|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-354 |
1.02e-144 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 413.72 E-value: 1.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAQRVAQQLQ--TCFGAH---PISEALAhHQEPIRCCFRPHQVQVFSQPTTGAIPATVLSSSFMGHAEQLRLQLDPETI 324
Cdd:COG3842 242 LPGTVLGDEGGgvRTGGRTlevPADAGLA-AGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
|
330 340 350
....*....|....*....|....*....|...
gi 514971686 325 ILAQVSPAQTA-YQ--EQVYVRLDLQQCFFFAQ 354
Cdd:COG3842 321 LVVRVPNRAALpLEpgDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
12-356 |
1.40e-123 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 360.16 E-value: 1.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ--QQIPAEARNI 89
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG------EILIGGRdvTDLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKlrKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS-- 245
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGsp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 246 ALNEIPAQRVAQQLQTCFGAHPISEALA-HHQEPIRCCFRPHQVQVfSQPTTGAIPATVLSSSFMGHAEQLRLQLDPETI 324
Cdd:COG3839 238 PMNLLPGTVEGGGVRLGGVRLPLPAALAaAAGGEVTLGIRPEHLRL-ADEGDGGLEATVEVVEPLGSETLVHVRLGGQEL 316
|
330 340 350
....*....|....*....|....*....|....
gi 514971686 325 ILaqVSPAQTAYQ--EQVYVRLDLQQCFFFAQDS 356
Cdd:COG3839 317 VA--RVPGDTRLRpgDTVRLAFDPERLHLFDAET 348
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-345 |
1.50e-120 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 352.14 E-value: 1.50e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQ---QIPAEARN 88
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG------RIVLNGRDlftNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFGLKKLP--KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPpsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSA 246
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 247 LNEIPAQRVAQQLQTcfGAHPISEALAHHQEPIRCCFRPHQVQVFSQPTT-GAIPATVLSSSFMGHAEQLRLQLDPET-- 323
Cdd:COG1118 237 VNVLRGRVIGGQLEA--DGLTLPVAEPLPDGPAVAGVRPHDIEVSREPEGeNTFPATVARVSELGPEVRVELKLEDGEgq 314
|
330 340
....*....|....*....|....*..
gi 514971686 324 IILAQVSPAQTAYQ-----EQVYVRLD 345
Cdd:COG1118 315 PLEAEVTKEAWAELglapgDPVYLRPR 341
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-226 |
1.87e-100 |
|
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: 295.97 E-value: 1.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKlrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
12-333 |
1.75e-97 |
|
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: 293.87 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEqqqiPAEARNIGL 91
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL----PPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAQRVA-QQLQTCFGAHPISEALAHHQEPIRCCFRPHQVQV-FSQPTTGAIPATVLSSSFMGHAEQLRLQLD--PETII 325
Cdd:TIGR03265 241 LPGTRGGgSRARVGGLTLACAPGLAQPGASVRLAVRPEDIRVsPAGNAANLLLARVEDMEFLGAFYRLRLRLEglPGQAL 320
|
....*...
gi 514971686 326 LAQVSPAQ 333
Cdd:TIGR03265 321 VADVSASE 328
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-250 |
5.79e-93 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 278.90 E-value: 5.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 6 AAQANVLTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQ 81
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTAlddvSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 82 IPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:COG1116 75 VTGPGPDRGVVFQEPALLPWLTVLDNVALGLElrGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQG-----EIIQIGTPKAlyRQ 234
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPRP--RD 232
|
250
....*....|....*.
gi 514971686 235 PATLFAARYFSALNEI 250
Cdd:COG1116 233 RELRTSPEFAALRAEI 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-243 |
7.51e-91 |
|
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: 272.19 E-value: 7.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIGL 91
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-253 |
3.39e-88 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 270.67 E-value: 3.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQ 80
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 81 QIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK09452 80 HVPAENRHVNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEIL-KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQM-QNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
250
....*....|....*.
gi 514971686 238 LFAARYFSALNEIPAQ 253
Cdd:PRK09452 239 LFVARFIGEINIFDAT 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-239 |
3.28e-84 |
|
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: 255.73 E-value: 3.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAE------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEirakvhELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLF 239
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-225 |
1.35e-83 |
|
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: 253.55 E-value: 1.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQIPAEAR 87
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-------PVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLElqGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQ--GEIIQI 225
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-237 |
1.49e-81 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 248.76 E-value: 1.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIG 90
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG1126 161 DEPTSALDPELVGEVL-DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-326 |
7.56e-81 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 251.16 E-value: 7.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAE------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 246 ALNEIPAQRVAQQLQTcfGAH--PISEALAhHQEPIRCCFRPHQVQVFSQPTTGA-IPATVLSSSFMGHAEQLRLQ---- 318
Cdd:PRK10851 239 EVNRLQGTIRGGQFHV--GAHrwPLGYTPA-YQGPVDLFLRPWEVDISRRTSLDSpLPVQVLEVSPKGHYWQLVVQplgw 315
|
....*....
gi 514971686 319 -LDPETIIL 326
Cdd:PRK10851 316 yNEPLTVVM 324
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-356 |
1.87e-80 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 250.02 E-value: 1.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQipaea 86
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgEDVTHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKmlGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYF 244
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 245 SALNEIPAQRVAQQLqTCFGAH---PISEALAHHQEPIRCCFRPHQVQvFSQPTTGAIPATVLSSSFMG---------HA 312
Cdd:PRK11432 238 GDANIFPATLSGDYV-DIYGYRlprPAAFAFNLPDGECTVGVRPEAIT-LSEQGEESQRCTIKHVAYMGpqyevtvdwHG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 514971686 313 EQLRLQLDPEtiilaQVSPAQTayqEQVYVRLDLQQCFFFAQDS 356
Cdd:PRK11432 316 QELLLQVNAT-----QLQPDLG---EHYYLEIHPYGMFLLADAA 351
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-329 |
3.17e-80 |
|
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: 248.56 E-value: 3.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 42 LLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQ 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE----DVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKmrKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 120 RQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVI 199
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 200 VTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNEIPAQRVAQQ-LQTCFGAHPISEALAHH--- 275
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKsEQVVLAGVEGRRCDIYTdvp 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 276 ---QEPIRCCFRPHQVQVFSQP---TTGAIPATVLSSSFMGHAEQLRLQLDPETIILAQV 329
Cdd:TIGR01187 237 vekDQPLHVVLRPEKIVIEEEDeanSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSE 296
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
14-248 |
1.80e-78 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 240.86 E-value: 1.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVF 93
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ----DATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEirKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 172 SNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALN 248
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-226 |
2.03e-77 |
|
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: 237.54 E-value: 2.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqqqIPAEARNIGL 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKlrKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-222 |
6.83e-77 |
|
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: 236.23 E-value: 6.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIPAE 85
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLllAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEAlQIADQIILMHQGEI 222
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-244 |
9.60e-77 |
|
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: 237.54 E-value: 9.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 6 AAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIP 83
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaaMSRKELRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 AEARNIGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:cd03294 99 LRRKKISMVFQSFALLPHRTVLENVAFGLevQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVR 258
|
...
gi 514971686 242 RYF 244
Cdd:cd03294 259 EFF 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-294 |
1.24e-75 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 238.58 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEARNIG 90
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKqdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 169 EPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALN 248
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 514971686 249 EIPAQRVAQQ-----LQTCFGAHPI---SEALAHHQEPIRCCFRPHQVQVFSQP 294
Cdd:PRK11607 255 VFEGVLKERQedglvIDSPGLVHPLkvdADASVVDNVPVHVALRPEKIMLCEEP 308
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
13-253 |
3.36e-74 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 234.12 E-value: 3.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQFGSR----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIPAEAR 87
Cdd:NF040933 4 RVENVTKIFKKGkkevVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKlVASPGKIIVPPEDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQ-RQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:NF040933 84 NIGMVFQNWALYPNMTVFDNIAFPLKikKVPKDEiEKKVKEVA-EILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYF 244
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242
|
....*....
gi 514971686 245 SALNEIPAQ 253
Cdd:NF040933 243 GDINLLEGK 251
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-238 |
4.66e-74 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 229.53 E-value: 4.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqIPAEARNIG 90
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN--LRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQ--DYALFpHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1122 79 LVFQnpDDQLF-APTVEEDVAFGPEnlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 167 MDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:COG1122 158 LDEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-223 |
7.57e-74 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 228.77 E-value: 7.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 9 ANVLTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQi 82
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSEREL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 pAEARN--IGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG1136 81 -ARLRRrhIGFVFQFFNLLPELTALENVALPLllAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrqntIEIL----KQTGTTTVIVTHDPeEALQIADQIILMHQGEII 223
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEV----LELLrelnRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-234 |
1.93e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.02 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNIGL 91
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV---RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 170 PFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG1131 158 PTSGLDpearRELWELLRE-----LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-274 |
5.08e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 229.21 E-value: 5.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ--QQIPAEA--R 87
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSG------RILIDGEdiRDLDPVElrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSM--QHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATvpRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA-- 241
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAdf 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 514971686 242 ----RYFSALNEIPAQRVAQ-QLQTCFGAHPISEALAH 274
Cdd:COG1125 237 vgadRGLRRLSLLRVEDLMLpEPPTVSPDASLREALSL 274
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-357 |
9.68e-73 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 230.50 E-value: 9.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEaRNIG 90
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PAD-RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKirGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 169 EPFSNLDHRLRDQIRqntIEILK---QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK11650 160 EPLSNLDAKLRVQMR---LEIQRlhrRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 246 --ALNEIPAQRVAQQLQTCFGAH---PISEALAHHQ-EPIRCCFRPHQVQVfsQPTTGAIPATVLSSSFMGhAEQL-RLQ 318
Cdd:PRK11650 237 spAMNLLDGRVSADGAAFELAGGialPLGGGYRQYAgRKLTLGIRPEHIAL--SSAEGGVPLTVDTVELLG-ADNLaHGR 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 514971686 319 LDPETIILAQVSPAQTAYQEQVYVRLDLQQCFFFAQDSQ 357
Cdd:PRK11650 314 WGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTG 352
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
16-331 |
1.41e-72 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 229.99 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 16 QLSKQFGSrFAVhQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVF 93
Cdd:COG4148 6 DFRLRRGG-FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 174 LDHRLRDQIrqntIEIL----KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:COG4148 164 LDLARKAEI----LPYLerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 250 IPAqRVAQQLQT------CFGAHPISEALAHHQ--EPIRCCFRPHQVQVFSQPTTG-----AIPATVLSSSFMGHAE-QL 315
Cdd:COG4148 240 LEA-TVAAHDPDygltrlALGGGRLWVPRLDLPpgTRVRVRIRARDVSLALEPPEGssilnILPGRVVEIEPADGGQvLV 318
|
330
....*....|....*.
gi 514971686 316 RLQLDpETIILAQVSP 331
Cdd:COG4148 319 RLDLG-GQTLLARITR 333
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-231 |
1.67e-72 |
|
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: 225.63 E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 7 AQANVLTIRQLSKQFGSRfAVHQ-ASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN----EQQQ 81
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDR-VVLDgVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 82 IPaeaRNIGLVFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG1127 80 LR---RRIGMLFQGGALFDSLTVFENVAFPLRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 159 APKPQVLLMDEPFSNLD----HRLRDQIRqntiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG1127 157 ALDPEILLYDEPTAGLDpitsAVIDELIR----ELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-250 |
9.77e-72 |
|
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: 223.72 E-value: 9.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAE-ARNI 89
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE---DIREQDPVElRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSM--QHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALvpKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
....*
gi 514971686 246 ALNEI 250
Cdd:cd03295 238 ADRLL 242
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
12-294 |
1.04e-71 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 227.27 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:NF040840 2 IRIENLSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGK----DITNLPPEKRGIAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:NF040840 77 VYQNYMLFPHKTVFENIAFGLKlrKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 514971686 250 IPAQRVAQQLQTCFGAHPISEALAHHQE-PIRCCFRPHQVQVFSQP 294
Cdd:NF040840 237 IEGVAEKGGEGTILDTGNIKIELPEEKKgKVRIGIRPEDITISTEK 282
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-222 |
1.41e-71 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 222.40 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGL 91
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 514971686 169 EPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03262 161 EPTSALDPELVGEV-LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-221 |
1.72e-70 |
|
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: 218.21 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGL 91
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGlkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-261 |
8.43e-69 |
|
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: 220.49 E-value: 8.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 19 KQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqqQIPAEARN-----IGLVF 93
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMK---QSPVELREvrrkkIGMVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR01186 78 QQFALFPHMTILQNTSLGPEllGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNEI- 250
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSq 237
|
250
....*....|...
gi 514971686 251 --PAQRVAQQLQT 261
Cdd:TIGR01186 238 vfDAERIAQRMNT 250
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-231 |
2.53e-67 |
|
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: 212.36 E-value: 2.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILW--NEQQQIPAEaRNIGL 91
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLR-RRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 169 EPFSNLDHRLRDQIrQNTIEILKQT-GTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03261 162 EPTAGLDPIASGVI-DDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-248 |
2.84e-67 |
|
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: 212.20 E-value: 2.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSrFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqqqIPAEARNIGL 91
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRkvDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALN 248
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-226 |
2.87e-67 |
|
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: 211.38 E-value: 2.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVFQDYALFPHLSVLDNVMFGLKK 114
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTG 194
Cdd:cd03297 103 KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLN 182
|
170 180 190
....*....|....*....|....*....|..
gi 514971686 195 TTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03297 183 IPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-246 |
2.52e-66 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 218.23 E-value: 2.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQFGSRF-----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-E 78
Cdd:COG1123 254 AAAAEPLLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 79 QQQIPAEARNIGLVFQD--YALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRV 152
Cdd:COG1123 334 RRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRlhgLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250
....*....|....
gi 514971686 233 RQPATLFAARYFSA 246
Cdd:COG1123 494 ANPQHPYTRALLAA 507
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-237 |
4.00e-66 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 214.20 E-value: 4.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIPAEARNIGLVFQDYALFPHLS 103
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDItkLSKKELRELRRKKMSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD----HR 177
Cdd:COG4175 122 VLENVAFGLEiqGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDplirRE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 178 LRDQIrqntIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG4175 202 MQDEL----LELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAN 257
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-224 |
1.43e-64 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 206.25 E-value: 1.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqqQIPAEAR 87
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPAlqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 niGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVAFGLRlrGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILM--HQGEIIQ 224
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-223 |
7.59e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 202.98 E-value: 7.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ-------QQI 82
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG------QVLVNGQdlsrlkrREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 PAEARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:COG2884 75 PYLRRRIGVVFQDFRLLPDRTVYENVALPLRvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIrqntIEILK---QTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEI----MELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-243 |
3.65e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 201.52 E-value: 3.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSrFAVHqASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQ--QIPAEARNI 89
Cdd:COG3840 2 LRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG------RILWNGQDltALPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGLRpglKLTAEQRAQV-EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-231 |
6.99e-63 |
|
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: 201.43 E-value: 6.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIPAE--ARN 88
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA----SLSRRelARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFG-------LKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREAV-EEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 162 PQVLLMDEPFSNLD--HRLR--DQIRqntiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG1120 156 PPLLLLDEPTSHLDlaHQLEvlELLR----RLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-221 |
1.47e-62 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 199.23 E-value: 1.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGS--RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGL 91
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQ--DYALFpHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd03225 159 DEPTAGLDPAGRRELLE-LLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-241 |
1.40e-61 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 201.80 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 9 ANVlTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEqqqIPAEARN 88
Cdd:PRK11000 2 ASV-TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-ND---VPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKlaGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 167 MDEPFSNLDHRLRDQIRqntIEIL---KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:PRK11000 157 LDEPLSNLDAALRVQMR---IEISrlhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-230 |
2.18e-61 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 196.16 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETP---SSGSIQLEQQILwneqQQIPAEARN 88
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL----TALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFGL-KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 168 DEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiadqiilmhQGEIIQIGTPKA 230
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-234 |
2.31e-60 |
|
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: 194.69 E-value: 2.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEAR-NI 89
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE----DVRKEPREARrQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNV-MFG-LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIrYFAeLYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 168 DEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG4555 157 DEPTNGLDvmarRLLREILRA-----LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-231 |
2.86e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 194.51 E-value: 2.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILW-NEQQQIPAEARN 88
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-230 |
9.22e-59 |
|
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: 190.34 E-value: 9.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQFGSRFAV----HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNE 78
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 79 QQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG4181 82 DARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrqntIEIL----KQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKA 230
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQI----IDLLfelnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-235 |
1.85e-56 |
|
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: 184.32 E-value: 1.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEA 86
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL---TLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RN----IGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:cd03258 78 RKarrrIGMIFQHFNLLSSRTVFENVALPLEiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-222 |
3.17e-56 |
|
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: 181.44 E-value: 3.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPaeaRNIGL 91
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03230 78 LPEEPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 172 SNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03230 124 SGLDPESRREFW-ELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-241 |
6.04e-56 |
|
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: 190.88 E-value: 6.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPS---SGSIQLEQQILWNEQQQIPAe 85
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 aRNIGLVFQD--YALFPhLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:COG1123 83 -RRIGMVFQDpmTQLNP-VTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
39-331 |
7.58e-56 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 186.47 E-value: 7.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 39 IICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVFQDYALFPHLSVLDNVMFGLKKLP 116
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTT 196
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 197 TVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY-FSALNEIpaqRVAQ--------QLQTCFGAHP 267
Cdd:TIGR02142 185 ILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREdQGSLIEG---VVAEhdqhygltALRLGGGHLW 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 268 ISEALAHHQEPIRCCFRPHQVQVFSQPTTG-----AIPATVLSSSfmgHAE--QLRLQLDPE-TIILAQVSP 331
Cdd:TIGR02142 262 VPENLGPTGARLRLRVPARDVSLALQKPEAtsirnILPARVVEIE---DSDigRVGVVLESGgKTLWARITR 330
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-250 |
1.15e-55 |
|
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: 182.28 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 33 SAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneQQQIPAEARNIglVFQDYALFPHLSVLDNVMFG- 111
Cdd:TIGR01184 7 TIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----QITEPGPDRMV--VFQNYSLLPWLTVRENIALAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 112 ---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:TIGR01184 80 drvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 189 ILKQTGTTTVIVTHDPEEALQIADQIILM------HQGEIIQIGTPKALYRQpATLFAARYFSALNEI 250
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPFPRPRDRL-EVVEDPSYYDLRNEA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-226 |
2.85e-55 |
|
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: 181.16 E-value: 2.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RN-IGLVFQDY--ALFPHLSVLDNVMFGLKKL----PKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:cd03257 81 RKeIQMVFQDPmsSLNPRMTIGEQIAEPLRIHgklsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrqntIEILK----QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQI----LDLLKklqeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-231 |
3.78e-55 |
|
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: 180.84 E-value: 3.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYALFPhLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM--QHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlhgIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
12-224 |
1.25e-54 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 179.94 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqILWNEQQQIPAEAR 87
Cdd:NF040729 2 LKIQNISKTFINNKKENEVlkdiSFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEI-----LVNGNEVTKPGPDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 niGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:NF040729 77 --GFVFQNYALFPWMTVKENIEYPMKqqKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDHRLRdQIRQNTIE-ILKQTGTTTVIVTHDPEEALQIADQIILM--HQGEIIQ 224
Cdd:NF040729 155 LMDEPLGAVDFQMR-QILQEELEsIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-237 |
2.96e-54 |
|
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: 179.23 E-value: 2.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEAR 87
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDY--ALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:COG1124 80 RVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-260 |
2.47e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 176.44 E-value: 2.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 15 RQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ 94
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 95 DYALFPHLSVLDNVMFG---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:PRK09493 85 QFYLFPHLTALENVMFGplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPatlfaaryfsalneiP 251
Cdd:PRK09493 165 SALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP---------------P 228
|
....*....
