLFYVPQRPYMTLgTLRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 93 PHlTVNQnvgFGLKDLSDQQkkekVQEMLELVHLDEFGDR---------YPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:TIGR00954 538 PD-SSED---MKRRGLSDKD----LEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 490872517 164 FSNIDTQVRHELISQIRKIfkkqGVTAIFVTH 195
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-223 |
4.35e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRNIGMIF-----QDYALFPHLTV 97
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS---PLDAVKKGMAYitesrRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 98 NQNVG-------------FGLKDLSDQQK-KEKVQEMLELVHLDEfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK09700 359 AQNMAisrslkdggykgaMGLFHEVDEQRtAENQRELLALKCHSV--NQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 164 FSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-182 |
5.35e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.30 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLT----CKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP---LSSGIMSLNCQTIDDGdnwlppEQR 80
Cdd:TIGR00956 763 RNLTyevkIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSS------FQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQDYALFPHLTVNQNVGFGL-----KDLSDQQKKEKVQEMLELVHLDEFGDRY---PHQ-LSGGQQQRVAIARSL 151
Cdd:TIGR00956 837 SIGYVQQQDLHLPTSTVRESLRFSAylrqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVEL 916
|
170 180 190
....*....|....*....|....*....|..
gi 490872517 152 AYKPDLLL-LDEPFSNIDTQVRHELISQIRKI 182
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-224 |
5.70e-15 |
|
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: 74.12 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKY--ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSlncqtidDGDNW----LPPE 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQI-------DGVSWnsvpLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPHlTVNQNVgfglkDLSDQQKKEKVQEMLELVHLDEFGDRYPHQ-----------LSGGQQQRVAI 147
Cdd:cd03289 76 RKAFGVIPQKVFIFSG-TFRKNL-----DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTQVrhelISQIRKIFKK--QGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPIT----YQVIRKTLKQafADCTVILSEH-RIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-213 |
7.52e-15 |
|
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: 72.75 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcQTIDDGDNWLPPEQRNIGMIfqDYA----LFPHL 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS-NKNESEPSFEATRSRNRYSV--AYAaqkpWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGlkDLSDQQKKEKVQEMLEL---VHLDEFGDRYPH-----QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNI 167
Cdd:cd03290 94 TVEENITFG--SPFNKQRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490872517 168 DTQVRHELISQ-IRKIFKKQGVTAIFVTHsREEAFAFADKMAVMNHG 213
Cdd:cd03290 172 DIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-213 |
9.55e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQT---------IDDGdnwlppeqrnIGMIFQDYA 90
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaaLAAG----------VAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 91 LFPHLTVNQNV-------GFGLKDlsdqQKKEKVQEMLELVHLDEfgDRYPHQ----LSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK11288 90 LVPEMTVAENLylgqlphKGGIVN----RRLLNYEAREQLEHLGV--DIDPDTplkyLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-232 |
1.32e-14 |
|
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: 75.05 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYE--SQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIddgdnwlppeQRNI 82
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----------LTNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFPHLTVNQNVGFGLKDL--------SDQQKKEKVQEM-LELVHLDEFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLylyarlrgVPAEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 154 KPDLLLLDEPFSNIDTQVRHELISQIRKIFkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASelyfHPSSKF 232
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ----HLKSKF 2161
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-208 |
1.76e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 25 LEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTI-----DDgdnwlPPeqRNI-GMIFqDYalfphltvn 98
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqQD-----PP--RNVeGTVY-DF--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 qnVGFGLKDLSDQQKK--------------------EKVQEMLELVHLDEFGDRY----------PHQ----LSGGQQQR 144
Cdd:PRK11147 87 --VAEGIEEQAEYLKRyhdishlvetdpseknlnelAKLQEQLDHHNLWQLENRInevlaqlgldPDAalssLSGGWLRK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNIDTqvrhELISQIRKIFKKQGVTAIFVTHSReeafAFADKMA 208
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDR----SFIRNMA 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-232 |
1.81e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIddGDNWLPPEQRNIGMIFQDYALFPHlTVN 98
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVgfglkDLSDQQKKEKVQEMLELVHLDEF---------------GDRYphqlSGGQQQRVAIARSLAYK-PDLLLLDE 162
Cdd:PTZ00243 1402 QNV-----DPFLEASSAEVWAALELVGLRERvasesegidsrvlegGSNY----SVGQRQLMCMARALLKKgSGFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 163 PFSNIDTQVRHELISQIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKF 232
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAF--SAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-195 |
1.81e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEI-----VCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcQTIddgdNWLPpeQRnigmIFQDYalfpH 94
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI----SYKP--QY----IKPDY----D 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 LTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLdefGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHE 174
Cdd:PRK13409 415 GTVEDLLRSITDDLGSSYYKSEIIKPLQLERL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180
....*....|....*....|.
gi 490872517 175 LISQIRKIFKKQGVTAIFVTH 195
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDH 512
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-224 |
2.55e-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: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIM------SLNCQTiddgdNWLPPEqrnigmifqdyalf 92
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgriSFSSQF-----SWIMPG-------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 93 phlTVNQNVGFGLKdlSDQQKKEKVqemLELVHLDEFGDRYPHQ-----------LSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03291 113 ---TIKENIIFGVS--YDEYRYKSV---VKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 162 EPFSNIDTQVRHELI-SQIRKIFKKQgvTAIFVThSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:cd03291 185 SPFGYLDVFTEKEIFeSCVCKLMANK--TRILVT-SKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-224 |
2.65e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMSLncqtidDGD---------- 72
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrVEVL------GGDmadarhrrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 73 ----NWLPpeQ---RNigmifqdyaLFPHLTVNQNVGF--GLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQ 143
Cdd:NF033858 75 cpriAYMP--QglgKN---------LYPTLSVFENLDFfgRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 144 RVAIARSLAYKPDLLLLDEPFSNIDTQVRH---ELISQIRKifKKQGVTAIFVTHSREEAFAFaDKMAVMNHGVIEQYGS 220
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGT 220
|
....
gi 490872517 221 ASEL 224
Cdd:NF033858 221 PAEL 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-222 |
3.50e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAG--LLPLSSGIMSLNCQTIDDgdnwLPPEQRN- 81
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILD----LEPEERAh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 --IGMIFQ--------DYALFPHLTVNQNVGF-GLKDLSDQQKKEKVQEMLELVHLDE-FGDRYPHQ-LSGGQQQRVAIA 148
Cdd:CHL00131 84 lgIFLAFQypieipgvSNADFLRLAYNSKRKFqGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHElISQIRKIFKKQGVTAIFVTH-SREEAFAFADKMAVMNHGVIEQYGSAS 222
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKI-IAEGINKLMTSENSIILITHyQRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-200 |
4.86e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS-------------SGimslncQTIDDgdn 73
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrrgSG------ETIWD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 74 wlppEQRNIGM----IFQDYalfphlTVNQNV------GF----GL-KDLSDQQKKeKVQEMLELVHLDEFGDRYP-HQL 137
Cdd:PRK10938 334 ----IKKHIGYvsssLHLDY------RVSTSVrnvilsGFfdsiGIyQAVSDRQQK-LAQQWLDILGIDKRTADAPfHSL 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 138 SGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRhELISQIRKIFKKQGVTA-IFVTHSREEA 200
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVDVLISEGETQlLFVSHHAEDA 465
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-264 |
5.14e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.44 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqtiddGDNWLPPEQrnigmifqdyALFPHLTVNQ 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK------GSVAYVPQQ----------AWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFGlKDLSDQQKKEKVQ--------EMLELVHLDEFGDRYPHqLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQV 171
Cdd:TIGR00957 718 NILFG-KALNEKYYQQVLEacallpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 172 -RHELISQIRKIFKKQGVTAIFVTHSReEAFAFADKMAVMNHGVIEQYGSASELYFHPSSkfVADFLggGSYLNAQRISE 250
Cdd:TIGR00957 796 gKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQRDGA--FAEFL--RTYAPDEQQGH 870
|
250
....*....|....*...