gi 514971686 252 AQRVAQQLQ 260
Cdd:PRK09493 229 SQRLQEFLQ 237
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-237 |
4.40e-53 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 176.53 E-value: 4.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQ---Q 80
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgEEIRLKPDrdgE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 81 QIPAEAR-------NIGLVFQDYALFPHLSVLDNVMFG---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQ 150
Cdd:COG4598 82 LVPADRRqlqrirtRLGMVFQSFNLWSHMTVLENVIEApvhVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQ----IRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEvlkvMRD-----LAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
250
....*....|.
gi 514971686 227 TPKALYRQPAT 237
Cdd:COG4598 237 PPAEVFGNPKS 247
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-231 |
5.66e-53 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 175.00 E-value: 5.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRF--AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPaeaRNI 89
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHRLRDQIrQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03263 158 DEPTSGLDPASRRAI-WDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
14-215 |
5.72e-53 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 174.34 E-value: 5.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAEARN----- 88
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ---ETPPLNSKKASKfrrek 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKykKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 514971686 167 MDEPFSNLDHRLRDQIrqntIEILKQ---TGTTTVIVTHDPEEAlQIADQII 215
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEV----LDLLLElndEGKTIIIVTHDPEVA-KQADRVI 204
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-238 |
5.75e-53 |
|
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: 176.49 E-value: 5.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEAR-NIGLVFQ--DYALFpHL 102
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRkKVGLVFQfpEHQLF-EE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLK--KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:TIGR04521 99 TVYKDIAFGPKnlGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 180 DQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:TIGR04521 179 KEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-228 |
7.09e-53 |
|
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: 174.93 E-value: 7.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILwneqqQIPAEARN-- 88
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDIT-----GLPPHEIArl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 -IGLVFQDYALFPHLSVLDNVM----------FGLKKLPKAQRQAV--AEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:cd03219 76 gIGRTFQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELA-ELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-235 |
1.46e-52 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 174.94 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-EQQI-----LWNEQQQIPAE 85
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIdtarsLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPHLSVLDNVMFG---LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-222 |
2.29e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.69 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--RNI 89
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK----PLSAMPPPEwrRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHlSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYT-LSGGEQQRVALARALAPKPQVLLMD 168
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 514971686 169 EPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-245 |
7.89e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 172.50 E-value: 7.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQiLWNEQQQIPAEA-----RN 88
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGH-QFDFSQKPSEKAirllrQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVM---FGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLIeapCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTpKALYRQPATLFAARYFS 245
Cdd:COG4161 164 LFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-268 |
1.66e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.88 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQQQIPAEA 86
Cdd:COG1135 2 IELENLSKTFPTKGGPVTAlddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 165 LLMDEPFSNLDhrlrdqiRQNTIEIL-------KQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:COG1135 162 LLCDEATSALD-------PETTRSILdllkdinRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
250 260 270
....*....|....*....|....*....|..
gi 514971686 238 LFAARYF-SALNEIPAQRVAQQLQTCFGAHPI 268
Cdd:COG1135 235 ELTRRFLpTVLNDELPEELLARLREAAGGGRL 266
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-220 |
1.99e-51 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 172.19 E-value: 1.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQIPAEARniGL 91
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAER--GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQG 220
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-231 |
2.79e-51 |
|
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: 171.21 E-value: 2.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRF-AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNI 89
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-229 |
6.85e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.27 E-value: 6.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 7 AQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQIPAEA 86
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-------PPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYAL---FPhLSVLDNVMFGL-------KKLPKAQRQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALAR 156
Cdd:COG1121 75 RRIGYVPQRAEVdwdFP-ITVRDVVLMGRygrrglfRRPSRADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGeIIQIGTPK 229
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPE 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
11-236 |
1.07e-50 |
|
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: 170.22 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneqQQIPAEARN- 88
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDI-----TGLPPHRIAr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLV--FQDYALFPHLSVLDNVMFG------------LKKLPKAQRQ-----AVAEQALQHVSMQHHLHSYPYTLSGGEQ 149
Cdd:COG0411 79 LGIArtFQNPRLFPELTVLENVLVAaharlgrgllaaLLRLPRARREerearERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
....*..
gi 514971686 230 ALYRQPA 236
Cdd:COG0411 239 EVRADPR 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
1.41e-50 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 169.83 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLR-------LIAGLETpsSGSIQLEQQ 73
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 74 ILWNEQQQIPAEARNIGLVFQDYALFPHlSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM----QHHLHSYPYTLSG 146
Cdd:COG1117 79 DIYDPDVDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRlhgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLD----HRLRDQIRQntieiLKQTgTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE-----LKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
250
....*....|...
gi 514971686 223 IQIGTPKALYRQP 235
Cdd:COG1117 232 VEFGPTEQIFTNP 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-245 |
4.28e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 168.27 E-value: 4.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQ----QIPAEARNI 89
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkAIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLKK---LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLIEAPCRvlgLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 167 MDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTpKALYRQPATLFAARYFS 245
Cdd:PRK11124 165 FDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-221 |
4.45e-50 |
|
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: 167.04 E-value: 4.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARN 88
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFGL----KKLPKAQRQAvaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLevrgKKEREIQRRV--GAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILD-LLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-226 |
1.59e-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: 164.53 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIPAEARniglv 92
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----SLSPKEL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 fqdyalfphlsvldnvmfglkklpkAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:cd03214 72 -------------------------ARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 173 NLDhrLRDQIRqnTIEILK----QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03214 127 HLD--IAHQIE--LLELLRrlarERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-222 |
2.93e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 166.39 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqqqipAEARN-IG 90
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL--------AEAREdTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGLKklpkAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLK----GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 514971686 171 FSNLDHRLRDQIrQNTIEIL-KQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK11247 161 LGALDALTRIEM-QDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-248 |
2.93e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 170.60 E-value: 2.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE----QQILWNEQQQIpaEAR 87
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAELREV--RRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFPHLSVLDNVMFG--LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
...
gi 514971686 246 ALN 248
Cdd:PRK10070 267 GVD 269
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-232 |
5.33e-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: 165.16 E-value: 5.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGS-RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEAR-N 88
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQaVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
11-245 |
1.24e-48 |
|
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: 164.39 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLE--TPS---SGSIQLEQQILWNEQQQIPAE 85
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlVPGvriEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPhLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRlhgIKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNLdhrlrDQIRQNTIEILKQ---TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:TIGR00972 160 AVEPEVLLLDEPTSAL-----DPIATGKIEELIQelkKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNP 234
|
250
....*....|
gi 514971686 236 ATLFAARYFS 245
Cdd:TIGR00972 235 KEKRTEDYIS 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-172 |
1.43e-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: 160.89 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneQQQIPAEARNIGLVFQDYALFPHLSVLD 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT--DDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 107 NVMFG--LKKLPKAQRQAVAEQALQHVSMQH----HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:pfam00005 79 NLRLGllLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-260 |
4.28e-48 |
|
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: 163.76 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqIPAEARNIGL 91
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN-LWEIRKKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDyalfPH-----LSVLDNVMFGL--KKLPKAQ-RQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:TIGR04520 82 VFQN----PDnqfvgATVEDDVAFGLenLGVPREEmRKRVDE-ALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQPATLFAAR 242
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLE-TIRKLNKEEGITVIsITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVELLKEIG 234
|
250
....*....|....*....
gi 514971686 243 YfsalnEIP-AQRVAQQLQ 260
Cdd:TIGR04520 235 L-----DVPfITELAKALK 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-221 |
7.10e-48 |
|
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: 159.33 E-value: 7.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneQQQIPAEARNIGLV 92
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 FQdyalfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:cd00267 79 PQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 514971686 173 NLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd00267 110 GLDPASRERLL-ELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
36-226 |
3.59e-47 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 159.58 E-value: 3.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLK-- 113
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 -KLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQ 192
Cdd:cd03298 99 lKLTAEDRQAI-EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|....
gi 514971686 193 TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-219 |
2.75e-46 |
|
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: 156.87 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAEARNIG 90
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE---PIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 514971686 171 FSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALqiADQIILMHQ 219
Cdd:COG4133 159 FTALDAAGVALLAE-LIAAHLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-205 |
7.47e-46 |
|
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: 156.03 E-value: 7.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 15 RQLSKQFGSRF-AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQQQIPAEARNIGLV 92
Cdd:cd03292 4 INVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 FQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEvtgVPPREIRKRVPA-ALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 514971686 170 PFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPE 205
Cdd:cd03292 163 PTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKE 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-234 |
8.28e-46 |
|
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: 166.55 E-value: 8.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFG--SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--R 87
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDPASlrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFpHLSVLDNVMFGLKKLPKAQRQAVAEQA--LQHVS-----MQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:COG2274 550 QIGVVLQDVFLF-SGTIRENITLGDPDATDEEIIEAARLAglHDFIEalpmgYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-234 |
8.64e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 158.25 E-value: 8.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEQQ--QIp 83
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETvwDV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 aeARNIGLVFQDY-ALFPHLSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:PRK13635 80 --RRQVGMVFQNPdNQFVGATVQDDVAFGLENigVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 161 KPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLE-TVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-228 |
1.01e-45 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 157.20 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNI 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaaWSPWEL----ARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYAL-FPhLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLH-SYPyTLSGGEQQRVALARALA------ 159
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRapHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 160 -PKPQVLLMDEPFSNLDhrLRDQirQNTIEILKQ---TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:COG4559 156 dGGPRWLFLDEPTSALD--LAHQ--HAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-226 |
1.24e-45 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 159.65 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 39 IICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQI--PAEARNIGLVFQDYALFPHLSVLDNVMFGLKKLP 116
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVaeqaLQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD-----------HRLRDQIRqn 185
Cdd:PRK11144 106 VAQFDKI----VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellpylERLAREIN-- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 514971686 186 tIEILkqtgtttvIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK11144 180 -IPIL--------YVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-236 |
3.61e-45 |
|
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: 155.01 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEAR-NIG 90
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLPMHKRARlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 169 EPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:cd03218 159 EPFAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
11-222 |
4.04e-45 |
|
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: 154.41 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQILWNEQQQIPAE 85
Cdd:TIGR02982 1 VISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPHLSVLDNVMFGLKKLPK---AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:TIGR02982 81 RRRIGYIFQAHNLLGFLTARQNVQMALELQPNlsyQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 163 QVLLMDEPFSNLDhrlrDQIRQNTIEILKQ----TGTTTVIVTHDPeEALQIADQIILMHQGEI 222
Cdd:TIGR02982 161 KLVLADEPTAALD----SKSGRDVVELMQKlakeQGCTILMVTHDN-RILDVADRILQMEDGKL 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-229 |
9.29e-45 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 153.97 E-value: 9.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqQQIPAEAR-NI 89
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH--LPMHERARlGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 167 MDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDI-KKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPA 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-236 |
1.97e-44 |
|
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: 155.60 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSR----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETP---SSGSIQLEQQILWN--EQQQ 81
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 82 IPAEARNIGLVFQD-Y-ALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM---QHHLHSYPYTLSGGEQQRVA 153
Cdd:COG0444 81 RKIRGREIQMIFQDpMtSLNPVMTVGDQIAEPLRihgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEILK----QTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQI----LNLLKdlqrELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*..
gi 514971686 230 ALYRQPA 236
Cdd:COG0444 237 ELFENPR 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-231 |
2.58e-44 |
|
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: 152.20 E-value: 2.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneqQQIPAEARN-- 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRDI-----TGLPPHERAra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 -IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQH----VSMQHHLhsyPYTLSGGEQQRVALARALAPKPQ 163
Cdd:cd03224 76 gIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELfprlKERRKQL---AGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 164 VLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-235 |
3.01e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 152.88 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-EQQIlwnEQQQIPAEARN- 88
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDI---THLPMHKRARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNVM--FGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILavLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 167 MDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:COG1137 160 LDEPFAGVDpiavADIQKIIRH-----LKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-217 |
1.29e-42 |
|
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: 147.68 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 21 FGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqipaeaRNIGLVFQDYAL-- 98
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-------KRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 99 -FPhLSVLDNVMFGL-------KKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:cd03235 82 dFP-ISVRDVVLMGLyghkglfRRLSKADKAKV-DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 514971686 171 FSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILM 217
Cdd:cd03235 160 FAGVDPKTQEDIYE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-234 |
1.61e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.99 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIP 83
Cdd:COG4988 330 PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV----DLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 AEA--RNIGLVFQDYALFpHLSVLDNVMFGlkkLPKAQRQAVaEQALQHVSMQHHLHSYP-----------YTLSGGEQQ 150
Cdd:COG4988 406 PASwrRQIAWVPQNPYLF-AGTIRENLRLG---RPDASDEEL-EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKA 230
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEI-LQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEE 557
|
....
gi 514971686 231 LYRQ 234
Cdd:COG4988 558 LLAK 561
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-236 |
1.96e-41 |
|
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: 145.12 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 9 ANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneqQQIPAEAR 87
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDI-----TGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 N---IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRqavAEQALQHV--------SMQHHLHSypyTLSGGEQQRVALAR 156
Cdd:COG0410 76 ArlgIGYVPEGRRIFPSLTVEENLLLGAYARRDRAE---VRADLERVyelfprlkERRRQRAG---TLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFE-IIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-235 |
5.81e-41 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 144.98 E-value: 5.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSR---------FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNeqQQI 82
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY--GDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 PAEARNIGLVFQD--YALFPHLSV---LDnvmFGLK---KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVA 153
Cdd:COG4167 83 KYRCKHIRMIFQDpnTSLNPRLNIgqiLE---EPLRlntDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYR 233
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
..
gi 514971686 234 QP 235
Cdd:COG4167 240 NP 241
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
28-222 |
1.23e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 142.88 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 28 HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNI--GLVFQDYALFPHLSVL 105
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKklGFIYQFHHLLPDFTAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 106 DNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIR 183
Cdd:TIGR02211 102 ENVAMPLliGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIF 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 514971686 184 QNTIEILKQTGTTTVIVTHDPEEALQIaDQIILMHQGEI 222
Cdd:TIGR02211 182 DLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-226 |
2.23e-40 |
|
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: 141.92 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMF 110
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLK---KLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTI 187
Cdd:TIGR01277 94 GLHpglKLNAEQQEKV-VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 514971686 188 EILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-237 |
4.54e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.42 E-value: 4.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-----------EQQILW 76
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 77 NEQQQIPAEARNIGLVFQDYALFPHLSVLDNVM---FGLKKLPKAQRQAVAEQALQHVSMQHHLH-SYPYTLSGGEQQRV 152
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
....*
gi 514971686 233 RQPAT 237
Cdd:PRK10619 241 GNPQS 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-221 |
9.39e-40 |
|
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: 138.67 E-value: 9.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSR--FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqiLWNEQ--QQIPAEA- 86
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI------LIDGVdlRDLDLESl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 -RNIGLVFQDYALFpHLSVLDNVmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03228 75 rKNIAYVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGE 221
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-231 |
1.09e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.49 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 24 RFAVHqaswsAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGLVFQDYALFPHLS 103
Cdd:PRK10771 17 RFDLT-----VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTPPSRRPVSMLFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLK---KLPKAQRQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PRK10771 88 VAQNIGLGLNpglKLNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 181 QIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-223 |
2.02e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.32 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 9 ANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQI--PAEA 86
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD-----GEPVRFrsPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RN--IGLVFQDYALFPHLSVLDNVMFG--LKKLP----KAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:COG1129 77 QAagIAIIHQELNLVPNLSVAENIFLGrePRRGGlidwRAMRRR-ARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 159 APKPQVLLMDEPFSNLDH----RLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG1129 156 SRDARVLILDEPTASLTEreveRLFRIIRR-----LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-265 |
2.49e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 142.63 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQFGSRF----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEAR 87
Cdd:PRK11153 3 ELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLElaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFS 245
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQ 242
|
250 260
....*....|....*....|....*
gi 514971686 246 AL--NEIPAQ---RVAQQLQTCFGA 265
Cdd:PRK11153 243 STlhLDLPEDylaRLQAEPTTGSGP 267
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
12-238 |
4.49e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.93 E-value: 4.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSK--QFGSRF---AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNE--QQQIPA 84
Cdd:PRK13634 3 ITFQKVEHryQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 EARNIGLVFQ--DYALFPHlSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHH-LHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
31-223 |
6.44e-39 |
|
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: 137.77 E-value: 6.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqiLWNEQQQIPAE-ARNIGLVFQD--YALFPHlSVLDN 107
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI------LLNGKPIKAKErRKSIGYVMQDvdYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLKKLPKAQRQAvaEQALQ--HVSMQHHLHsyPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQN 185
Cdd:cd03226 93 LLLGLKELDAGNEQA--ETVLKdlDLYALKERH--PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV-GE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 514971686 186 TIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03226 168 LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-207 |
1.08e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 137.99 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSrfAVHQAS------WSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQ 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQ--GEHELSiltgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 82 IPAEARNIGLVFQDYALFPHLSVLDNVMFG--LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK10584 83 AKLRAKHVGFVFQSFMLIPTLNALENVELPalLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEA 207
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-236 |
1.49e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 144.91 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQI 82
Cdd:COG4987 327 PAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL----RDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 PAEA--RNIGLVFQDYALFpHLSVLDNVMFGLkklPKAQRQAVaEQALQHVSMQHHLHSYPY-----------TLSGGEQ 149
Cdd:COG4987 403 DEDDlrRRIAVVPQRPHLF-DTTLRENLRLAR---PDATDEEL-WAALERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPK 229
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHE 554
|
....*..