gi 490872517 251 LEFETSLGVV----EAKP 264
Cdd:TIGR00957 871 LEDSWTALVSgegkEAKL 888
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-197 |
1.23e-13 |
|
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: 71.50 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGllplssgimslncqtID---DGDNWLPPEqRNIGMIFQDYALFPHL 95
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------------VDkdfNGEARPQPG-IKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNVGFGLKDLSDQQKK----------------------EKVQEMLELVHLDEF---------------GDRYPHQLS 138
Cdd:TIGR03719 84 TVRENVEEGVAEIKDALDRfneisakyaepdadfdklaaeqAELQEIIDAADAWDLdsqleiamdalrcppWDADVTKLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDTqvrhELISQIRKIFKKQGVTAIFVTHSR 197
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHDR 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-224 |
1.26e-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: 72.25 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES--QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPlSSGIMSLncqtidDGDNW----LPPE 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI------DGVSWnsvtLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 79 QRNIGMIFQDYALFPHlTVNQNVgfglkDLSDQQKKEKVQEMLELVHLDEFGDRYPHQ-----------LSGGQQQRVAI 147
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSG-TFRKNL-----DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDTqVRHELisqIRKIFKK--QGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDP-VTLQI---IRKTLKQsfSNCTVILSEH-RVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-227 |
1.37e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.46 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDL---TCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDgdnwlppeQRNIG 83
Cdd:PRK13545 24 LKDLffrSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG-------TVDI--------KGSAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVgfGLKDLSDQQKKEKVQEMLELVhlDEFGD--RYPHQ----LSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK13545 89 LIAISSGLNGQLTGIENI--ELKGLMMGLTKEKIKEIIPEI--IEFADigKFIYQpvktYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 158 LLLDEPFSNIDTQVRHELISQIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFH 227
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-254 |
1.38e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDNW---LPPEQRNIGMIFQDYALFphl 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI-----MIDDCDVAkfgLTDLRRVLSIIPQSPVLF--- 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 tvNQNVGFGLKDLSDQQKKEkVQEMLELVHLDEFGDRYPHQL-----------SGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PLN03232 1323 --SGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 165 SNIDTQVRHELISQIRKIFKKqgVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELYFHPSSKFVADFLGGGSyLN 244
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP-AN 1475
|
250
....*....|
gi 490872517 245 AQRISELEFE 254
Cdd:PLN03232 1476 AQYLSNLVFE 1485
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
80-224 |
2.00e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 RNIGMIFQDYALFPHLTVNQNVGFGLKDLSdqqkKEKVQEMLELVHLDEFGDRYPHQ-----------LSGGQQQRVAIA 148
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGKEDAT----REDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIA 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHsREEAFAFADKMAVMNH-----GVIEQYGSASE 223
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNNpdrtgSFVQAHGTHEE 1449
|
.
gi 490872517 224 L 224
Cdd:PTZ00265 1450 L 1450
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-198 |
2.15e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 4 ALSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqtiddgdNWlpPEQRNIG 83
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KW--SENANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYAL-FPH-LTvnqnvgfgLKDLSDQQKKEK-----VQEMLE--LVHLDEFGdRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK15064 386 YYAQDHAYdFENdLT--------LFDWMSQWRQEGddeqaVRGTLGrlLFSQDDIK-KSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490872517 155 PDLLLLDEPFSNIDTqvrhELISQIRKIFKKQGVTAIFVTHSRE 198
Cdd:PRK15064 457 PNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDRE 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
2.77e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 21 ESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDnwlPPEQRNIGMIF------QDyALFPH 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS---PRDAIRAGIMLcpedrkAE-GIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 LTVNQNVG---------FGLKdLSDQQKKEKVQEMLELVHLDEfgdRYPHQ----LSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK11288 346 HSVADNINisarrhhlrAGCL-INNRWEAENADRFIRSLNIKT---PSREQlimnLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490872517 162 EPFSNIDTQVRHElISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK11288 422 EPTRGIDVGAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-224 |
3.40e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.76 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 107 DLSDQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFkKQ 186
Cdd:NF000106 115 DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RD 193
|
90 100 110
....*....|....*....|....*....|....*...
gi 490872517 187 GVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASEL 224
Cdd:NF000106 194 GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-195 |
5.40e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHG-----EIVCLLGASGCGKTTLLKAVAGLLplssgimslncqTIDDGdnWLPPE-------QRnigmIFQ 87
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVL------------KPDEG--EVDEDlkisykpQY----ISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 88 DYalfpHLTVNQNVGFGLKD-LSDQQKKEKVQEMLELVHLdefGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:COG1245 413 DY----DGTVEEFLRSANTDdFGSSYYKTEIIKPLGLEKL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180
....*....|....*....|....*....
gi 490872517 167 IDTQVRHELISQIRKIFKKQGVTAIFVTH 195
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-224 |
1.01e-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: 69.20 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncQTIDDGDN----WLPPEQRNIGMIFQDYALFPH 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG------EIIIDGLNiakiGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 lTVNQNVgfglkDLSDQQKKEKVQEMLELVHLDEFGDRYP----HQ-------LSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:TIGR00957 1375 -SLRMNL-----DPFSQYSDEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 164 FSNIDTQVRHELISQIRKIFkkQGVTAIFVTHSREEAFAFAdKMAVMNHGVIEQYGSASEL 224
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-222 |
1.06e-12 |
|
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: 67.05 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHG-----EIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDdgdnwLPPEQrnigmIFQDYALfph 94
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-----YKPQY-----IKADYEG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 lTVNQNVGFGLKDL-SDQQKKEKVQEMLELvhlDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRH 173
Cdd:cd03237 77 -TVRDLLSSITKDFyTHPYFKTEIAKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490872517 174 ELISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNhGVIEQYGSAS 222
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVAN 200
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-182 |
1.58e-12 |
|
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: 65.34 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 3 CALSIKDLT----CKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAG--LLPLSSGIMSLNCQTIDdgdnwlP 76
Cdd:cd03232 2 SVLTWKNLNytvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRNIGMIFQDYALFPHLTVNQNVGFG--LKDLSDQQKKekvqemlelvhldefgdryphqlsggqqqRVAIARSLAYK 154
Cdd:cd03232 76 NFQRSTGYVEQQDVHSPNLTVREALRFSalLRGLSVEQRK-----------------------------RLTIGVELAAK 126
|
170 180
....*....|....*....|....*...
gi 490872517 155 PDLLLLDEPFSNIDTQVRHELISQIRKI 182
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-228 |
2.22e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQ----TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLlplssgimslncqtidDGDNW------ 74
Cdd:PRK15093 4 LDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV----------------TKDNWrvtadr 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 75 ----------LPPEQR------NIGMIFQD--YALFPHLTVNQNV-----GFGLKDLSDQQKKEKVQEMLELVHLDEFGD 131
Cdd:PRK15093 68 mrfddidllrLSPRERrklvghNVSMIFQEpqSCLDPSERVGRQLmqnipGWTYKGRWWQRFGWRKRRAIELLHRVGIKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 132 R------YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIFVTHSREEAFAFAD 205
Cdd:PRK15093 148 HkdamrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWAD 227
|
250 260
....*....|....*....|...
gi 490872517 206 KMAVMNHGVIEQYGSASELYFHP 228
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-236 |
3.79e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqtiddGDnwlppeqrnIGMIFQDYALFPHLTVNQ 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN------GE---------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFGLKDLSDQQK--KEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELIS 177
Cdd:PRK13546 105 NIEFKMLCMGFKRKeiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 178 QIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGSASELYFHpSSKFVADF 236
Cdd:PRK13546 185 KIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDF 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-199 |
3.97e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.16 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 29 HGEIVCLLGASGCGKTTLLKAVAGLL-PLSSGIMSLNCQTIddgdnwlppeqrnigmifqdyalfphltvnqnvgfglkd 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 108 lsdqqkkekvQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQ- 186
Cdd:smart00382 42 ----------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLl 111
|
170
....*....|....*..
gi 490872517 187 ----GVTAIFVTHSREE 199
Cdd:smart00382 112 ksekNLTVILTTNDEKD 128
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-213 |
8.95e-12 |
|
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: 66.00 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT---ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLS-SGIMSLNCQTIDDgDNWLPPEQR 80
Cdd:TIGR02633 258 LEARNLTCWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDI-RNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 NIGMIFQD---YALFPHLTVNQNVGF-------GLKDLSDQQKKEKVQEMLELVHLDEFGDRYP-HQLSGGQQQRVAIAR 149
Cdd:TIGR02633 337 GIAMVPEDrkrHGIVPILGVGKNITLsvlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 150 SLAYKPDLLLLDEPFSNIDTQVRHElISQIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYE-IYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-182 |
1.03e-11 |
|
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: 64.31 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 30 GEIVCLLGASGCGKTTLLKAVAG-LLPlssgimslNCQTIDDGDNWLPPEQRNIGMIFQDY------------------A 90
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGkLKP--------NLGKFDDPPDWDEILDEFRGSELQNYftkllegdvkvivkpqyvD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 91 LFPHlTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLDefgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQ 170
Cdd:cd03236 98 LIPK-AVKGKVGELLKKKDERGKLDELVDQLELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170
....*....|....*....