gi 514971686 230 ALYRQPA 236
Cdd:COG4987 555 ELLAQNG 561
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-236 |
1.66e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.25 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 6 AAQANVLTIRQLSKQF---GSRF--------AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQ 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 74 ILWNEQQQIPAEARNIGLVFQD-YA-LFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGG 147
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQDpYAsLNPRMTVGDIIAEPLRihgLASKAERRERVAELLELVGLrPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 148 EQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQT-GTTTVIVTHDpeeaL----QIADQIILMHQGEI 222
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQV-LNLLEDLQDElGLTYLFISHD----LsvvrHISDRVAVMYLGKI 236
|
250
....*....|....
gi 514971686 223 IQIGTPKALYRQPA 236
Cdd:COG4608 237 VEIAPRDELYARPL 250
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-234 |
1.88e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.92 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqiLWNEQ--QQIPAEA--RNIGLVFQDYA 97
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI------LIDGVdiRDLTLESlrRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 98 LFpHLSVLDNVMFGLkklPKAQRQAVaEQALQHVSMQHHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1132 425 LF-SGTIRENIRYGR---PDATDEEV-EEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-228 |
2.20e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 137.98 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARN 88
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadWSPAEL----ARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYAL-FPhLSVLDNVMFGLKKLP--KAQRQAVAEQALQHVSMQHHLH-SYPyTLSGGEQQRVALARALA----- 159
Cdd:PRK13548 78 RAVLPQHSSLsFP-FTVEEVVAMGRAPHGlsRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 160 -PKPQVLLMDEPFSNLDhrLRDQirQNTIEILKQ----TGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK13548 156 dGPPRWLLLDEPTSALD--LAHQ--HHVLRLARQlaheRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-226 |
3.72e-38 |
|
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: 135.78 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGqIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQQI--PAEARN- 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSG------TIRIDGQDVLkqPQKLRRr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQDYALFPHLSVLDNV--MFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 167 MDEPFSNLDHRLRDQIRqntiEILKQTGTTTVIV--THDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03264 154 VDEPTAGLDPEERIRFR----NLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-226 |
4.21e-38 |
|
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: 135.96 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQA----SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA- 86
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAvdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF----DVVKEPAEAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 165 LLMDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03266 158 LLLDEPTTGLDvmatRALREFIRQ-----LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-231 |
4.31e-38 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 135.96 E-value: 4.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 17 LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSiqleqqiLWNEQQQIPAEA----RNIGLV 92
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-------ATVAGHDVVREPrevrRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 FQDYALFPHLSVLDNV-MFG-LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:cd03265 79 FQDLSVDDELTGWENLyIHArLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 171 FSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-229 |
5.18e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.43 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQ--DYAlFP 100
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI--SKENLKEIRKKIGIIFQnpDNQ-FI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:PRK13632 98 GATVEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 514971686 179 RDQIRQNTIEiLKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPK 229
Cdd:PRK13632 178 KREIKKIMVD-LRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-258 |
5.53e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 137.93 E-value: 5.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQQIPAEARNIG 90
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSG------EVLWDGEPLDPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 lvfqdY-----ALFPHLSVLDNVMF--GLKKLPKAQrqavAEQALQHVSMQHHLHSYPY----TLSGGEQQRVALARALA 159
Cdd:COG4152 75 -----YlpeerGLYPKMKVGEQLVYlaRLKGLSKAE----AKRRADEWLERLGLGDRANkkveELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ- 234
Cdd:COG4152 146 HDPELLILDEPFSGLDpvnvELLKDVIRE-----LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQf 220
|
250 260
....*....|....*....|....*..
gi 514971686 235 PATLFAARY---FSALNEIPAQRVAQQ 258
Cdd:COG4152 221 GRNTLRLEAdgdAGWLRALPGVTVVEE 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-245 |
1.40e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 135.74 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQiPA 84
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVD-PI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 EAR-NIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQRQ--AVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK14267 82 EVRrEVGMVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
250
....*....|
gi 514971686 236 ATLFAARYFS 245
Cdd:PRK14267 240 EHELTEKYVT 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-238 |
1.43e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 136.47 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGS--------IQLEQQILWNEQ 79
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 80 QQIpaearniGLVFQDY-ALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK13640 84 EKV-------GIVFQNPdNQFVGATVGDDVAFGLenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
..
gi 514971686 237 TL 238
Cdd:PRK13640 236 ML 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-223 |
1.03e-36 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 131.96 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEARNIGL 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK----SYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNvmFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03268 77 LIEAPGFYPNLTAREN--LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 172 SNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03268 155 NGLDpdgiKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-230 |
4.48e-36 |
|
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: 131.75 E-value: 4.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSG-SIQL--EQQILWNeqqqIPAEAR 87
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgERRGGED----VWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLV---FQDYaLFPHLSVLDNVMFGL-------KKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:COG1119 79 RIGLVspaLQLR-FPRDETVLDVVLSGFfdsiglyREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQIADQIILMHQGEIIQIGtPKA 230
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLA-LLDKLAAEGAPTLVlVTHHVEEIPPGITHVLLLKDGRVVAAG-PKE 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-249 |
5.68e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.16 E-value: 5.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 9 ANVLTIRQLSKQFGS---RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL-----WNEQQ 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 81 QIpaearniGLVFQDY-ALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:PRK13650 82 KI-------GMVFQNPdNQFVGATVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEaLQIADQIILMHQGEIIQIGTPKALYRQPAT 237
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
250 260
....*....|....*....|
gi 514971686 238 L--------FAARYFSALNE 249
Cdd:PRK13650 234 LlqlgldipFTTSLVQSLRQ 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-214 |
8.95e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 130.32 E-value: 8.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFG----SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RN--IGLVFQDYALFPHLSVLDNVMFGL--KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:PRK11629 85 RNqkLGFIYQFHHLLPDFTALENVAMPLliGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDpeeaLQIADQI 214
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-226 |
1.76e-35 |
|
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: 128.94 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQQQIPAEARNIGL 91
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG------EVLFDGKPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYlaQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 170 PFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03269 155 PFSGLDpvnvELLKDVIRE-----LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-235 |
1.78e-35 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 130.66 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqilWNEQQQIPAEAR 87
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-------LFDGENIPAMSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 N--------IGLVFQDYALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK11831 77 SrlytvrkrMSMLFQSGALFTDMNVFDNVAYPLRehtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNldhrlRDQIRQNTI-----EILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK11831 157 AIALEPDLIMFDEPFVG-----QDPITMGVLvklisELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
....
gi 514971686 232 YRQP 235
Cdd:PRK11831 232 QANP 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-223 |
9.01e-35 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 125.62 E-value: 9.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQI--PAEARN- 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GKEVSFasPRDARRa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 -IGLVFQdyalfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03216 76 gIAMVYQ-------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03216 107 DEPTAALTpaevERLFKVIRR-----LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
26-223 |
1.38e-34 |
|
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: 126.94 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQI-PAEAR-NIGLVFQDYALFpHLS 103
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLdPADLRrNIGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLkklPKAQRQAV---AEQALQHVSMQHHLHSYPY-------TLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:cd03245 94 LRDNITLGA---PLADDERIlraAELAGVTDFVNKHPNGLDLqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 514971686 174 LDHRLRDQIRQNtieiLKQT--GTTTVIVTHDPeEALQIADQIILMHQGEII 223
Cdd:cd03245 171 MDMNSEERLKER----LRQLlgDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-241 |
1.81e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 128.27 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ--DYALF-Phl 102
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQnpDDQLFaP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PRK13639 95 TVEEDVAFGPLnlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 181 QIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAA 241
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-223 |
1.90e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.46 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 9 ANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWN-EQQQI--PAE 85
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG------EILIDgKPVRIrsPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARN--IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQ-RQAVAEQALQHVSMQHHL----HSYPYTLSGGEQQRVALARAL 158
Cdd:COG3845 77 AIAlgIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRlDRKAARARIRELSERYGLdvdpDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNL-----DHrLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG3845 157 YRGARILILDEPTAVLtpqeaDE-LFEILRR-----LAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-232 |
2.29e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.56 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGS--RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEAR 87
Cdd:PRK13648 6 SIIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI--TDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQD-YALFPHLSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:PRK13648 84 HIGIVFQNpDNQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 165 LLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVI-VTHDPEEALQiADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13648 164 IILDEATSMLDPDARQNL-LDLVRKVKSEHNITIIsITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-238 |
2.54e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.86 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ--DYALFPHlS 103
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLKKL----PKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:PRK13637 101 IEKDIAFGPINLglseEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 180 DQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATL 238
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-234 |
4.00e-34 |
|
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: 131.85 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF-----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAE 85
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARN-----IGLVFQDYALFPHLSVLDNVM--FGLKkLPK--AQRQAVaeQALQHVSMQHH-----LHSYPYTLSGGEQQR 151
Cdd:TIGR03269 359 GRGrakryIGILHQEYDLYPHRTVLDNLTeaIGLE-LPDelARMKAV--ITLKMVGFDEEkaeeiLDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 152 VALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 514971686 232 YRQ 234
Cdd:TIGR03269 516 VEE 518
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-243 |
4.05e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 126.57 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWneQQQIPA 84
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF--KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 EARNIGLVFQDYALFPHLSVLDNVMFGLK--KLPKAQR--QAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKelQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 157 ALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
....*..
gi 514971686 237 TLFAARY 243
Cdd:PRK14247 238 HELTEKY 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-224 |
4.31e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.73 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQF---------GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQ 79
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 80 QQIPAEARNIGLVFQDY--ALFPHLSV---LDNVMFGLKKLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRVA 153
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSisAVNPRKTVreiIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ 224
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-203 |
4.51e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 125.76 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 16 QLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNIGLVF 93
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSgHDITRLKNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFGL----KKLPKAQRQAVAeqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLiiagASGDDIRRRVSA--ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|....
gi 514971686 170 PFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHD 203
Cdd:PRK10908 164 PTGNLDDALSEGILR-LFEEFNRVGVTVLMATHD 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
27-224 |
4.65e-34 |
|
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: 126.84 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN-EQQQIPAEARNIGLVFQDY--ALFPHLS 103
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRAFRRDVQLVFQDSpsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 V---LDNVMFGLKKLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:TIGR02769 107 VrqiIGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 514971686 180 DQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ 224
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-241 |
8.84e-34 |
|
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: 130.96 E-value: 8.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTT----MLRLIagletPSSGSIQLEQQIL--WNEQQQIPAEaRNIGLVFQD-YA- 97
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLdgLSRRALRPLR-RRMQVVFQDpFGs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 98 LFPHLSVLDNVMFGLK----KLPKAQRQAVAEQALQHVSMQH-HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:COG4172 375 LSPRMTVGQIIAEGLRvhgpGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 173 NLDHRLRDQIrqntIEILKQ----TGTTTVIVTHDpeeaLQ----IADQIILMHQGEIIQIGTPKALYRQPAT-----LF 239
Cdd:COG4172 455 ALDVSVQAQI----LDLLRDlqreHGLAYLFISHD----LAvvraLAHRVMVMKDGKVVEQGPTEQVFDAPQHpytraLL 526
|
..
gi 514971686 240 AA 241
Cdd:COG4172 527 AA 528
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-231 |
1.84e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.13 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSgSIQLEQQILWNEQQQIPAEARNI- 89
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-SAGSHIELLGRTVQREGRLARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 ------GLVFQDYALFPHLSVLDNVMFG-----------LKKLPKAQRQAvAEQALQHVSMQHHLHSYPYTLSGGEQQRV 152
Cdd:PRK09984 83 ksrantGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVT-HDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
31-222 |
2.08e-33 |
|
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: 122.32 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEAR-NIGLVFQDYALFPHlSVLDNVm 109
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---SQWDPNELGdHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 110 fglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTIEI 189
Cdd:cd03246 97 ----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAIAA 141
|
170 180 190
....*....|....*....|....*....|...
gi 514971686 190 LKQTGTTTVIVTHDPeEALQIADQIILMHQGEI 222
Cdd:cd03246 142 LKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-236 |
2.16e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.50 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQIPAE 85
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPhLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRlkgIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKI-EETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-234 |
2.70e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.20 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE------QQILWNEQQqipaearNIGLVFQ-- 94
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsdEENLWDIRN-------KAGMVFQnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 95 DYALFPHLsVLDNVMFGLKKL---PKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:PRK13633 95 DNQIVATI-VEEDVAFGPENLgipPEEIRERV-DESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 172 SNLDHRLRDQIrQNTI-EILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13633 173 AMLDPSGRREV-VNTIkELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-231 |
3.88e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 123.47 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEAR--- 87
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE----DISLLPLHARarr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQV 164
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-223 |
1.09e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.87 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqilwneqqQIPAEARnIGLVF 93
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------------SIPKGLR-IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFGLKKLPKAQRQ-AVAEQA-------------LQHVSMQHHLHSYPY----------------- 142
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAElEELEAKlaepdedlerlaeLQEEFEALGGWEAEAraeeilsglgfpeedld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 ----TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHrlrdqirqNTIE----ILKQTGTTTVIVTHDpeEAL--QIAD 212
Cdd:COG0488 148 rpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------ESIEwleeFLKNYPGTVLVVSHD--RYFldRVAT 217
|
250
....*....|.
gi 514971686 213 QIILMHQGEII 223
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-243 |
2.18e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 122.08 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 39 IICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEA----RNIGLVFQDYALFPHLSVLDNVMFGLKK 114
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 ---LPKAQRQAVAEQALQHVSMQHHLH----SYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTI 187
Cdd:PRK14246 118 hgiKEKREIKKIVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 188 EILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:PRK14246 198 ELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-271 |
3.60e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.53 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 16 QLSKQFGSRfAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN--EQQQIPAEARNIGLVF 93
Cdd:PRK13643 12 QPNSPFASR-ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 Q--DYALFPHlSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHL-HSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK13643 91 QfpESQLFEE-TVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 169 EPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARyfsaLN 248
Cdd:PRK13643 170 EPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHE----LG 244
|
250 260
....*....|....*....|....*..
gi 514971686 249 EIPAQRVAQQLQT----CFGAHPISEA 271
Cdd:PRK13643 245 VPKATHFADQLQKtgavTFEKLPITRA 271
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-260 |
5.25e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.38 E-value: 5.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipaEARN-IGLVFQDY--ALFPhLSVLDN 107
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSkVGLVFQDPddQVFS-STVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQn 185
Cdd:PRK13647 101 VAFGPVnmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 186 TIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYR----QPATL---FAARYFSALNEIPAQRVAQQ 258
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDedivEQAGLrlpLVAQIFEDLPELGQSKLPLT 259
|
..
gi 514971686 259 LQ 260
Cdd:PRK13647 260 VK 261
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-217 |
6.11e-32 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 119.85 E-value: 6.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF------GSRF-AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILW------N 77
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 78 EQQQIPAEARNIGLVFQdyalF----PHLSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQHHL-HSYPYTLSGGEQQ 150
Cdd:COG4778 84 PREILALRRRTIGYVSQ----FlrviPRVSALDVVAEPLLERgvDREEARARARELLARLNLPERLwDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILM 217
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVE-LIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-226 |
1.32e-31 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 118.91 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLEtpSSGSIqLEQQILWNEQQQIPAEAR-NIGLVFQDYALFPHLSVLDNVMFGL--- 112
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRV--EGGGT-TSGQILFNGQPRKPDQFQkCVAYVRQDDILLPGLTVRETLTYTAilr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 --KKLPKAQRQAVAEQ-ALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEI 189
Cdd:cd03234 110 lpRKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL----VST 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 514971686 190 LKQTGTT--TVIVT-HDP-EEALQIADQIILMHQGEIIQIG 226
Cdd:cd03234 186 LSQLARRnrIVILTiHQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-235 |
1.45e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 120.14 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-----ETPSSGSIQLEQQILWNEQQQIPAEA 86
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYALFPhLSVLDNVMFGLKKL---PKAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQ-----GEIIQIGTPKALYRQ 234
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
.
gi 514971686 235 P 235
Cdd:PRK14258 247 P 247
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-227 |
4.95e-31 |
|
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: 123.70 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNIGLVFQDYALF 99
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqWDREEL----GRHIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 100 PHlSVLDNVmfglKKLPKAQRQAVAEqALQHVSMqHHL-HSYP--Y---------TLSGGEQQRVALARALAPKPQVLLM 167
Cdd:COG4618 419 DG-TIAENI----ARFGDADPEKVVA-AAKLAGV-HEMiLRLPdgYdtrigeggaRLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHR----LRDQIRQntieiLKQTGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGT 227
Cdd:COG4618 492 DEPNSNLDDEgeaaLAAAIRA-----LKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-231 |
9.01e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 116.94 E-value: 9.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIP-AEARN-IGLVFQDYALFPHlS 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISrKSLRSmIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLkklPKAQRQAVAEqALQHVSMQHHLHSYP--Y---------TLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:cd03254 93 IMENIRLGR---PNATDEEVIE-AAKEAGAHDFIMKLPngYdtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 173 NLDHRLrDQIRQNTIEILKQtGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03254 169 NIDTET-EKLIQEALEKLMK-GRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-223 |
9.98e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGS-----RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipa 84
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 eARNIGLVFQDYAL--FPHLSVLDNVM--------FGLKK-LPKAQRQAVAEQ-ALQHVSMQHHLHSYPYTLSGGEQQRV 152
Cdd:COG1101 79 -AKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRgLTKKRRELFRELlATLGLGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-236 |
1.09e-30 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 116.70 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETP----SSGSIQLEQQILwneqQQIPAEARNIGLVFQD--YALF 99
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL----LPLSIRGRHIATIMQNprTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 100 PHLSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQHH---LHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNL 174
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLgkLSKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 175 DHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPK 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-231 |
1.30e-30 |
|
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: 116.56 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFpHL 102
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIGVVPQDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQhhlhSYP--YT---------LSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03253 90 TIGYNIRYGRPDATDEEVIEAAKAAQIHDKIM----RFPdgYDtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKAL 231
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-222 |
1.80e-30 |
|
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: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSkqfgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNeqqqIPAEARNI 89
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVTRR----SPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVF-----QDYALFPHLSVLDNVMFglkklpkaqrqavaeqalqhvsmqhhlhsyPYTLSGGEQQRVALARALAPKPQV 164
Cdd:cd03215 76 GIAYvpedrKREGLVLDLSVAENIAL------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 165 LLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-235 |
3.89e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.76 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNIGLVFQD-YA-LFPHL 102
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgQDLLKADPEAQKLLRQKIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLK---KLPKAQRQAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:PRK11308 110 KVGQILEEPLLintSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 179 RDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-228 |
4.96e-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: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLET--PSSGSI--------------------- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 69 ---------QLEQQILWNEQQQIPAE-ARNIGLVFQ-DYALFPHLSVLDNVMFGLKKLPKAQRQAV--AEQALQHVSMQH 135
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDKLRRRiRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVgrAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 136 HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQII 215
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|...
gi 514971686 216 LMHQGEIIQIGTP 228
Cdd:TIGR03269 241 WLENGEIKEEGTP 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-231 |
9.84e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.06 E-value: 9.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwnEQQQIPAEARN-- 88
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL-------CGEPVPSRARHar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 --IGLVFQDYALFPHLSVLDNVM-----FGlkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:PRK13537 80 qrVGVVPQFDNLDPDFTVRENLLvfgryFG---LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-223 |
1.28e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIlwneqqqipaearNIG 90
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV-------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALF-PHLSVLDNVMFGLKKLPKAQ-RQAVA------EQALQHVSmqhhlhsypyTLSGGEQQRVALARALAPKP 162
Cdd:COG0488 382 YFDQHQEELdPDKTVLDELRDGAPGGTEQEvRGYLGrflfsgDDAFKPVG----------VLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 163 QVLLMDEPFSNLDhrlrdqIrqNTIEILKQ-----TGtTTVIVTHDpEEALQ-IADQIILMHQGEII 223
Cdd:COG0488 452 NVLLLDEPTNHLD------I--ETLEALEEalddfPG-TVLLVSHD-RYFLDrVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-238 |
1.31e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.10 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSR-----FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-----QQILWNEQQ 80
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 81 QIPAEA---------RNIGLVFQ--DYALFPHlSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSMQH-HLHSYPYTLSG 146
Cdd:PRK13631 101 TNPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALgvKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|..
gi 514971686 227 TPKALYRQPATL 238
Cdd:PRK13631 259 TPYEIFTDQHII 270
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
33-232 |
1.56e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 33 SAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQ--DYALFPhLSVLDNVMF 110
Cdd:PRK13636 28 NIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQdpDNQLFS-ASVYQDVSF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLK--KLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:PRK13636 107 GAVnlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 514971686 189 ILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13636 187 MQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-230 |
1.97e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 118.61 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQq 80
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 81 qiPAEARNIG--LVFQDYALFPHLSVLDNVMFGLKKLPKAQRQavAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARAL 158
Cdd:PRK15439 80 --PAKAHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQK--MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 159 APKPQVLLMDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQG-------------- 220
Cdd:PRK15439 156 MRDSRILILDEPTASLTpaetERLFSRIRE-----LLAQGVGIVFISHKLPEIRQLADRISVMRDGtialsgktadlstd 230
|
250
....*....|
gi 514971686 221 EIIQIGTPKA 230
Cdd:PRK15439 231 DIIQAITPAA 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
37-223 |
2.07e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.44 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEAR--NIGLVFQDYALFPHLSVLDNVMFG--L 112
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRreHFGFIFQRYHLLSHLTAAQNVEVPavY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 KKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQ 192
Cdd:PRK10535 114 AGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV-MAILHQLRD 192
|
170 180 190
....*....|....*....|....*....|.
gi 514971686 193 TGTTTVIVTHDPEEALQiADQIILMHQGEII 223
Cdd:PRK10535 193 RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-260 |
2.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.54 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 29 QASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL--EQQILWNEQQQIPAEARNIGLVFQ--DYALFPHlSV 104
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagYHITPETGNKNLKKLRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNVMFGLKKLPKAQRQAvAEQALQ---HVSMQHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEA-KEKALKwlkKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 181 QIRQNTIEILKqTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLfaARYFsaLNEIPAQRVAQQLQ 260
Cdd:PRK13641 183 EMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL--KKHY--LDEPATSRFASKLE 257
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-234 |
6.68e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.30 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWN--EQQQIPAEARNIGLVFQ--DYALFPHlSVLDNVMFGL 112
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 KKLPKAQRQA--VAEQALQHVSMQHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEI 189
Cdd:PRK13649 112 QNFGVSQEEAeaLAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 514971686 190 LKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13649 191 LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-223 |
1.20e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSkqfgSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQI--PAEARN 88
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD-----GKPVRIrsPRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVF-----QDYALFPHLSVLDNVMFG-LKKL-------PKAQRQAVAE--QAL--------QHVSmqhhlhsypyTLS 145
Cdd:COG1129 327 AGIAYvpedrKGEGLVLDLSIRENITLAsLDRLsrgglldRRRERALAEEyiKRLriktpspeQPVG----------NLS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 146 GGEQQRVALARALAPKPQVLLMDEPFSNLD-------HRLrdqIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMH 218
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakaeiYRL---IRE-----LAAEGKAVIVISSELPELLGLSDRILVMR 468
|
....*
gi 514971686 219 QGEII 223
Cdd:COG1129 469 EGRIV 473
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-242 |
2.01e-28 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.94 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 7 AQANVLTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKT----TMLRLIAGLETPSSGSIQLE-QQILwn 77
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgQDLL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 78 eqqQIPAEA------RNIGLVFQD--YALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSM---QHHLHSYPYT 143
Cdd:COG4172 80 ---GLSERElrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLrlhRGLSGAAARARALELLERVGIpdpERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEILK----QTGTTTVIVTHDpeeaL----QIADQII 215
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQI----LDLLKdlqrELGMALLLITHD----LgvvrRFADRVA 228
|
250 260 270
....*....|....*....|....*....|..
gi 514971686 216 LMHQGEIIQIGTPKALYRQPA-----TLFAAR 242
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAAPQhpytrKLLAAE 260
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-234 |
2.37e-28 |
|
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: 110.71 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFPhLSVLDNVMF 110
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLFD-GTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLKKLPKAQRQAVAEQALQH---VSMQHHLHS----YPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIr 183
Cdd:cd03249 100 GKPDATDEEVEEAAKKANIHdfiMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 184 QNTIEILKQtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:cd03249 179 QEALDRAMK-GRTTIVIAHR-LSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-248 |
2.47e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 111.73 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 7 AQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSG-----SIQLEQQILWNEQQQ 81
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 82 IPAEaRNIGLVFQDYALFPhLSVLDNVMFGL---KKLPKAQRQAVAEQALQHV----SMQHHLHSYPYTLSGGEQQRVAL 154
Cdd:PRK14271 97 LEFR-RRVGMLFQRPNPFP-MSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 155 ARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtgTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
250
....*....|....
gi 514971686 235 PATLFAARYFSALN 248
Cdd:PRK14271 253 PKHAETARYVAGLS 266
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-240 |
3.96e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.46 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 7 AQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQL-EQQILWNEQQQIpae 85
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIEGLPGHQI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARnIGLV--FQDYALFPHLSVLDNVMF------------GLKKLP---KAQRQAV--AEQALQHVSMQHHLHSYPYTLSG 146
Cdd:PRK11300 78 AR-MGVVrtFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPafrRAESEALdrAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
250
....*....|....
gi 514971686 227 TPKALYRQPATLFA 240
Cdd:PRK11300 237 TPEEIRNNPDVIKA 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-228 |
4.32e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.49 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIPAE--ARNI 89
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS----MLSSRqlARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQ--------------DYALFPHLSvldnvMFGlkKLPKAQRQAVaEQALQ--HVSmqhHLHSYPYT-LSGGEQQRV 152
Cdd:PRK11231 79 ALLPQhhltpegitvrelvAYGRSPWLS-----LWG--RLSAEDNARV-NQAMEqtRIN---HLADRRLTdLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLD--HR--LRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDinHQveLMRLMRE-----LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-241 |
6.00e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.01 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGL 91
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV--EALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYAL--------------FPHLSVLDnvmfglkKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA 157
Cdd:PRK09536 82 VPQDTSLsfefdvrqvvemgrTPHRSRFD-------TWTETDRAAV-ERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 158 LAPKPQVLLMDEPFSNLDhrLRDQIRqnTIEI---LKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYrQ 234
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD--INHQVR--TLELvrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL-T 228
|
....*..
gi 514971686 235 PATLFAA 241
Cdd:PRK09536 229 ADTLRAA 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-228 |
1.06e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.40 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAE--ARNIG 90
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV----ATTPSRelAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFG-----LKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGrfpysKGRLTAEDREII-DEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 166 LMDEPFSNLD--H--RLRDQIRQNTIEIlkqtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:COG4604 158 LLDEPLNNLDmkHsvQMMKLLRRLADEL----GKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-242 |
1.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.89 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqIPAEARN 88
Cdd:PRK13652 2 HLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQ--DYALFPHlSVLDNVMFGLKKLpKAQRQAVA---EQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:PRK13652 80 VGLVFQnpDDQIFSP-TVEQDIAFGPINL-GLDEETVAhrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAAR 242
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVH 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-212 |
1.17e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.49 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQAN-VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLR-------LIAGLETpsSGSIQLEQQILW 76
Cdd:PRK14243 3 TLNGTEtVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 77 NEQQQiPAEARN-IGLVFQDYALFPHlSVLDNVMFGLKKLP-KAQRQAVAEQALQHVSM----QHHLHSYPYTLSGGEQQ 150
Cdd:PRK14243 81 APDVD-PVEVRRrIGMVFQKPNPFPK-SIYDNIAYGARINGyKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLD--HRLRDQirqntiEILKQTGT--TTVIVTHDPEEALQIAD 212
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSD 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-234 |
1.67e-27 |
|
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: 108.47 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 24 RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFpHLS 103
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLKKLPKAQRQAVAEQALQH---VSMQHHLHSY----PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDH 176
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARAANAHefiMELPEGYDTVigerGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 177 RLRDQIrQNTIEILKQtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:cd03251 172 ESERLV-QAALERLMK-NRTTFVIAHR-LSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-217 |
1.69e-27 |
|
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: 113.15 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqQIP 83
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA----DAD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 AEA--RNIGLVFQDYALFPHlSVLDNVMFGLKKLPKAQRQAVAEQA-----LQHVSMQHH--LHSYPYTLSGGEQQRVAL 154
Cdd:TIGR02857 391 ADSwrDQIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAgldefVAALPQGLDtpIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 155 ARALAPKPQVLLMDEPFSNLDhrlrDQIRQNTIEILKQ--TGTTTVIVTHDPEEALQiADQIILM 217
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLD----AETEAEVLEALRAlaQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-223 |
2.04e-27 |
|
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: 106.87 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 18 SKQFGSRFAV-HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSsgsiQLEQQILWNEQQQIPAEARN-IGLVFQD 95
Cdd:cd03213 15 SSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL----GVSGEVLINGRPLDKRSFRKiIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 96 YALFPHLSVLDNVMFGLKklpkaqrqavaeqalqhvsmqhhLHSypytLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:cd03213 91 DILHPTLTVRETLMFAAK-----------------------LRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 514971686 176 HRLRDQIRQnTIEILKQTGTTTVIVTHDP-EEALQIADQIILMHQGEII 223
Cdd:cd03213 144 SSSALQVMS-LLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-232 |
3.69e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQ---ASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL-----WNEQqqi 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaenvWNLR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 paeaRNIGLVFQDY-ALFPHLSVLDNVMFGLKK--LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK13642 81 ----RKIGMVFQNPdNQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 160 PKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-228 |
4.40e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.56 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSG-SIQLEQQILWNEQQ--QIPAEARNIGLVFQ--DYALFP 100
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKikEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HlSVLDNVMFGLKKLPKAQRQAVAE--QALQHVSM-QHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHR 177
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 178 LRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-216 |
1.39e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 21 FGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNIGLVFQDYAL-- 98
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-------------AGGARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 99 -FPhLSVLDNVMFG-------LKKLPKAQRqAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:NF040873 69 sLP-LTVRDLVAMGrwarrglWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 514971686 171 FSNLDHRLRDQIrqntIEILKQ---TGTTTVIVTHDPEEALQIADQIIL 216
Cdd:NF040873 147 TTGLDAESRERI----IALLAEehaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-236 |
2.05e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQ--LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTT----MLRLIAgletpSSGSIQLEQQIL--WNEQQQIPAE 85
Cdd:PRK15134 287 IRKgiLKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhnLNRRQLLPVR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARnIGLVFQD--YALFPHLSVLDNVMFGL----KKLPKAQRQAVAEQALQHVSMQHHL-HSYPYTLSGGEQQRVALARAL 158
Cdd:PRK15134 362 HR-IQVVFQDpnSSLNPRLNVLQIIEEGLrvhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVI-VTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-234 |
2.18e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNE--QQQIPAEARNIGLVFQdyalFPHLS 103
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPVRKRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VL-DNV----MFGLK--KLPKAQRQAVAEQALQHVSMQHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PRK13646 98 LFeDTVereiIFGPKnfKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 176 HRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-227 |
2.67e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 106.03 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRF---------AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQ 81
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 82 IPAEARNIGLVFQD--YALFPHLSVLDNVMFGLK---KLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK15112 82 YSYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRlntDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGT 227
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-234 |
5.00e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.39 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqqiPAEarnIGLVF 93
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA------LLE---LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QdyalfPHLSVLDNVMF-----GLKKL-PKAQRQAVAEQAlqhvSMQHHLHSyPY-TLSGGEQQRVALARALAPKPQVLL 166
Cdd:COG1134 100 H-----PELTGRENIYLngrllGLSRKeIDEKFDEIVEFA----ELGDFIDQ-PVkTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 167 MDEPFSNLD----HRLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK---ALYRQ 234
Cdd:COG1134 170 VDEVLAVGDaafqKKCLARIRE-----LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEeviAAYEA 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-226 |
6.07e-26 |
|
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: 103.77 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 24 RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqqiPAEarnIGLVFQdyalfPHLS 103
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS------LLG---LGGGFN-----PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFG--LKKLPKAQRQAVAEQALQHVSMQHHLHsYPY-TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:cd03220 101 GRENIYLNgrLLGLSRKEIDEKIDEIIEFSELGDFID-LPVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 514971686 181 QIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03220 180 KC-QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-231 |
6.99e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.45 E-value: 6.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 17 LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqQIPAEAR----NIGLV 92
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-------PVPARARlaraRIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 FQDYALFPHLSVLDNVM-----FGLKKlpkAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLvfgryFGMST---REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 168 DEPFSNLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
35-236 |
3.40e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqLEQQILWNEQQQIPAEARNIGLVFQD-YALFPHLSVLDNVMFGLK 113
Cdd:PRK13644 26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 KL--PKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNtIEILK 191
Cdd:PRK13644 105 NLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLER-IKKLH 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 514971686 192 QTGTTTVIVTHDPEEaLQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK13644 184 EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-226 |
3.61e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.70 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIP-AEARNI 89
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdGQLRDLYALSeAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 -----GLVFQDYA--LFPHLSVLDNVmfGLKKLPKAQR-----QAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALAR 156
Cdd:PRK11701 87 lrtewGFVHQHPRdgLRMQVSAGGNI--GERLMAVGARhygdiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 157 ALAPKPQVLLMDEPFSNLD----HRLRDQIRQNTIEIlkqtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVREL----GLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-227 |
7.33e-25 |
|
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: 105.89 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNIGLVFQDYALF 99
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLkqWDRETF----GKHIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 100 PHlSVLDNVM-FGlkklPKAQRQAVAEQAlqHVSMQHHL-HSYP--Y---------TLSGGEQQRVALARALAPKPQVLL 166
Cdd:TIGR01842 405 PG-TVAENIArFG----ENADPEKIIEAA--KLAGVHELiLRLPdgYdtvigpggaTLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 167 MDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGT 227
Cdd:TIGR01842 478 LDEPNSNLDEE-GEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGRIARFGE 536
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
37-235 |
9.79e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.86 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQILWNEQQQIPAEARNIGLVFQD--YALFPHLSVLDNVMFGLK 113
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 KL-PKAQRQAVAEQA---LQHVSMQHHL-HSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:PRK15079 127 TYhPKLSRQEVKDRVkamMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 514971686 189 ILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK15079 207 LQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-223 |
1.71e-24 |
|
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: 100.10 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNIGLVF-QDYALFPHLSV 104
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF---LRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LD--NVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQI 182
Cdd:cd03267 113 IDsfYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 514971686 183 RQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-231 |
2.67e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.57 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQ-QQIPAEArnI 89
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA--V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQ-HVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 169 EPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK11614 163 EPSLGLAPIIIQQIF-DTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-234 |
3.20e-24 |
|
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: 99.48 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 23 SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL------WNEQQqipaearnIGLVFQDY 96
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpaWLRRQ--------VGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 97 ALFpHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYT-------LSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:cd03252 86 VLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIvgeqgagLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 170 PFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICA--GRTVIIIAHR-LSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
12-228 |
5.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRF-----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqILWNEQ------- 79
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKnkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 80 ------------------QQIPAEARNIGLVFQ--DYALFPHlSVLDNVMFGLKKL--PKAQRQAVAEQALQHVSM-QHH 136
Cdd:PRK13651 80 kekvleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMgvSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 137 LHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlrdqiRQNTIEILK------QTGTTTVIVTHDPEEALQI 210
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD-------PQGVKEILEifdnlnKQGKTIILVTHDLDNVLEW 231
|
250
....*....|....*...