gi 490872517 171 VR-------HELISQIRKI 182
Cdd:cd03236 174 QRlnaarliRELAEDDNYV 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-223 |
1.28e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 15 ESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqtiddgdnWlppEQRNIGMIFQDyALFPH 94
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------------W---AERSIAYVPQQ-AWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 95 LTVNQNVGFglkdlSDQQKKEKVQEMLELVHLD------------EFGDRYPHqLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:PTZ00243 735 ATVRGNILF-----FDEEDAARLADAVRVSQLEadlaqlgggletEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490872517 163 PFSNIDTQVRHELisqIRKIF--KKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PTZ00243 809 PLSALDAHVGERV---VEECFlgALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-213 |
1.73e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMSLNCQTIDDGdnwlpP---EQRNIGMIFQDYALFPHL 95
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsILYLGKEVTFNG-----PkssQEAGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 96 TVNQNV--------GFGLKDLsdQQKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNI 167
Cdd:PRK10762 95 TIAENIflgrefvnRFGRIDW--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490872517 168 -DTQVRhELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK10762 173 tDTETE-SLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-215 |
1.87e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQT---ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLP-LSSGIMSLNCQTIDDGDnwlpPEQ- 79
Cdd:PRK13549 260 LEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRN----PQQa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 80 --RNIGMIFQD---YALFPHLTVNQNVGfgLKDLSDQQKKEKVQEMLELVHLDEFGDR------YPHQ----LSGGQQQR 144
Cdd:PRK13549 336 iaQGIAMVPEDrkrDGIVPVMGVGKNIT--LAALDRFTGGSRIDDAAELKTILESIQRlkvktaSPELaiarLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHE---LISQirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEiykLINQ----LVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-237 |
2.65e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 18 TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVA----GLLPLSSGIMSLNCQTIDDGDNWLPPEQRNIGmifQDYALFP 93
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNA---ETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 94 HLTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLDEF---------------GDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVymatyglshtrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIFKKQGVTAiFVT--HSREEAFAFADKMAVMNHGVIEQYGSASEL--YFH------P 228
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTP-LVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqYFEkmgfkcP 310
|
....*....
gi 490872517 229 SSKFVADFL 237
Cdd:TIGR00956 311 DRQTTADFL 319
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-213 |
2.84e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKyeSQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQT---------IDDGDNWL 75
Cdd:PRK10982 251 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnaneaINHGFALV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 PPEQRNIGMIFQDYALFPHLTVNQN---VGFGLkdLSDQQKKEKVQEMLELVHLDEFGDRYP-HQLSGGQQQRVAIARSL 151
Cdd:PRK10982 329 TEERRSTGIYAYLDIGFNSLISNIRnykNKVGL--LDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 152 AYKPDLLLLDEPFSNIDTQVRHE---LISQIRKifKKQGVtaIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEiyqLIAELAK--KDKGI--IIISSEMPELLGITDRILVMSNG 467
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-172 |
8.04e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.66 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 17 QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMSLNCQTiddgDNWLPPEQRNIGmifQDYALFPHL 95
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGnIYYKNCNI----NNIAKPYCTYIG---HNLGLKLEM 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 96 TVNQNVGFGLKDLSdqqKKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK13541 86 TVFENLKFWSEIYN---SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-210 |
1.83e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 16 SQTILESL-SLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimSLNC-------------QTIDDgDNWlppEQRN 81
Cdd:PRK10938 14 SDTKTLQLpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSqfshitrlsfeqlQKLVS-DEW---QRNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 82 IGMIFQDYALFPHlTVNQNVGFGLKDlsdqqkKEKVQEMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK10938 88 TDMLSPGEDDTGR-TTAEIIQDEVKD------PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490872517 162 EPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-163 |
2.35e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLlplssgimslncQTIDDGDNWLPPEQRnIGMIFQDYALFPHLTVN 98
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------------DKEFEGEARPAPGIK-VGYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 99 QNVGFGLKDLSDQQKK---------EKVQEMLELvhLDEFGD------------------------RYPH------QLSG 139
Cdd:PRK11819 89 ENVEEGVAEVKAALDRfneiyaayaEPDADFDAL--AAEQGElqeiidaadawdldsqleiamdalRCPPwdakvtKLSG 166
|
170 180
....*....|....*....|....
gi 490872517 140 GQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-213 |
3.07e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 20 LESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDDGDNWLPPEQrNIGMIFQDYALFPHLTVNQ 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN-GISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 100 NVGFG---LKDL-SDQQKKEKVQEMLelvhLDEFG-DRYPHQ----LSGGQQQRVAIARSLAYKPDLLLLDEPFSNI-DT 169
Cdd:PRK10982 93 NMWLGrypTKGMfVDQDKMYRDTKAI----FDELDiDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490872517 170 QVRHeLISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK10982 169 EVNH-LFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-212 |
9.07e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 19 ILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLL-PLSSGIMSLNCQTIDDGD-NWLppeQRNIGMIFQDYALFPHlT 96
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIINDSHNLKDINlKWW---RSKIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 97 VNQNVGFGL-----------------------------------KDLSDQQKKEKVQEMLE------------------- 122
Cdd:PTZ00265 476 IKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcaGDLNDMSNTTDSNELIEmrknyqtikdsevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 123 -LVH--LDEFGDRY-------PHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQGVTAIF 192
Cdd:PTZ00265 556 vLIHdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
250 260
....*....|....*....|
gi 490872517 193 VTHsREEAFAFADKMAVMNH 212
Cdd:PTZ00265 636 IAH-RLSTIRYANTIFVLSN 654
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-168 |
9.42e-10 |
|
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: 59.80 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 30 GEIVCLLGASGCGKTTLLKAVAGLLplssgIMSLncqtiddGDNWLPPEQRNI-----GMIFQDYalFPHLtVNQNVGFG 104
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGEL-----KPNL-------GDYDEEPSWDEVlkrfrGTELQDY--FKKL-ANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 105 LK----DLSDQQKKEKVQEMLELVhlDEFG---------------DRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:COG1245 164 HKpqyvDLIPKVFKGTVRELLEKV--DERGkldelaeklglenilDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
...
gi 490872517 166 NID 168
Cdd:COG1245 242 YLD 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-218 |
1.21e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 7 IKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimSLNCQTiddgdnwlppeQRNIGMiF 86
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG--RIHCGT-----------KLEVAY-F 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 87 QDY--ALFPHLTVNQNVGFGLKDLSDQQKKEKVqemleLVHLDEF-----GDRYP-HQLSGGQQQRVAIARsLAYKP-DL 157
Cdd:PRK11147 388 DQHraELDPEKTVMDNLAEGKQEVMVNGRPRHV-----LGYLQDFlfhpkRAMTPvKALSGGERNRLLLAR-LFLKPsNL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 158 LLLDEPFSNIDTQVRhELISQIrkIFKKQGvTAIFVTHSReeafAFADKmAVMN------HGVIEQY 218
Cdd:PRK11147 462 LILDEPTNDLDVETL-ELLEEL--LDSYQG-TVLLVSHDR----QFVDN-TVTEcwifegNGKIGRY 519
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-232 |
7.54e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 2 SCALSIKDLTCKYESQ--TILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDGDN---WLP 76
Cdd:PLN03130 1235 SGSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI-----LIDGCDIskfGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 77 PEQRNIGMIFQDYALFphltvNQNVGFGLkDLSDQQKKEKVQEMLELVHLDEFGDRYPHQL-----------SGGQQQRV 145
Cdd:PLN03130 1310 DLRKVLGIIPQAPVLF-----SGTVRFNL-DPFNEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLL 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 146 AIARSLAYKPDLLLLDEPFSNIDtqVRHELISQ--IRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASE 223
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVD--VRTDALIQktIREEFK--SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPEN 1458
|
....*....
gi 490872517 224 LYFHPSSKF 232
Cdd:PLN03130 1459 LLSNEGSAF 1467
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-168 |
7.90e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGL--LPLSSGIMSLNCQTIDDgdnwLPPEQR-- 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLE----LSPEDRag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 81 -NIGMIFQDYALFPHLTvNQnvgFGLKDLSDQQKKEKVQEMLELVHLDEFGDRYPHQL---------------SGGQQQR 144
Cdd:PRK09580 78 eGIFMAFQYPVEIPGVS-NQ---FFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKR 153
|
170 180
....*....|....*....|....
gi 490872517 145 VAIARSLAYKPDLLLLDEPFSNID 168
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLD 177
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-168 |
1.27e-08 |
|
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: 56.10 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGimslncqTIDDGdnwlppEQRNIGM 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG-------TIEIG------ETVKLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDY-ALFPHLTVNQNVGFGLKDL--------------------SDQQKKEKvqemlelvhldefgdryphQLSGGQQQ 143
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEISGGLDIIklgkreipsrayvgrfnfkgSDQQKKVG-------------------QLSGGERN 450
|
170 180
....*....|....*....|....*
gi 490872517 144 RVAIARSLAYKPDLLLLDEPFSNID 168
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-195 |
2.15e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 30 GEIVCLLGASGCGKTTLLKAVAG-LLPlssgimslNCQTIDDGDNWLPPEQRNIGMIFQDYalfphltvnqnvgfgLKDL 108
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGeLIP--------NLGDYEEEPSWDEVLKRFRGTELQNY---------------FKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 109 SDQQKK--EKVQ---------------------------EMLELVHLDEFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13409 156 YNGEIKvvHKPQyvdlipkvfkgkvrellkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 490872517 160 LDEPFSNIDTQVRHELISQIRKIFKKQGVtaIFVTH 195
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEH 269
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
135-206 |
3.78e-08 |
|
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: 51.98 E-value: 3.78e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 135 HQLSGGQQQRVAIARSLA---YKPD-LLLLDEPFSNIDTQVRHELISQIRKIFKKqGVTAIFVTHsREEAFAFADK 206
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITH-LPELAELADK 149
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-223 |
5.26e-08 |
|
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: 52.19 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 26 EVEHGEIVCLLGASGCGKTTLLKAVAGLLplssgimslncQTIDDGDNWlppeqrnigmifqdyalfPHLTVNQnvgfgl 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------IPNGDNDEW------------------DGITPVY------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 106 kdlsdqqKKEKVQemlelvhldefgdryphqLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKK 185
Cdd:cd03222 66 -------KPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180 190
....*....|....*....|....*....|....*...