gi 514971686 211 ADQIILMHQGEIIQIGTP 228
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDT 249
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-226 |
1.90e-23 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 97.59 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQ-ILWNEQQQIP-AEARN 88
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsGAELELYQLSeAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 I-----GLVFQDYALFPHLSVLDNVMFGLKKLPKAQR-----QAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALARA 157
Cdd:TIGR02323 83 LmrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 158 LAPKPQVLLMDEPFSNLD----HRLRDQIRQntieILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-241 |
2.24e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 101.74 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 15 RQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwneqqqiPAEARNI----- 89
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---------PVDAGDIatrrr 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 -GLVFQDYALFPHLSVLDNVM-----FGlkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:NF033858 341 vGYMSQAFSLYGELTVRQNLElharlFH---LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALY--RQPATLFAA 241
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVaaRGAATLEEA 496
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-235 |
4.73e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFPHlSVLDNVMFGLKKLP 116
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTP 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVAEQALQHVSMQHHLHSYpYT--------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlrDQIRQNTIE 188
Cdd:TIGR00958 584 DEEIMAAAKAANAHDFIMEFPNGY-DTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQE 658
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 514971686 189 ILKQTGTTTVIVTHDPEEAlQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:TIGR00958 659 SRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-235 |
6.05e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.31 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILWNEQQQIPAEARNIGLVFQD-YA-LFPHL 102
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgQRIDTLSPGKLQALRRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 103 SVLDNVMFGLKKLPKAQRQAVAEQA---LQHVSMQ-HHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVawlLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 179 RDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-221 |
6.49e-23 |
|
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: 93.28 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIlwneqqqipaearNIGL 91
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQdyalfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03221 68 FEQ-------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 514971686 172 SNLDHRLRDQIrqntIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGE 221
Cdd:cd03221 99 NHLDLESIEAL----EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-204 |
7.66e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 94.73 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEQQQIPaeARNIGL 91
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEP--HENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFGLKKLPKAQRQavAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR01189 78 LGHLPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 514971686 172 SNLD----HRLRDQIRQNTieilkQTGTTTVIVTHDP 204
Cdd:TIGR01189 156 TALDkagvALLAGLLRAHL-----ARGGIVLLTTHQD 187
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-235 |
2.20e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 96.35 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRF----AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-ETP---SSGSIQLEQQILwneqQQI 82
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDL----QRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 PAEAR------NIGLVFQD--YALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM------QHHLHSYPYTLSGGE 148
Cdd:PRK11022 79 SEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 149 QQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
....*..
gi 514971686 229 KALYRQP 235
Cdd:PRK11022 239 HDIFRAP 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-254 |
3.62e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.00 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKT-TMLRLIAGLETpSSGSIQLEQQILWNEQQQI-- 82
Cdd:PRK10261 11 DVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRRSRQVie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 83 -----PAEAR-----NIGLVFQD--YALFPHLSVLDNVMFGLKKLPKAQRQ---AVAEQALQHVSM---QHHLHSYPYTL 144
Cdd:PRK10261 90 lseqsAAQMRhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREeamVEAKRMLDQVRIpeaQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 145 SGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMGVIfITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270
....*....|....*....|....*....|.
gi 514971686 224 QIGTPKALYRQPATLFAARYFSALNEIPAQR 254
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVPQLGAMK 279
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
37-204 |
4.30e-22 |
|
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: 97.43 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipAEARNIGLVFQDYALFpHLSVLDNVMFGLkklP 116
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD--EVRRRVSVCAQDAHLF-DTTVRENLRLAR---P 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVAEqALQHVSMQHHLHSYPY-----------TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqn 185
Cdd:TIGR02868 435 DATDEELWA-ALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL--- 510
|
170 180
....*....|....*....|.
gi 514971686 186 tIEILKQ--TGTTTVIVTHDP 204
Cdd:TIGR02868 511 -LEDLLAalSGRTVVLITHHL 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-254 |
4.97e-22 |
|
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: 98.16 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGL 91
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFyaQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 170 PFSNLDHRLRDQIRQNTIEIlkQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARYFSALNE 249
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKN 1165
|
....*
gi 514971686 250 IPAQR 254
Cdd:TIGR01257 1166 IQSQR 1170
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-221 |
5.94e-22 |
|
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: 92.15 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 18 SKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipaeARNIGLVFQdYA 97
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---------------PGSIAYVSQ-EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 98 LFPHLSVLDNVMFG--------------------LKKLPKAQRQAVAEQALqhvsmqhhlhsypyTLSGGEQQRVALARA 157
Cdd:cd03250 76 WIQNGTIRENILFGkpfdeeryekvikacalepdLEILPDGDLTEIGEKGI--------------NLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDpEEALQIADQIILMHQGE 221
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQ-LQLLPHADQIVVLDNGR 204
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
10-235 |
1.07e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.87 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIlwneqqqipaearNI 89
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-------------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLKklPKAQRQAVAEqALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLR--PGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 170 PFSNLD-------HRLRDQIRQntieilkQTGTTTVIVTHDPEEALQIADQIILMHQgEIIQIGTPKALYRQP 235
Cdd:PRK09544 147 PTQGVDvngqvalYDLIDQLRR-------ELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-215 |
1.43e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA- 86
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE----DISTLKPEIy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 -RNIGLVFQDYALFPHlSVLDNVMFglkklP-KAQRQAVAEQALQHVSMQ-----HHLHSYPYTLSGGEQQRVALARALA 159
Cdd:PRK10247 80 rQQVSYCAQTPTLFGD-TVYDNLIF-----PwQIRNQQPDPAIFLDDLERfalpdTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 160 PKPQVLLMDEPFSNLDhrlrDQIRQNTIEIL----KQTGTTTVIVTHDPEEaLQIADQII 215
Cdd:PRK10247 154 FMPKVLLLDEITSALD----ESNKHNVNEIIhryvREQNIAVLWVTHDKDE-INHADKVI 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-226 |
1.63e-21 |
|
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: 90.45 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFG--SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNI 89
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDyalfPHL---SVLDNVmfGLKklpkaqrqavaeqalqhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLL 166
Cdd:cd03247 78 SVLNQR----PYLfdtTLRNNL--GRR------------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIG 226
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHH-LTGIEHMDKILFLENGKIIMQG 178
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-231 |
1.65e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.35 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFG-SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIG 90
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL--KDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHlSVLDNVMFGLK------KLPKAQRQAVAEQALQHVSMQHH--LHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLGAKenvsqdEIWAACEIAEIKDDIENMPLGYQteLSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQNtieILKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNN---LLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-231 |
3.14e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 16 QLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQIlwneQQQIPAE-ARNIGLVF 93
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDgEHI----QHYASKEvARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFG-------LKKLPKAQRQAVAeQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK10253 88 QNATTPGDITVQELVARGryphqplFTRWRKEDEEAVT-KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 167 MDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-263 |
4.04e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.06 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQQIL-------------WNEQQQIPAEARnigLVFQDYA 97
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLsdwsaaelarhraYLSQQQSPPFAM---PVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 98 LFphlsvldnvmfglkkLPKAQRQAVAEQALQHVS--------MQHHLHsypyTLSGGEQQRVALARALA-------PKP 162
Cdd:COG4138 92 LH---------------QPAGASSEAVEQLLAQLAealgledkLSRPLT----QLSGGEWQRVRLAAVLLqvwptinPEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 163 QVLLMDEPFSNLDhrlrdqIRQNT-----IEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYrQPAT 237
Cdd:COG4138 153 QLLLLDEPMNSLD------VAQQAaldrlLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
|
250 260
....*....|....*....|....*.
gi 514971686 238 LfaaryfSALNEIPAQRVAQQLQTCF 263
Cdd:COG4138 226 L------SEVFGVKFRRLEVEGHRWL 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
42-232 |
4.53e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 42 LLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAEARNIGLVFQD--YALFpHLSVLDNVMFGLKKL--PK 117
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDpeQQIF-YTDIDSDIAFSLRNLgvPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 118 AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntIEILK---QTG 194
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM----IAIIRrivAQG 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 514971686 195 TTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALY 232
Cdd:PRK13638 187 NHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-235 |
4.95e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 1 MNAYTAAQANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNE 78
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLesWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 79 QqqipAEARNIGLVFQDYALFPHLSVLDNVMFG-------LKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTLSGGEQQR 151
Cdd:PRK10575 81 K----AFARKVAYLPQQLPAAEGMTVRELVAIGrypwhgaLGRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 152 VALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
....
gi 514971686 232 YRQP 235
Cdd:PRK10575 236 MRGE 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
37-242 |
9.63e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 9.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQQilwnEQQQIPAEA--RNIGLVFQDYALFpHLSVLDNVMFGLKK 114
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGI----ELRELDPESwrKHLSWVGQNPQLP-HGTLRDNVLLGNPD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 LPKAQRQAVAEQA--LQHVSMQHHLHSYPY-----TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrqntI 187
Cdd:PRK11174 450 ASDEQLQQALENAwvSEFLPLLPQGLDTPIgdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV----M 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 188 EILKQ--TGTTTVIVTHDPEEaLQIADQIILMHQGEIIQIGTPKALYRQP---ATLFAAR 242
Cdd:PRK11174 526 QALNAasRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAGglfATLLAHR 584
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-204 |
1.87e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwNEQQQIPAEARNI 89
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD-----GGDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLKKLpkAQRQAVAEQALQHVSMQHHLHsYPY-TLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK13539 76 HYLGHRNAMKPALTVAENLEFWAAFL--GGEELDIAAALEAVGLAPLAH-LPFgYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 514971686 169 EPFSNLDhRLRDQIRQNTIEILKQTGTTTVIVTHDP 204
Cdd:PRK13539 153 EPTAALD-AAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-223 |
3.10e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaeARNIGLVF-QDYALFPHLSV 104
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEF---ARRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNvmFGLKK----LPKAQ-RQAVAEQAlQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD---- 175
Cdd:COG4586 114 IDS--FRLLKaiyrIPDAEyKKRLDELV-ELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvsk 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 514971686 176 HRLRDQIRqntiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:COG4586 191 EAIREFLK----EYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-230 |
4.29e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 91.42 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSgsiqLEQQILWNEQQQIPA-----E 85
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT----WDGEIYWSGSPLKASnirdtE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAV------AEQALQHVSMQHHLHSYPYT-LSGGEQQRVALARAL 158
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYnamylrAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 159 APKPQVLLMDEPFSNLDhRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEiiQIGTPKA 230
Cdd:TIGR02633 157 NKQARLLILDEPSSSLT-EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKDM 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-220 |
6.67e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 17 LSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEqQILWNEQQQIPAEARNIGLVFQDY 96
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NINYNKLDHKLAAQLGIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 97 ALFPHLSVLDNVMFGlkKLPK-----------AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK09700 90 SVIDELTVLENLYIG--RHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 166 LMDEPFSNLDHRLRDQ----IRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQG 220
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYlfliMNQ-----LRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-228 |
7.92e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 28 HQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLetpSSGSIQLEQQILWNEQqqiPAEARNI----GLVFQDYALFPHLS 103
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGM---PIDAKEMraisAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGL-----KKLPKAQRQAVAEQALQHVSM---QHHLHSYPYT---LSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:TIGR00955 116 VREHLMFQAhlrmpRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 173 NLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPE-EALQIADQIILMHQGEIIQIGTP 228
Cdd:TIGR00955 196 GLDSFMAYSVVQ-VLKGLAQKGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-226 |
9.90e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipaeaRNIGLVFQ----DYAlFPH 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK-----NLVAYVPQseevDWS-FPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 102 LsVLDNVMFG------LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PRK15056 96 L-VEDVVMMGryghmgWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 176 HRLRDQIRQNTIEiLKQTGTTTVIVTHDPEEALQIADQIIlMHQGEIIQIG 226
Cdd:PRK15056 175 VKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASG 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-236 |
1.07e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.63 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 1 MNAYTAAQANVLTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPS---SGSIQLE-Q 72
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNgR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 73 QIL-WNEQQQIPAEARNIGLVFQD--YALFPHLSVLDNVMFGL---KKLPKAQRQAVAEQALQHVSM---QHHLHSYPYT 143
Cdd:PRK09473 82 EILnLPEKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLmlhKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250
....*....|...
gi 514971686 224 QIGTPKALYRQPA 236
Cdd:PRK09473 242 EYGNARDVFYQPS 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-236 |
1.37e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.06 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQfGSRFAVHQASWSAQRGQIICLLGHSGCGKTtmLRLIAGLETPSSGSIQLEQQILWNEQQQIPAE--ARN 88
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCAlrGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 IGLVFQD--YALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM---QHHLHSYPYTLSGGEQQRVALARALAPKPQ 163
Cdd:PRK10418 81 IATIMQNprSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 164 VLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPA 236
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-234 |
1.39e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 90.26 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneqQQIPAEA--RNIGLVFQDYALFpHLSVLDNVMFGLkk 114
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI----RDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYGR-- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 lPKAQRQAVaEQALQHVsmqhHLH----SYP--Y-T--------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:COG5265 457 -PDASEEEV-EAAARAA----QIHdfieSLPdgYdTrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 180 DQIrQNTIEILKQtGTTTVIVTH------DpeealqiADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:COG5265 531 RAI-QAALREVAR-GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-225 |
1.40e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.03 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSR-FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipAEARNIG 90
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE--DYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLsvldnvmfgLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYT-----LSGGEQQRVALARALAPKPQVL 165
Cdd:PRK10522 401 AVFTDFHLFDQL---------LGPEGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 166 LMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDpEEALQIADQIILMHQGEIIQI 225
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-227 |
1.67e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--RNIGLVFQDYALF 99
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVTRASlrRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 100 pHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYPY-------TLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:PRK13657 422 -NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 173 NLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGT 227
Cdd:PRK13657 501 ALDVETEAKVKAALDELMK--GRTTFIIAHR-LSTVRNADRILVFDNGRVVESGS 552
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-230 |
2.39e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPsSGSiqLEQQILWNEQQQIPA-----E 85
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP-HGT--YEGEIIFEGEELQASnirdtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 ARNIGLVFQDYALFPHLSVLDNVMFGLKKLPK-----AQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAP 160
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 161 KPQVLLMDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEiiQIGTPKA 230
Cdd:PRK13549 161 QARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR--HIGTRPA 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-204 |
2.66e-19 |
|
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: 84.85 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGL 91
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---DFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VFQDYALFPHLSVLDNVMFglkkLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRF----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 514971686 172 SNLD----HRLRDQIRQNTieilkQTGTTTVIVTHDP 204
Cdd:cd03231 154 TALDkagvARFAEAMAGHC-----ARGGMVVLTTHQD 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-229 |
2.81e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.14 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQQIL-------------WNEQQQIPAEARNiglVFQDYA 97
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsaaelarhraYLSQQQTPPFAMP---VFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 98 LfpHLSVldnvmfglkKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA-------RALAPKPQVLLMDEP 170
Cdd:PRK03695 92 L--HQPD---------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 171 FSNLD---HRLRDQIrqntIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:PRK03695 161 MNSLDvaqQAALDRL----LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-205 |
3.16e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSKQFGS-RFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqiP 83
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR------------P 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 AEARniglvfqdyALF----PHLSV--LDNVMFglkkLPKAQRQ---AVAEQALQHVSMQHHLHSY------PYTLSGGE 148
Cdd:COG4178 424 AGAR---------VLFlpqrPYLPLgtLREALL----YPATAEAfsdAELREALEAVGLGHLAERLdeeadwDQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 149 QQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQntieILKQT--GTTTVIVTHDPE 205
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ----LLREElpGTTVISVGHRST 545
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-231 |
4.16e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLS-KQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEARNI 89
Cdd:COG3845 257 VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVF-----QDYALFPHLSVLDNVMFGLKKLPKAQR------QAVAEQALQHVSmqhhlhSY------PYT----LSGGE 148
Cdd:COG3845 334 GVAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIE------EFdvrtpgPDTparsLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 149 QQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTP 228
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPA 486
|
...