gi 490872517 186 QGVTAIFVTHSREEAFAFADKMAVMnHGVIEQYGSASE 223
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIASQ 157
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-198 |
2.62e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 24 SLEVEHGEIVCLLGASGCGKTTLLKAVAglLPLSSGIMSlNCQTiddgdnwLPPEQRNIG-------------------- 83
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGIPK-NCQI-------LHVEQEVVGddttalqcvlntdiertqll 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 ----MIFQDYALFPHLTVNQNVGFGLKDLSDQ----QKKEKVQEMLELVHLD-----------------EFGDRYPHQLS 138
Cdd:PLN03073 267 eeeaQLVAQQRELEFETETGKGKGANKDGVDKdavsQRLEEIYKRLELIDAYtaearaasilaglsftpEMQVKATKTFS 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKkqgvTAIFVTHSRE 198
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHARE 402
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-232 |
4.17e-07 |
|
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: 50.68 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYES--QTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqTIDDGDNWLPPEQRNI 82
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID--GIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 83 GMIFQDYALFphltvNQNVGFGLkdlsDQQKK---EKVQEMLELVHLDEFGDRYPHQL-----------SGGQQQRVAIA 148
Cdd:cd03288 98 SIILQDPILF-----SGSIRFNL----DPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 149 RSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGSASELYFHP 228
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
....
gi 490872517 229 SSKF 232
Cdd:cd03288 246 DGVF 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-175 |
5.92e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLnCQTIDDGDNwlppEQRNIGM 84
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKLGYF----AQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTvnqnvgfglkDLSDQQKKEKVQEmlelvHLDEF---GDRYPH---QLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK10636 388 LRADESPLQHLA----------RLAPQELEQKLRD-----YLGGFgfqGDKVTEetrRFSGGEKARLVLALIVWQRPNLL 452
|
170
....*....|....*..
gi 490872517 159 LLDEPFSNIDTQVRHEL 175
Cdd:PRK10636 453 LLDEPTNHLDLDMRQAL 469
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
5-198 |
6.70e-07 |
|
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: 48.86 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYesqtiLESLSLEVEHGEIVCLLGASGCGKTTLLKAvagllplssGIMSLNCQTIDDGDNwLPPEQRNIgM 84
Cdd:cd03238 1 LTVSGANVHN-----LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE---------GLYASGKARLISFLP-KFSRNKLI-F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYAL----FPHLTVNQNVGfglkdlsdqqkkekvqemlelvhldefgdryphQLSGGQQQRVAIARSLA--YKPDLL 158
Cdd:cd03238 65 IDQLQFLidvgLGYLTLGQKLS---------------------------------TLSGGELQRVKLASELFsePPGTLF 111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490872517 159 LLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSRE 198
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLD 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-169 |
7.98e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 8 KDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSL-----------NCQTIDDGDN-Wl 75
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqSRDALDPNKTvW- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 76 ppEQRNIGmifQDYalfphLTVNQN-------VG-FGLKDlSDQQKKEKVqemlelvhldefgdryphqLSGGQQQRVAI 147
Cdd:PRK11819 407 --EEISGG---LDI-----IKVGNReipsrayVGrFNFKG-GDQQKKVGV-------------------LSGGERNRLHL 456
|
170 180
....*....|....*....|..