gi 514971686 229 KAL 231
Cdd:COG3845 487 AEA 489
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-245 |
5.25e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQipaeARNIGLVFQDYALFPHlS 103
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSEAAL----RQAISVVSQRVHLFSA-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGlkkLPKAQRQAVAEqALQHVSMQHHLHSYP----------YTLSGGEQQRVALARAL---APkpqVLLMDEP 170
Cdd:PRK11160 430 LRDNLLLA---APNASDEALIE-VLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALlhdAP---LLLLDEP 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 171 FSNLDHRLRDQIRQNTIEILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQpatlfAARYFS 245
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQ--NKTVLMITHR-LTGLEQFDRICVMDNGQIIEQGTHQELLAQ-----QGRYYQ 569
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-224 |
1.98e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwNEQQQIPAEAR 87
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI------DGQEMRFASTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 N-----IGLVFQDYALFPHLSVLDNVMFGlkKLP-------KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK11288 75 AalaagVAIIYQELHLVPEMTVAENLYLG--QLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQ----IRQntieiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ 224
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQlfrvIRE-----LRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-222 |
2.71e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 5 TAAQANVLTIRQLSkqfGSRFAvhQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPA 84
Cdd:PRK15439 262 QAAGAPVLTVEDLT---GEGFR--NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 EARNIGLVF-----QDYALFPHLSVLDNV---MFGLKKL---PKAQRqAVAEQALQHVSMQ-HHLHSYPYTLSGGEQQRV 152
Cdd:PRK15439 334 QRLARGLVYlpedrQSSGLYLDAPLAWNVcalTHNRRGFwikPAREN-AVLERYRRALNIKfNHAEQAARTLSGGNQQKV 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 153 ALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-222 |
2.89e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSkqfGSRfaVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEARNIGL 91
Cdd:PRK10762 258 LKVDNLS---GPG--VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS---PQDGLANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 92 VF--QDY---ALFPHLSVLDNV-----------MFGLKKlpKAQRQAVA-------------EQALQhvsmqhhlhsypy 142
Cdd:PRK10762 330 VYisEDRkrdGLVLGMSVKENMsltalryfsraGGSLKH--ADEQQAVSdfirlfniktpsmEQAIG------------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-226 |
3.27e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.09 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 13 TIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSgsiqLEQQILWNEQQQIPAEARNIGLV 92
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 FQDYALFPHLSVLDNVMF-GLKKLPKAQRQAVAEQALQHVSMQHHL---------HSYPYTLSGGEQQRVALARALAPKP 162
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFcSLLRLPKSLTKQEKILVAESVISELGLtkcentiigNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEAL-QIADQIILMHQGEIIQIG 226
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVL-TLGSLAQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFG 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-222 |
2.17e-17 |
|
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: 80.21 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFPHlSVLDNVMF 110
Cdd:cd03248 34 SFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 GLKKLPKAQRQAVAEQALQHVSMQHHLHSYpYT--------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQI 182
Cdd:cd03248 111 GLQSCSFECVKEAAQKAHAHSFISELASGY-DTevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 514971686 183 RQNTIEILKQtgtTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:cd03248 190 QQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-223 |
2.42e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQILWNEQQQipAEARNI 89
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKS--SQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVM--------FGLKKLPKAQRQAvaEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPK 161
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFlgrefvnrFGRIDWKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 162 PQVLLMDEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLF-RVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-236 |
6.83e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGS----RFAVHQASWSAQRGQIICLLGHSGCGKT----TMLRLIagletPSSGSIQLEQQILWNEQQQIP 83
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSPPVVYPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 AEAR--------NIGLVFQD--YALFPhLSVLDNVMFGLKKLPKAQRQAVAE----QALQHVSMQH---HLHSYPYTLSG 146
Cdd:PRK15134 81 ASEQtlrgvrgnKIAMIFQEpmVSLNP-LHTLEKQLYEVLSLHRGMRREAARgeilNCLDRVGIRQaakRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250
....*....|
gi 514971686 227 TPKALYRQPA 236
Cdd:PRK15134 240 RAATLFSAPT 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-203 |
7.64e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.91 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF-GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqqilwneqQQIPAEARNI 89
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------------EARPQPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLSVLDNVMFGLKKLPKAQR-----------------QAVAEQA-LQHVSMQHHLHSY----------- 140
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAEIKDALDrfneisakyaepdadfdKLAAEQAeLQEIIDAADAWDLdsqleiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 141 ---PY-----TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNtieiLKQTGTTTVIVTHD 203
Cdd:TIGR03719 151 rcpPWdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH----LQEYPGTVVAVTHD 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-254 |
1.70e-16 |
|
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: 78.74 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 21 FGSRFAVHQA------SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQ--IPAEAR-NI-- 89
Cdd:cd03291 41 FFSNLCLVGApvlkniNLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSwiMPGTIKeNIif 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYAlfpHLSVLDNVMF--GLKKLPKAQRQAVAEQALqhvsmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLM 167
Cdd:cd03291 121 GVSYDEYR---YKSVVKACQLeeDITKFPEKDNTVLGEGGI--------------TLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 168 DEPFSNLDHRLRDQIRQNTieILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATlFAARY--FS 245
Cdd:cd03291 184 DSPFGYLDVFTEKEIFESC--VCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLmgYD 260
|
....*....
gi 514971686 246 ALNEIPAQR 254
Cdd:cd03291 261 TFDQFSAER 269
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-225 |
1.93e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLE--TPSSGSIQLEQQILWNEqqqipaearniglvfqdyalfphLSVLDNVmfGLKK 114
Cdd:COG2401 56 GEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE-----------------------ASLIDAI--GRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 LPKAQRQAVAEQALqhVSMQHHLHSYPyTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTG 194
Cdd:COG2401 111 DFKDAVELLNAVGL--SDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAG 187
|
170 180 190
....*....|....*....|....*....|...
gi 514971686 195 TTTVIVTHDPE--EALQiADQIILMHQGEIIQI 225
Cdd:COG2401 188 ITLVVATHHYDviDDLQ-PDLLIFVGYGGVPEE 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-235 |
2.13e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.53 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVF 93
Cdd:PRK10789 318 IRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHlSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSYP-------YTLSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK10789 396 QTPFLFSD-TVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDtevgergVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 167 MDEPFSNLDHRLRDQIRQNtieiLKQTGTT-TVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHN----LRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
36-220 |
2.32e-16 |
|
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: 77.37 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQiLWNEQQQIPAEARNIGLVfqDYAL----FPHLSVLDNVMFG 111
Cdd:cd03290 26 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSV--AYAAqkpwLLNATVEENITFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 112 lKKLPKAQRQAVAEQAlqhvSMQHHLHSYPY-----------TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:cd03290 103 -SPFNKQRYKAVTDAC----SLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 514971686 181 QIRQNTI-EILKQTGTTTVIVTHDpEEALQIADQIILMHQG 220
Cdd:cd03290 178 HLMQEGIlKFLQDDKRTLVLVTHK-LQYLPHADWIIAMKDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-222 |
2.44e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 30 ASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGLVF------QDyALFPHLS 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIRAGIMLcpedrkAE-GIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNV---------MFGLKkLPKAQRQAVAEQALQHVSMQH-HLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:PRK11288 348 VADNInisarrhhlRAGCL-INNRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 514971686 174 LDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK11288 427 IDVGAKHEI-YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-215 |
3.53e-16 |
|
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: 75.27 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQleqqilwneqqqIPAEArniglvfqdyalfphlsvld 106
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG------------MPEGE-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 107 NVMFglkkLPkaQR----QAVAEQALqhvsmqhhlhSYPY--TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:cd03223 65 DLLF----LP--QRpylpLGTLREQL----------IYPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*
gi 514971686 181 QIRQntieILKQTGTTTVIVTHdPEEALQIADQII 215
Cdd:cd03223 129 RLYQ----LLKELGITVISVGH-RPSLWKFHDRVL 158
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
11-175 |
3.89e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.00 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEQ---QQIPAEAR 87
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG------EVLWQGEpirRQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NigLVFQDYA--LFPHLSVLDNVMFgLKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:PRK13538 75 D--LLYLGHQpgIKTELTALENLRF-YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|
gi 514971686 166 LMDEPFSNLD 175
Cdd:PRK13538 152 ILDEPFTAID 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-233 |
4.82e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.17 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAG--LETPSSGSIQLEQQILWNEQ--QQIPAE- 85
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEplAAIDAPr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 --ARNIGLVFQDYALFPhLSVLDNVMFGlkKLPKAQRQA--------VAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK13547 81 laRLRAVLPQAAQPAFA-FSAREIVLLG--RYPHARRAGalthrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALA---------PKPQVLLMDEPFSNLD----HRLRDQIRQNTIEIlkQTGTTTVIvtHDPEEALQIADQIILMHQGEI 222
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDlahqHRLLDTVRRLARDW--NLGVLAIV--HDPNLAARHADRIAMLADGAI 233
|
250
....*....|.
gi 514971686 223 IQIGTPKALYR 233
Cdd:PRK13547 234 VAHGAPADVLT 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-222 |
4.70e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-ETPSSGSIQLEQQ--ILWNEQQQIpaeARNIGLVFQD---YALFP 100
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKpvKIRNPQQAI---AQGIAMVPEDrkrDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HLSVLDNVMF-------GLKKLPKAQRQAVAEQALQHVSMQHhlhSYPY----TLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK13549 355 VMGVGKNITLaaldrftGGSRIDDAAELKTILESIQRLKVKT---ASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 514971686 170 PFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK13549 432 PTRGIDVGAKYEI-YKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-228 |
4.73e-15 |
|
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: 73.30 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 22 GSRFAVHQASWSAQRGQIICLLGHSGCGKTTM----LRLIagleTPSSGSIQLEQQILwneqQQIPAEA--RNIGLVFQD 95
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDI----SKIGLHDlrSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 96 YALFPhlsvlDNVMFGLKKLPKAQRQAVaEQALQHVSMQHHLHSYPYTL-----------SGGEQQRVALARALAPKPQV 164
Cdd:cd03244 87 PVLFS-----GTIRSNLDPFGEYSDEEL-WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 165 LLMDEPFSNLDHRLrDQIRQNTIEiLKQTGTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTP 228
Cdd:cd03244 161 LVLDEATASVDPET-DALIQKTIR-EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-202 |
6.03e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.68 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwNEQQQIPAEARNIG 90
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 91 LVFQDYALFPHLSVLDNVMFGLkklpKAQRQAVAEQALQHVSMQHHLHSYPY-TLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDI----HFSPGAVGITELCRLFSLEHLIDYPCgLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 514971686 170 PFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTH 202
Cdd:PRK13540 154 PLVALDELSLLTI-ITKIQEHRAKGGAVLLTSH 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-222 |
6.18e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.02 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGL-ETPSSGSIQLEQQIL--WNEQQQIPAearNIGLVFQD---YALFP 100
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdiRNPAQAIRA---GIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 HLSVLDNVMFG-LKKLPKAQR-QAVAEQALQHVSMQHhLH---SYPY----TLSGGEQQRVALARALAPKPQVLLMDEPF 171
Cdd:TIGR02633 353 ILGVGKNITLSvLKSFCFKMRiDAAAELQIIGSAIQR-LKvktASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 514971686 172 SNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:TIGR02633 432 RGVDVGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
40-262 |
6.29e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 40 ICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQipAEARNIGLVFQDYALFPHlSVLDNVMFGlkklpKAQ 119
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS--VLRQGVAMVQQDPVVLAD-TFLANVTLG-----RDI 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 120 RQAVAEQALQHVSMQHHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIE 188
Cdd:PRK10790 442 SEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 189 ILKQtgTTTVIVTHDPEEALQiADQIILMHQGEIIQIGTPKALYRQpatlfAARYFSALNeipAQRVAQQLQTC 262
Cdd:PRK10790 522 VREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA-----QGRYWQMYQ---LQLAGEELAAS 584
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-231 |
1.99e-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: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 8 QANVLTIRQLSKQFG--SRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLE-QQILwneqqqipa 84
Cdd:TIGR01257 1934 KTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAgKSIL--------- 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 eaRNIGLVFQDYALFPHLSVLDNVMFG---------LKKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALA 155
Cdd:TIGR01257 2005 --TNISDVHQNMGYCPQFDAIDDLLTGrehlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 156 RALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
35-231 |
3.38e-14 |
|
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: 73.68 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqQILWNEqQQIPAEAR-----NIGLVFQDYALFPHLsvldnvm 109
Cdd:COG4615 356 RRGELVFIVGGNGSGKSTLAKLLTGLYRPESG------EILLDG-QPVTADNReayrqLFSAVFSDFHLFDRL------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 110 FGLKKLPKAQRqavAEQALQHVSMQHHLH------SypyT--LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDq 181
Cdd:COG4615 422 LGLDGEADPAR---ARELLERLELDHKVSvedgrfS---TtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR- 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 514971686 182 irqntI---EIL---KQTGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKAL 231
Cdd:COG4615 495 -----VfytELLpelKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-235 |
5.49e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.14 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQqILWNE---QQQIP 83
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADR-MRFDDidlLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 84 AEAR-----NIGLVFQD--YALFPHLSVLDNVMfglKKLP----KAQ-------RQAVAEQALQHVSMQHH---LHSYPY 142
Cdd:PRK15093 81 RERRklvghNVSMIFQEpqSCLDPSERVGRQLM---QNIPgwtyKGRwwqrfgwRKRRAIELLHRVGIKDHkdaMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250
....*....|...
gi 514971686 223 IQIGTPKALYRQP 235
Cdd:PRK15093 238 VETAPSKELVTTP 250
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-228 |
5.60e-14 |
|
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: 70.13 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilwnEQQQIPAEA--RNIGLVFQDYALFP--- 100
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIPLEDlrSSLTIIPQDPTLFSgti 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 101 --HLSVLDnvMFGLKKLPKAQRqaVAEQALQhvsmqhhlhsypytLSGGEQQRVALARALAPKPQVLLMDEPFSNL---- 174
Cdd:cd03369 99 rsNLDPFD--EYSDEEIYGALR--VSEGGLN--------------LSQGQRQLLCLARALLKRPRVLVLDEATASIdyat 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 175 DHRLRDQIRQNTieilkqTGTTTVIVTHdpeeALQ-IA--DQIILMHQGEIIQIGTP 228
Cdd:cd03369 161 DALIQKTIREEF------TNSTILTIAH----RLRtIIdyDKILVMDAGEVKEYDHP 207
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-220 |
6.28e-14 |
|
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: 69.58 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETpsSGSIqlEQQILWNEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFglkklp 116
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKT--AGVI--TGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRF------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 kaqrqavaeqalqhvsmqhhlHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlrDQIRQNTIEILKQ---T 193
Cdd:cd03232 103 ---------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD----SQAAYNIVRFLKKladS 157
|
170 180
....*....|....*....|....*...
gi 514971686 194 GTTTVIVTHDPEEAL-QIADQIILMHQG 220
Cdd:cd03232 158 GQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-227 |
7.10e-14 |
|
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: 73.41 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 21 FGSRFAVH------QASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQ--IPAEARNIGLV 92
Cdd:TIGR01271 430 FFSNFSLYvtpvlkNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSwiMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 FQDYALFPHLSVLDNVMF--GLKKLPKAQRQAVAEQALqhvsmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQLeeDIALFPEKDKTVLGEGGI--------------TLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 171 FSNLDHRLRDQIRQNTieILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGT 227
Cdd:TIGR01271 576 FTHLDVVTEKEIFESC--LCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGT 630
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-281 |
8.26e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.48 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQF----GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIQLEQqILWNEQQ--QIPAE 85
Cdd:COG4170 4 LDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADR-FRWNGIDllKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 86 AR------NIGLVFQD--YALFPHLSVLDNVMFGLKKLP--------KAQRQAVAEQALQHVSMQHH---LHSYPYTLSG 146
Cdd:COG4170 82 ERrkiigrEIAMIFQEpsSCLDPSAKIGDQLIEAIPSWTfkgkwwqrFKWRKKRAIELLHRVGIKDHkdiMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 147 GEQQRVALARALAPKPQVLLMDEPFSNLD-------HRLRDQIRQNtieilkqTGTTTVIVTHDPEEALQIADQIILMHQ 219
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMEsttqaqiFRLLARLNQL-------QGTSILLISHDLESISQWADTITVLYC 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 220 GEIIQIGTPKALYRQP------ATLFAARYFSalNEIPAQrvaQQLQTCFGAHPISEALahhqePIRC 281
Cdd:COG4170 235 GQTVESGPTEQILKSPhhpytkALLRSMPDFR--QPLPHK---SRLNTLPGSIPPLQHL-----PIGC 292
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-203 |
1.28e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 40 ICLLGHSGCGKTTMLRLIAGLETPSSGsiqleqqilwneqQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGLKKL---- 115
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVkaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 ------------PKAQRQAVA-EQA-LQHVsMQHH---------------LHSYPY-----TLSGGEQQRVALARALAPK 161
Cdd:PRK11819 103 drfneiyaayaePDADFDALAaEQGeLQEI-IDAAdawdldsqleiamdaLRCPPWdakvtKLSGGERRRVALCRLLLEK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 514971686 162 PQVLLMDEPFSNLDhrlrdqirQNTIEILKQ-----TGtTTVIVTHD 203
Cdd:PRK11819 182 PDMLLLDEPTNHLD--------AESVAWLEQflhdyPG-TVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-231 |
2.31e-13 |
|
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: 71.90 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqipaearniglvfqdyALFPHLSVLD 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ----------------AWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 107 NVMFGLKKLPKAQRQAVAEQAL-QHVSM-----QHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:TIGR00957 718 NILFGKALNEKYYQQVLEACALlPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 514971686 181 QIRQNTI---EILKqtGTTTVIVTHDPEEALQIaDQIILMHQGEIIQIGTPKAL 231
Cdd:TIGR00957 798 HIFEHVIgpeGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-203 |
2.63e-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: 71.12 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNI 89
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-------------GETVKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDY-ALFPHLSV-------LDNVMFGLKKLPkaQRQAVAEQALQHVSMQHHLHSypytLSGGEQQRVALARALAPK 161
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVweeisggLDIIKLGKREIP--SRAYVGRFNFKGSDQQKKVGQ----LSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 514971686 162 PQVLLMDEPFSNLD-HRLRdqirqnTIE--ILKQTGtTTVIVTHD 203
Cdd:TIGR03719 462 GNVLLLDEPTNDLDvETLR------ALEeaLLNFAG-CAVVISHD 499
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-234 |
2.83e-13 |
|
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: 67.94 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLE--TPSSGSIQLE-QQILwneqqQIPAEAR- 87
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKgEDIT-----DLPPEERa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 --NIGLVFQDYALFPhlsvldnvmfGlkklpkaqrqavaeqalqhVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVL 165
Cdd:cd03217 76 rlGIFLAFQYPPEIP----------G-------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 166 LMDEPFSNLDhrlRDQIRQ--NTIEILKQTGTTTVIVTHDPEEALQI-ADQIILMHQGEIIQIGtPKALYRQ 234
Cdd:cd03217 127 ILDEPDSGLD---IDALRLvaEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-234 |
3.41e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 26 AVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwnEQQQIPAEARNIGLVFQDYALFpHLSVL 105
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTLASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 106 DNVMFGLK-KLPKAQRQAVAEQ--ALQHVS-MQHHLHSY----PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHR 177
Cdd:PRK11176 435 NNIAYARTeQYSREQIEEAARMayAMDFINkMDNGLDTVigenGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 178 LRDQIrQNTIEILKQTGTTTVIvTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK11176 515 SERAI-QAALDELQKNRTSLVI-AHR-LSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-225 |
1.35e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwneQQQIPAEARNIGLVF-----QDYALFPH 101
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKKGMAYitesrRDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 102 LSVLDNV-------------MFGLKKLPKAQRQAVAEQALQHVSMqHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:PRK09700 356 FSIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 169 EPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQI 225
Cdd:PRK09700 435 EPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-203 |
1.48e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAeaRNI-GLVFqDY------ALFPHL----S 103
Cdd:PRK11147 27 EDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPP--RNVeGTVY-DFvaegieEQAEYLkryhD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMF-----GLKKLpkAQRQAVAEQA--------LQHVSMQHHLHsyPYT----LSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK11147 104 ISHLVETdpsekNLNEL--AKLQEQLDHHnlwqlenrINEVLAQLGLD--PDAalssLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 514971686 167 MDEPFSNLDhrlrdqirQNTIE----ILKQTGTTTVIVTHD 203
Cdd:PRK11147 180 LDEPTNHLD--------IETIEwlegFLKTFQGSIIFISHD 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-215 |
1.92e-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: 66.28 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaEARNIGLVfqDYALFphlSVLDNvmfglkKL 115
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI--KADYEGTV--RDLLS---SITKD------FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 PKAQRQAVAEQALQhvsMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGT 195
Cdd:cd03237 91 THPYFKTEIAKPLQ---IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEK 167
|
170 180
....*....|....*....|
gi 514971686 196 TTVIVTHDPEEALQIADQII 215
Cdd:cd03237 168 TAFVVEHDIIMIDYLADRLI 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-175 |
2.27e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqipaeARNIGLVFQDYALFPHLSVLDNVMFgLKKLP 116
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR-----SRFMAYLGHLPGLKADLSTLENLHF-LCGLH 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 117 KAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARA-LAPKPqVLLMDEPFSNLD 175
Cdd:PRK13543 111 GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYANLD 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-227 |
2.86e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAG-LETPSSGSIQLEQQILWNEQqqipaearnIGLVFqdyalfpHLSVLDNVMFGLKKL 115
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVPQ---------VSWIF-------NATVRDNILFGSPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 PkaqrqAVAEQALQHVSMQHHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQ 184
Cdd:PLN03130 707 P-----ERYERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 514971686 185 NTI-EILKqtGTTTVIVTHDPEEALQIaDQIILMHQGEIIQIGT 227
Cdd:PLN03130 782 KCIkDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGT 822
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-203 |
3.77e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 42 LLGHSGCGKTTMLRLIAGLETPSSGSIQLEqqilwneqqqiPAEarNIGLVFQDYALFPHLSVLDNVMFGLKKL--PKAQ 119
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNE--RLGKLRQDQFAFEEFTVLDTVIMGHTELweVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 120 RQA--------------VAE------------------QALQHVSMQHHLHSYPYT-LSGGEQQRVALARALAPKPQVLL 166
Cdd:PRK15064 99 RDRiyalpemseedgmkVADlevkfaemdgytaearagELLLGVGIPEEQHYGLMSeVAPGWKLRVLLAQALFSNPDILL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 514971686 167 MDEPFSNLDhrlrdqIrqNTI----EILKQTGTTTVIVTHD 203
Cdd:PRK15064 179 LDEPTNNLD------I--NTIrwleDVLNERNSTMIIISHD 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-239 |
3.90e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 35 QRGQIICLLGHSGCGKTTMLRLIAG----LETPS---SGSIQLEQQILWneqqqipaearniglVFqdyalfpHLSVLDN 107
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISAMLGelshAETSSvviRGSVAYVPQVSW---------------IF-------NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLKKLPKAQRQAVAEQALQHvsmqhHLHSYP-----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDH 176
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQH-----DLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 177 RLRDQIRQNTI-EILKqtGTTTVIVTHDpEEALQIADQIILMHQGEIIQIGTPKALYRQpATLF 239
Cdd:PLN03232 774 HVAHQVFDSCMkDELK--GKTRVLVTNQ-LHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLF 833
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-223 |
4.39e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQleqqilWneqqqipAEARNI 89
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------W-------SENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYAL-FPH-LSVLDnVMFGLKKlPKAQRQAV----------AEQALQHVSMqhhlhsypytLSGGEQQRVALARA 157
Cdd:PRK15064 385 GYYAQDHAYdFENdLTLFD-WMSQWRQ-EGDDEQAVrgtlgrllfsQDDIKKSVKV----------LSGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 158 LAPKPQVLLMDEPFSNLDhrlrdqirQNTIEIL-----KQTGtTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD--------MESIESLnmaleKYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
44-204 |
4.97e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.12 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 44 GHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIPAE-ARNIGLVFQdyalfphLSVLDNVMFGLKKLPKAqrqA 122
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYiGHNLGLKLE-------MTVFENLKFWSEIYNSA---E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 123 VAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTH 202
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL-NNLIVMKANSGGIVLLSSH 181
|
..
gi 514971686 203 DP 204
Cdd:PRK13541 182 LE 183
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
87-202 |
7.12e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNI-GLVFQDYALFpHLSVLDNVMFG-----LKKLPKAQRQAVAEQALQHVSMQHHLHSYPY--TLSGGEQQRVALARAL 158
Cdd:PTZ00265 1295 RNLfSIVSQEPMLF-NMSIYENIKFGkedatREDVKRACKFAAIDEFIESLPNKYDTNVGPYgkSLSGGQKQRIAIARAL 1373
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTH 202
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
143-226 |
1.34e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.73 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALA--PKPQVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDpEEALQIADQIILM--- 217
Cdd:cd03238 87 TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQL-LEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDFgpg 164
|
90
....*....|..
gi 514971686 218 ---HQGEIIQIG 226
Cdd:cd03238 165 sgkSGGKVVFSG 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-203 |
1.35e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 17 LSKQFGSrFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWnEQQQIPAEARniGLVfQDY 96
Cdd:COG1245 347 LTKSYGG-FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISY-KPQYISPDYD--GTV-EEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 97 ALFPHLSVLDNVMF--------GLKKLpkaqrqavaeqalqhvsmqhhLHSYPYTLSGGEQQRVALARALAPKPQVLLMD 168
Cdd:COG1245 422 LRSANTDDFGSSYYkteiikplGLEKL---------------------LDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 514971686 169 EPFSNLD--HRLR--DQIRQntieILKQTGTTTVIVTHD 203
Cdd:COG1245 481 EPSAHLDveQRLAvaKAIRR----FAENRGKTAMVVDHD 515
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
37-228 |
1.40e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLE--TPSSGSIQLE-QQILwneqqQIPAEAR---NIGLVFQDYALFPHLSVLDnvmF 110
Cdd:COG0396 26 GEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDgEDIL-----ELSPDERaraGIFLAFQYPVEIPGVSVSN---F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 111 --------GLKKLPKAQRQAVAEQALQHVSM-QHHLHSY-PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDhrlRD 180
Cdd:COG0396 98 lrtalnarRGEELSAREFLKLLKEKMKELGLdEDFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD---ID 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 514971686 181 QIRQ--NTIEILKQTGTTTVIVTHDpEEALQI--ADQIILMHQGEIIQIGTP 228
Cdd:COG0396 175 ALRIvaEGVNKLRSPDRGILIITHY-QRILDYikPDFVHVLVDGRIVKSGGK 225
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-216 |
1.64e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 36 RGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqIPAEARNIGLVFQdyalfphlsvldnvmfglkkl 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------IDGEDILEEVLDQ--------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 pkaqrqavaeqalqhvSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQN-----TIEIL 190
Cdd:smart00382 49 ----------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLK 112
|
170 180
....*....|....*....|....*.
gi 514971686 191 KQTGTTTVIVTHDPEEALQIADQIIL 216
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-222 |
1.91e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLeTPS---SGSIQLEQQILwnEQQQIPA-EA 86
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVC--RFKDIRDsEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 RNIGLVFQDYALFPHLSVLDNVM-------FGLKKLPKAQRQAvaEQALQHVSmqhhLHSYPYTLSG----GEQQRVALA 155
Cdd:NF040905 78 LGIVIIHQELALIPYLSIAENIFlgnerakRGVIDWNETNRRA--RELLAKVG----LDESPDTLVTdigvGKQQLVEIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDH----RLRDQIRQntieiLKQTGTTTVIVTHDPEEALQIADQI-IL----------MHQG 220
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEedsaALLDLLLE-----LKAQGITSIIISHKLNEIRRVADSItVLrdgrtietldCRAD 226
|
..
gi 514971686 221 EI 222
Cdd:NF040905 227 EV 228
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-254 |
3.82e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 64.65 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPK-PQVL-LMDEPFSNLdHRlRDQIRQ-NTIEILKQTGTTTVIVTHDpEEALQIADQIILM-- 217
Cdd:TIGR00630 488 TLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGL-HQ-RDNRRLiNTLKRLRDLGNTLIVVEHD-EDTIRAADYVIDIgp 564
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 514971686 218 ----HQGEIIQIGTPKALYRQPATLfAARYFSALNEI--PAQR 254
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILANPDSL-TGQYLSGRKKIevPAER 606
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-203 |
4.73e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 17 LSKQFGSrFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQ-----QQIPAEA--RNI 89
Cdd:PRK13409 346 LTKKLGD-FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdYDGTVEDllRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYALFPHLsvldNVMFGLKKLpkaqrqavaeqalqhvsmqhhLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:PRK13409 425 TDDLGSSYYKSEI----IKPLQLERL---------------------LDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190
....*....|....*....|....*....|....*...
gi 514971686 170 PFSNLD--HRLR--DQIRQntieILKQTGTTTVIVTHD 203
Cdd:PRK13409 480 PSAHLDveQRLAvaKAIRR----IAEEREATALVVDHD 513
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-223 |
1.32e-10 |
|
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: 60.35 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 34 AQRGQIICLLGHSGCGKTTMLRLIAGLeTPSSGSIqlEQQILWN------EQQQIPAEarnIGLVFQDYALFPHLSVLDN 107
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSV--EGDIHYNgipykeFAEKYPGE---IIYVSEEDVHFPTLTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 108 VMFGLKKlpkaqrqavaeQALQHVSmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTI 187
Cdd:cd03233 104 LDFALRC-----------KGNEFVR----------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 514971686 188 EILKQTGTTTVIVTHDP-EEALQIADQIILMHQGEII 223
Cdd:cd03233 163 TMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-203 |
1.44e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.84 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQilWNEqqqIPAEARniGLVFQDYalFPHLsvLDNVMFGLKK-- 114
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD--WDE---ILDEFR--GSELQNY--FTKL--LEGDVKVIVKpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 ----LPKAQRQAVAE------------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:cd03236 95 yvdlIPKAVKGKVGEllkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*
gi 514971686 179 RDQIRQnTIEILKQTGTTTVIVTHD 203
Cdd:cd03236 175 RLNAAR-LIRELAEDDNYVLVVEHD 198
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
143-226 |
1.59e-10 |
|
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: 60.35 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLL--MDEPFSNLDHRLRDQIRqNTIEILKQTGTTTVIVTHDpEEALQIADQIILM--- 217
Cdd:cd03270 137 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLI-ETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIgpg 214
|
90
....*....|..
gi 514971686 218 ---HQGEIIQIG 226
Cdd:cd03270 215 agvHGGEIVAQG 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-223 |
1.70e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 14 IRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILwNEQQQIPAEARNIGLVF 93
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 94 QDYALFPHLSVLDNVMFGL----------KKLPKAQRQAVAEQAL-----QHVSmqhhlhsypyTLSGGEQQRVALARAL 158
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRyptkgmfvdqDKMYRDTKAIFDELDIdidprAKVA----------TLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 159 APKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFT-IIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-175 |
1.98e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLeqqilwneqqqipAEARNI 89
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-------------GETVKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDY-ALFPHLSV-------LDNVMFGLKKLPkaQRQAVA-------EQAlQHVSMqhhlhsypytLSGGEQQRVAL 154
Cdd:PRK11819 390 AYVDQSRdALDPNKTVweeisggLDIIKVGNREIP--SRAYVGrfnfkggDQQ-KKVGV----------LSGGERNRLHL 456
|
170 180
....*....|....*....|.
gi 514971686 155 ARALAPKPQVLLMDEPFSNLD 175
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLD 477
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-202 |
7.67e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQ-------QILWNEQQqipaearnIGLVFQDYALFPHlS 103
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdiNLKWWRSK--------IGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 104 VLDNVMFGLKKLP-------------------------------------------------KAQRQAVAEQALQHVSMQ 134
Cdd:PTZ00265 476 IKNNIKYSLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemRKNYQTIKDSEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 135 HHLHSY---------------PYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTIEILK-QTGTTTV 198
Cdd:PTZ00265 556 VLIHDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKgNENRITI 634
|
....
gi 514971686 199 IVTH 202
Cdd:PTZ00265 635 IIAH 638
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-203 |
1.04e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSI----QLEqqILWNEQQQIpaea 86
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLE--VAYFDQHRA---- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 rniglvfqdyALFPHLSVLDNVMFGLKKL-------------------PKAQRQAVAeqalqhvsmqhhlhsypyTLSGG 147
Cdd:PRK11147 393 ----------ELDPEKTVMDNLAEGKQEVmvngrprhvlgylqdflfhPKRAMTPVK------------------ALSGG 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 148 EQQRVALARALApKPQVLL-MDEPFSNLDhrlrdqirQNTIEILKQTGT----TTVIVTHD 203
Cdd:PRK11147 445 ERNRLLLARLFL-KPSNLLiLDEPTNDLD--------VETLELLEELLDsyqgTVLLVSHD 496
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-243 |
1.57e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 31 SWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQqqiPAEARNIG--LVFQD---YALFPHLSVL 105
Cdd:PRK10982 268 SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN---ANEAINHGfaLVTEErrsTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 106 DNVM----------FGL---KKLPKAQRQAVAEQALQHVSMQHHLHSypytLSGGEQQRVALARALAPKPQVLLMDEPFS 172
Cdd:PRK10982 345 FNSLisnirnyknkVGLldnSRMKSDTQWVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 173 NLDHRLRDQIRQNTIEILKQtGTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPKALYRQPATLFAARY 243
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRLASLH 490
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
10-226 |
1.81e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMlRLIAGLETPSSGSiQLEQQILWNEQQQipAEARNI 89
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR-RPWRF*TWCANRR--ALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GL-------VFQDYALFPHLSVLDNVMfglkKLPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKP 162
Cdd:NF000106 88 G*hrpvr*gRRESFSGRENLYMIGR*L----DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEV-WDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-235 |
2.50e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 27 VHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQqipaearniglvfqdyALFPHLSVLD 106
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ----------------AWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 107 NVMF----GLKKLPKAQRQAVAEQALQHVS--MQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRD 180
Cdd:PTZ00243 740 NILFfdeeDAARLADAVRVSQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 514971686 181 QIRQNTIeILKQTGTTTVIVTHDPeEALQIADQIILMHQGEIIQIGTPKALYRQP 235
Cdd:PTZ00243 820 RVVEECF-LGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-222 |
4.24e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 20 QFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGlETPSSGSIQLeqqILWNEQ----QQIPAEARNIGLV--- 92
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSNDL---TLFGRRrgsgETIWDIKKHIGYVsss 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 93 -FQDYALfpHLSVLDNVMFGL-------KKLPKAQRQaVAEQALQHVSMQHHLHSYPY-TLSGGeQQRVAL-ARALAPKP 162
Cdd:PRK10938 345 lHLDYRV--STSVRNVILSGFfdsigiyQAVSDRQQK-LAQQWLDILGIDKRTADAPFhSLSWG-QQRLALiVRALVKHP 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 163 QVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVI-VTHDPEEALQ-IADQIILMHQGEI 222
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRR-FVDVLISEGETQLLfVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-221 |
5.33e-09 |
|
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: 57.87 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiQLEQQILWNEqqqipaearniglVFQDYA---LFPHLSVLDNvmfG 111
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG--DYDEEPSWDE-------------VLKRFRgteLQDYFKKLAN---G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 112 LKK----------------------LPKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDE 169
Cdd:COG1245 159 EIKvahkpqyvdlipkvfkgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514971686 170 PFSNLDhrlrdqIRQ-----NTIEILKQTGTTTVIVTHDpeeaLQI----ADQIILMHqGE 221
Cdd:COG1245 239 PSSYLD------IYQrlnvaRLIRELAEEGKYVLVVEHD----LAIldylADYVHILY-GE 288
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
17-221 |
5.73e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 17 LSKQFGSRFAVHQASwSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWNEQQQIpaearniglvfqdy 96
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 97 alfphlsvldnvmfglkklpkaqrqavaeqalqhvsmqhhlhsypyTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDH 176
Cdd:cd03222 71 ----------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 514971686 177 RLRDQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMhQGE 221
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGE 148
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-247 |
6.38e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQ-LEQQIlwneqqqipAEARNI 89
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDM---------ADARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 90 GLVFQDYA---------LFPHLSVLDNV-----MFGLkklPKAQRQAVAEQALQHVSMqhhlhsYPYT------LSGGEQ 149
Cdd:NF033858 72 RAVCPRIAympqglgknLYPTLSVFENLdffgrLFGQ---DAAERRRRIDELLRATGL------APFAdrpagkLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 150 QRVALARALAPKPQVLLMDEPFSNLD--HR-----LRDQIRQntieilkQTGTTTVIV-THDPEEALQIaDQIILMHQGE 221
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDplSRrqfweLIDRIRA-------ERPGMSVLVaTAYMEEAERF-DWLVAMDAGR 214
|
250 260
....*....|....*....|....*...
gi 514971686 222 IIQIGTPKALYRQ--PATLFAAryFSAL 247
Cdd:NF033858 215 VLATGTPAELLARtgADTLEAA--FIAL 240
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-254 |
6.54e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 57.73 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKpqvlLM------DEPFSNLdHRlRDQIR-QNTIEILKQTGTTTVIVTHDpEEALQIADQII 215
Cdd:COG0178 485 TLSGGEAQRIRLATQIGSG----LVgvlyvlDEPSIGL-HQ-RDNDRlIETLKRLRDLGNTVIVVEHD-EDTIRAADYII 557
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 514971686 216 LM------HQGEIIQIGTPKALYRQPATLfAARYFSALNEI--PAQR 254
Cdd:COG0178 558 DIgpgageHGGEVVAQGTPEEILKNPDSL-TGQYLSGRKRIpvPKKR 603
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
40-175 |
2.09e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 40 ICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQILWneqqqipaearnigLVFQDYalfpHLSVLD----NVMFGLKKL 115
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRM--------------AVFSQH----HVDGLDlssnPLLYMMRCF 599
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 116 PkaqrqAVAEQALQHvsmqhHLHSYP----------YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PLN03073 600 P-----GVPEQKLRA-----HLGSFGvtgnlalqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-227 |
4.24e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 10 NVLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGleTPSSgSIqLEQQILWNEQQ--QIPAEAR 87
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAY-KI-LEGDILFKGESilDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 N---IGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAE---------QALQHVSM-QHHLHSYPYT-LSGGEQQRVA 153
Cdd:CHL00131 82 AhlgIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDplefleiinEKLKLVGMdPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514971686 154 LARALAPKPQVLLMDEPFSNLDhrlRDQIRQ--NTIEILKQTGTTTVIVTHDPeEALQ--IADQIILMHQGEIIQIGT 227
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLD---IDALKIiaEGINKLMTSENSIILITHYQ-RLLDyiKPDYVHVMQNGKIIKTGD 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-234 |
4.69e-08 |
|
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: 54.92 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETpSSGSIQLEQqILWNE---QQQIPAea 86
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG-VSWNSvtlQTWRKA-- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 87 rnIGLVFQDYALF---------PHLSVLDNVMFglKKLPKAQRQAVAEQALQHVSMQhhLHSYPYTLSGGEQQRVALARA 157
Cdd:TIGR01271 1294 --FGVIPQKVFIFsgtfrknldPYEQWSDEEIW--KVAEEVGLKSVIEQFPDKLDFV--LVDGGYVLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 158 LAPKPQVLLMDEPFSNLDHRLRDQIRQNtieiLKQT-GTTTVIVTHDPEEALQIADQIIL-----MHQGEIIQ-IGTPKA 230
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKT----LKQSfSNCTVILSEHRVEALLECQQFLViegssVKQYDSIQkLLNETS 1443
|
....