gi 490872517 148 ARSLAYKPDLLLLDEPFSNIDT 169
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
5-198 |
2.24e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTIleslslEVEHGeIVCLLGASGCGKTTLLKAVAgllplssgimslncqtiddgdnwlppeqrnigm 84
Cdd:cd03240 4 LSIRNIRSFHERSEI------EFFSP-LTLIVGQNGAGKTTIIEALK--------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 ifqdYALFPHLTVNQNVGFGLKDL---------------SDQQKKEKVQ---EMLE---LVHLDEFGD---RYPHQLSGG 140
Cdd:cd03240 44 ----YALTGELPPNSKGGAHDPKLiregevraqvklafeNANGKKYTITrslAILEnviFCHQGESNWpllDMRGRCSGG 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872517 141 QQQ------RVAIARSLAYKPDLLLLDEPFSNIDT-QVRHELISQIRKIFKKQGVTAIFVTHSRE 198
Cdd:cd03240 120 EKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEE 184
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-197 |
1.77e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTILESLSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNcqtiddgdnwlpPEQRnIGM 84
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------------PNER-LGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 85 IFQDYALFPHLTVNQNVGFGLKDL-SDQQKKEKVQEMLELVHLD---------EFG--DRYP------------------ 134
Cdd:PRK15064 69 LRQDQFAFEEFTVLDTVIMGHTELwEVKQERDRIYALPEMSEEDgmkvadlevKFAemDGYTaearagelllgvgipeeq 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 135 H-----QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDtqvrhelISQIR---KIFKKQGVTAIFVTHSR 197
Cdd:PRK15064 149 HyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRwleDVLNERNSTMIIISHDR 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-207 |
2.31e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 131 DRYPHQLSGGQQQRVAIARSLAykPDLL----LLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSrEEAFAFADK 206
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADR 546
|
.
gi 490872517 207 M 207
Cdd:PRK00635 547 I 547
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-176 |
8.24e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 33 VCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqtiddgdnWLPPEQRnigmifqdYALFPHLTVNqnvgfGLkDLSDQ- 111
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV------------FRSAKVR--------MAVFSQHHVD-----GL-DLSSNp 591
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872517 112 -----QKKEKVQEMLELVHLDEFGD------RYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELI 176
Cdd:PLN03073 592 llymmRCFPGVPEQKLRAHLGSFGVtgnlalQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-215 |
1.06e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 1.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 137 LSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
136-181 |
1.34e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 40.30 E-value: 1.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490872517 136 QLSGGQQQR---VAIARSLAY----------KPDLLLLDEPFSNIDTQVRHELISQIRK 181
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
25-72 |
5.31e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.82 E-value: 5.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490872517 25 LEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSG-IMSLNCQTIDDGD 72
Cdd:cd00009 14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRPGApFLYLNASDLLEGL 62
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-205 |
8.93e-04 |
|
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: 40.32 E-value: 8.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872517 137 LSGGQQQRVAIARSLAYKPD--LLLLDEPFSNIDTQVRHELISQIRKIfKKQGVTAIFVTHSrEEAFAFAD 205
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAAD 206
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
23-84 |
1.95e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 39.68 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 23 LSLEVEHGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMslncqTIDDG-------DNWLP--------PEQRNIGM 84
Cdd:COG0630 283 LWLLLENGKSVLVAGGTASGKTTLLNALLSFIPPDAKIV-----TIEDTrelnlphENWISlvtresfgGEEGDVTM 354
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
29-70 |
3.27e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 37.18 E-value: 3.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490872517 29 HGEIVCLLGASGCGKTTLLKAVAGLLPLSSGIMSLNCQTIDD 70
Cdd:pfam13173 1 SRKILVITGPRQVGKTTLLLQLIKELLPPENILYINLDDPRL 42
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-207 |
5.15e-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: 38.01 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490872517 136 QLSGGQQQRVAIARSLA-YKPD---LLLLDEPFSNIDTQVRHELISQIRKIFKK-QGVTAIFvthsREEAFAFADKM 207
Cdd:cd03272 158 QLSGGQKSLVALALIFAiQKCDpapFYLFDEIDAALDAQYRTAVANMIKELSDGaQFITTTF----RPELLEVADKF 230
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
5-182 |
7.85e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.91 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 5 LSIKDLTCKYESQTIleslslEVEHGeIVCLLGASGCGKTTLLKAVA-GLLPLSSGIMSLNCQTIDDGDnwlppEQRNIG 83
Cdd:COG0419 5 LRLENFRSYRDTETI------DFDDG-LNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGS-----EEASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872517 84 MIFQDYALFPHLTVNQNVGFGLKDLSDQQKKEKVQEMLELVHLDEFGDRY------------------------------ 133
Cdd:COG0419 73 LEFEHGGKRYRIERRQGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLkeleealesaleelaelqklkqeilaqlsg 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490872517 134 ---PHQLSGGQQQRVAIARSLAykpdlLLLDepFSNIDTQVRHELISQIRKI 182
Cdd:COG0419 153 ldpIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL 197
|
|
|