gi 514971686 231 LYRQ 234
Cdd:TIGR01271 1444 LFKQ 1447
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-251 |
4.73e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETpsSGSIQLEQQILWNEQQQiPAEARNIGLVFQDYALFPHLSVLDNVMFGL---- 112
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIRISGFPKKQ-ETFARISGYCEQNDIHSPQVTVRESLIYSAflrl 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 -KKLPKAQRQAVAEQALQHV---SMQHHLHSYP--YTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRdQIRQNT 186
Cdd:PLN03140 983 pKEVSKEEKMMFVDEVMELVeldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA-AIVMRT 1061
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514971686 187 IEILKQTGTTTVIVTHDPE-EALQIADQIILMHQ-GEIIQIGTpkaLYRQPATLFaaRYFSALNEIP 251
Cdd:PLN03140 1062 VRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRgGQVIYSGP---LGRNSHKII--EYFEAIPGVP 1123
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-222 |
4.98e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 11 VLTIRQLSKQFGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQQIL--WNEQQQIPaearn 88
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKlgYFAQHQLE----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 89 igLVFQDYALFPHLSVLdnvmfglkklpkaqrqavAEQALQHvSMQHHLHSYPYT----------LSGGEQQRVALARAL 158
Cdd:PRK10636 387 --FLRADESPLQHLARL------------------APQELEQ-KLRDYLGGFGFQgdkvteetrrFSGGEKARLVLALIV 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514971686 159 APKPQVLLMDEPFSNLDHrlrdQIRQNTIEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEI 222
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
143-215 |
6.05e-08 |
|
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: 52.61 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQ------RVALARALAPKPQVLLMDEPFSNLDhrlRDQIRQNTIEILK----QTGTTTVIVTHDpEEALQIAD 212
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEerksQKNFQLIVITHD-EELVDAAD 190
|
...
gi 514971686 213 QII 215
Cdd:cd03240 191 HIY 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-226 |
7.93e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 25 FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIqleqqilwneqqQIPAEARNIGLvfqDYALFPHLSV 104
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV------------DIKGSAALIAI---SSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNV-----MFGLKklpKAQRQAVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLR 179
Cdd:PRK13545 103 IENIelkglMMGLT---KEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 514971686 180 DQIRQNTIEiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK13545 180 KKCLDKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-204 |
2.38e-07 |
|
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: 52.44 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETPSSG--SIQLEQQILWNEQQqiPAEARNiglVFQDYALFPHlSVLDNVMFGLkk 114
Cdd:TIGR00954 478 GNNLLICGPNGCGKSSLFRILGELWPVYGGrlTKPAKGKLFYVPQR--PYMTLG---TLRDQIIYPD-SSEDMKRRGL-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 115 lpkaqRQAVAEQALQHVSMQHHLH---------SYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQN 185
Cdd:TIGR00954 550 -----SDKDLEQILDNVQLTHILEreggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
170
....*....|....*....
gi 514971686 186 tieiLKQTGTTTVIVTHDP 204
Cdd:TIGR00954 625 ----CREFGITLFSVSHRK 639
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-231 |
4.42e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 142 YTLSGGEQQRVALARALAPK---PQVLLMDEPFSNLdHrlRDQIRQ--NTIEILKQTGTTTVIVTHDpEEALQIADQIIL 216
Cdd:TIGR00630 828 TTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL-H--FDDIKKllEVLQRLVDKGNTVVVIEHN-LDVIKTADYIID 903
|
90 100
....*....|....*....|.
gi 514971686 217 M------HQGEIIQIGTPKAL 231
Cdd:TIGR00630 904 LgpeggdGGGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
136-234 |
5.51e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 136 HLHSYPYT-LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDPEEALQIADQI 214
Cdd:PRK10938 127 ALLDRRFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE-LLASLHQSGITLVLVLNRFDEIPDFVQFA 205
|
90 100
....*....|....*....|
gi 514971686 215 ILMHQGEIIQIGTPKALYRQ 234
Cdd:PRK10938 206 GVLADCTLAETGEREEILQQ 225
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
143-254 |
1.25e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.46 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALAralapkPQ-------VL-LMDEPFSNLdHRlRDQIRQ-NTIEILKQTGTTTVIVTHDpEEALQIADQ 213
Cdd:PRK00349 489 TLSGGEAQRIRLA------TQigsgltgVLyVLDEPSIGL-HQ-RDNDRLiETLKHLRDLGNTLIVVEHD-EDTIRAADY 559
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 514971686 214 IILM------HQGEIIQIGTPKALYRQPATLFAArYFSALNEI--PAQR 254
Cdd:PRK00349 560 IVDIgpgagvHGGEVVASGTPEEIMKNPNSLTGQ-YLSGKKKIevPKER 607
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-203 |
1.27e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 35 QRGQIICLLGHSGCGKTTMLRLIAGLETPSSGsiQLEQQILWNEqqqIPAEARniGLVFQDYalFPHLSvlDNvmfGLK- 113
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSWDE---VLKRFR--GTELQNY--FKKLY--NG---EIKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 --------KLPKAQRQAVAE------------QALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSN 173
Cdd:PRK13409 163 vhkpqyvdLIPKVFKGKVREllkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|....
gi 514971686 174 LD--HRLR--DQIRqntiEILKqtGTTTVIVTHD 203
Cdd:PRK13409 243 LDirQRLNvaRLIR----ELAE--GKYVLVVEHD 270
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-254 |
1.64e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQ--VLLMDEPFSNLDHRLRDQIRQnTIEILKQTGTTTVIVTHDpEEALQIADQIIL---- 216
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLIN-VIKKLRDQGNTVLLVEHD-EQMISLADRIIDigpg 553
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 514971686 217 --MHQGEIIQIGTPKALYRQPATLFAARYFSALN-EIPAQR 254
Cdd:PRK00635 554 agIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTiPIPEKR 594
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-226 |
2.37e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGlETPSSgSIQLEQQILWNEQQQIPAEARNIGLVF---QDYALFPHLSVLDNVMFGLK 113
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAS-NTDGF-HIGVEGVITYDGITPEEIKKHYRGDVVynaETDVHFPHLTVGETLDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 114 -KLPKAQRQAVAEQA----LQHVSMQHHLHSYPYT----------LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRL 178
Cdd:TIGR00956 165 cKTPQNRPDGVSREEyakhIADVYMATYGLSHTRNtkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 514971686 179 RDQIRQNTIEILKQTGTTTVIVTHDP-EEALQIADQIILMHQGEIIQIG 226
Cdd:TIGR00956 245 ALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQIYFG 293
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-220 |
3.42e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 37 GQIICLLGHSGCGKTTMLRLIAGLETpssGSIQLEQQILWNEQQQIPAEARNIGLVFQDYALFPHLSVLDNVMFGL---- 112
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAylrq 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 113 -KKLPKAQRQAVAEQALQHVSMQhhlhSYPYTLSG--GE------QQRVALARALAPKPQVLL-MDEPFSNLDHRLRDQI 182
Cdd:TIGR00956 866 pKSVSKSEKMEYVEEVIKLLEME----SYADAVVGvpGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
170 180 190
....*....|....*....|....*....|....*....
gi 514971686 183 RQnTIEILKQTGTTTVIVTHDPEEAL-QIADQIILMHQG 220
Cdd:TIGR00956 942 CK-LMRKLADHGQAILCTIHQPSAILfEEFDRLLLLQKG 979
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-231 |
3.50e-06 |
|
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: 47.93 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQLSKQF--GSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETpSSGSIQLEQqILWNeqqQIPAEA--R 87
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-VSWN---SVPLQKwrK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 88 NIGLVFQDYALF---------PH--------LSVLDNVmfGLKklpkaqrqAVAEQALQHVSMQhhLHSYPYTLSGGEQQ 150
Cdd:cd03289 78 AFGVIPQKVFIFsgtfrknldPYgkwsdeeiWKVAEEV--GLK--------SVIEQFPGQLDFV--LVDGGCVLSHGHKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 151 RVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQntieILKQT-GTTTVIVTHDPEEALQIADQIILMHQGEIIQIGTPK 229
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRK----TLKQAfADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQ 221
|
..
gi 514971686 230 AL 231
Cdd:cd03289 222 KL 223
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-203 |
5.42e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 36 RGQIICLLGHSGCGKTTMLRLIA-GLETPSSGSIQLEQQILWneqqqIPAEARNIGLVFQ-------------DYALFPH 101
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLIN-----VGSEEASVELEFEhggkryrierrqgEFAEFLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 102 ---------------LSVLDNVMFGLKKLPKAQRQAVAEQALQHVSMQHHLHSY-----PYTLSGGEQQRVALARALApk 161
Cdd:COG0419 97 akpserkealkrllgLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALADLLS-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 514971686 162 pqvLLMDepFSNLDHRLRDQIrqntIEILKQTGtttvIVTHD 203
Cdd:COG0419 175 ---LILD--FGSLDEERLERL----LDALEELA----IITHV 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
145-239 |
5.69e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 145 SGGEQQRVALARALAPKPQ-VLLMDEPFSNLDHRLRDQIrQNTIeiLKQTGTTTVI-VTHDPEEALQIaDQIILMHQGEI 222
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQI-QATV--MSAFSAYTVItIAHRLHTVAQY-DKIIVMDHGAV 1522
|
90
....*....|....*..
gi 514971686 223 IQIGTPKALYRQPATLF 239
Cdd:PTZ00243 1523 AEMGSPRELVMNRQSIF 1539
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-251 |
6.48e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 121 QAVAEQALQHVSMQHHLhsypYTLSGGEQQRVALARAL---APKPQVLLMDEPFSNL-DHRLRDQIrqNTIEILKQTGTT 196
Cdd:PRK00635 791 HALCSLGLDYLPLGRPL----SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhTHDIKALI--YVLQSLTHQGHT 864
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 197 TVIVTHDpEEALQIADQII-LMHQG--------------EIIQIGTPKALYRQPatlfaarYFSALNEIP 251
Cdd:PRK00635 865 VVIIEHN-MHVVKVADYVLeLGPEGgnlggyllascspeELIHLHTPTAKALRP-------YLSSPQELP 926
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-228 |
6.76e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 126 QALQHVSMQH-HLHSYPYTLSGGEQQRVALARAL---APKPQVLLMDEPFSNLD-----------HRLRDQirqntieil 190
Cdd:cd03271 151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHfhdvkkllevlQRLVDK--------- 221
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 514971686 191 kqtGTTTVIVTHDpEEALQIADQIILM------HQGEIIQIGTP 228
Cdd:cd03271 222 ---GNTVVVIEHN-LDVIKCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-226 |
1.16e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 25 FAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQleqqilwnEQQQIPAEARNIGLVFQdyalfphLSV 104
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD--------RNGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 105 LDNVMFGLKKLPKAQRQ--AVAEQALQHVSMQHHLHSYPYTLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQI 182
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEikAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 514971686 183 RQNTIEiLKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQIG 226
Cdd:PRK13546 183 LDKIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
143-217 |
2.95e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.57 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQV----------LLMDEPFSNLDHRLRDQIrQNTIEILKQTGTTTVIVTHDPEEALQIAD 212
Cdd:cd03279 123 TLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAV-ATALELIRTENRMVGVISHVEELKERIPQ 201
|
....*
gi 514971686 213 QIILM 217
Cdd:cd03279 202 RLEVI 206
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-256 |
4.16e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 12 LTIRQlskqfGSRFAVHQASWSAQRGQIICLLGHSGCGKTTMLRLIAGLETPSSGSIQLEQ--QILWNEQQ----QIPA- 84
Cdd:PRK10636 7 LQIRR-----GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQEtpalPQPAl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 85 --------EARNIGLVFQDYALFPHLSVLDNVMFGLKKLPKAQRQAVAEQALQHVSM-QHHLHSYPYTLSGGEQQRVALA 155
Cdd:PRK10636 82 eyvidgdrEYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 156 RALAPKPQVLLMDEPFSNLDhrLRDQIRQNtiEILKQTGTTTVIVTHDPEEALQIADQIILMHQGEIIQ-IGTPKALYRQ 234
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD--LDAVIWLE--KWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEyTGNYSSFEVQ 237
|
250 260
....*....|....*....|..
gi 514971686 235 PATLFAARyfSALNEIPAQRVA 256
Cdd:PRK10636 238 RATRLAQQ--QAMYESQQERVA 257
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
143-239 |
7.18e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLrDQIRQNTI-EILKQtgTTTVIVTHDPEEALQiADQIILMHQGE 221
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSLIQRTIrEEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQ 1446
|
90
....*....|....*...
gi 514971686 222 IIQIGTPKALYRQPATLF 239
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSAF 1464
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-175 |
8.38e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 8.38e-05
10 20 30
....*....|....*....|....*....|...
gi 514971686 143 TLSGGEQQRVALARALAPKPQVLLMDEPFSNLD 175
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
144-234 |
1.40e-04 |
|
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: 44.17 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIrQNTIEilKQTGTTTVIVTHDPEEALQIADQIILMHQGEII 223
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI-QSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
90
....*....|.
gi 514971686 224 QIGTPKALYRQ 234
Cdd:TIGR00957 1499 EFGAPSNLLQQ 1509
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-217 |
2.09e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514971686 144 LSGGEQQRVALARALA-----PKPQVLLmDEPFSNLDHRlRDQIRQNTIEILKQTGTTTVIVTHDPEEALqIADQIILM 217
Cdd:cd03227 78 LSGGEKELSALALILAlaslkPRPLYIL-DEIDRGLDPR-DGQALAEAILEHLVKGAQVIVITHLPELAE-LADKLIHI 153
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
144-241 |
2.29e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLdhrlrDQIRQNTIEILKQTG---TTTVIVTHDPEEALQiADQIILMHQG 220
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASI-----DMATENILQKVVMTAfadRTVVTIAHRVSTILD-ADLVLVLSRG 230
|
90 100
....*....|....*....|.
gi 514971686 221 EIIQIGTPKALYRQPATLFAA 241
Cdd:cd03288 231 ILVECDTPENLLAQEDGVFAS 251
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
143-228 |
2.38e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQ---VLLMDEPFSNL---D--------HRLRDQirqntieilkqtGTTTVIVTHDpeeaL 208
Cdd:PRK00349 830 TLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDirkllevlHRLVDK------------GNTVVVIEHN----L 893
|
90 100
....*....|....*....|....*....
gi 514971686 209 QI---ADQIILM------HQGEIIQIGTP 228
Cdd:PRK00349 894 DViktADWIIDLgpeggdGGGEIVATGTP 922
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-228 |
2.68e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 143 TLSGGEQQRVALARALAPKPQ---VLLMDEPFSNL---D--------HRLRDQirqntieilkqtGTTTVIVTHDPeEAL 208
Cdd:COG0178 826 TLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDirkllevlHRLVDK------------GNTVVVIEHNL-DVI 892
|
90 100
....*....|....*....|....*.
gi 514971686 209 QIADQIILM------HQGEIIQIGTP 228
Cdd:COG0178 893 KTADWIIDLgpeggdGGGEIVAEGTP 918
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
143-192 |
3.03e-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: 39.14 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514971686 143 TLSGGEQQR---VALARALA----------PKPQVLLMDEPFSNLDHRLRDQIrqntIEILKQ 192
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTA----LELLRA 90
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
112-232 |
4.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 112 LKKLpKAQRQAVAEQALQHVSMQHHLHSypytLSGGEQQRVALARAL--APK-PQVLLMDEPFSNLDHRLRDQIrQNTIE 188
Cdd:PRK00635 1673 LKKI-QKPLQALIDNGLGYLPLGQNLSS----LSLSEKIAIKIAKFLylPPKhPTLFLLDEIATSLDNQQKSAL-LVQLR 1746
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 514971686 189 ILKQTGTTTVIVTHDPeEALQIADQIILM------HQGEIIQIGTPKALY 232
Cdd:PRK00635 1747 TLVSLGHSVIYIDHDP-ALLKQADYLIEMgpgsgkTGGKILFSGPPKDIS 1795
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
284-352 |
1.05e-03 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 37.21 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514971686 284 RPHQVQVFSQPTtgAIPATVLSSSFMGHAEQLRLQLDPETIILAQVSPAQT---AYQEQVYVRLDLQQCFFF 352
Cdd:pfam08402 4 RPEKIRLAAAAN--GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHArppAPGDRVGLGWDPEDAHVL 73
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
144-170 |
2.57e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 2.57e-03
10 20
....*....|....*....|....*..
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEP 170
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
145-240 |
3.66e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 145 SGGEQQRVALARALAPKPQVLLMDEPFSNLDHRlRDQIRQNTI-EILKqtGTTTVIVTHDPEEALQiADQIILMHQGEII 223
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIrEEFK--SCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
90
....*....|....*..
gi 514971686 224 QIGTPKALYRQPATLFA 240
Cdd:PLN03130 1452 EFDTPENLLSNEGSAFS 1468
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
144-226 |
4.36e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514971686 144 LSGGEQQRVALARALAPKPQVLLMDEPFSNLDHRLRDQIRQNTIEILKQTGTTTVIVTHDPE-EALQIADQIILMHQGEI 222
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPApETFDLFDDIILLSEGQI 416
|
....
gi 514971686 223 IQIG 226
Cdd:PLN03140 417 VYQG 420
|
|
|