|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-347 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 593.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPSMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 241 LFEGGVSDGGFRIeGGVSLPLPPQLSHSAARTY--GIRPEDLDIAETG---IPATVLTVEPTGAETHLSVRVGTQTATIV 315
Cdd:COG3839 241 LLPGTVEGGGVRL-GGVRLPLPAALAAAAGGEVtlGIRPEHLRLADEGdggLEATVEVVEPLGSETLVHVRLGGQELVAR 319
|
330 340 350
....*....|....*....|....*....|...
gi 644976330 316 LHRRVDLKPDQQIDLAPKSEKIHLFSAE-GRRM 347
Cdd:COG3839 320 VPGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-348 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 529.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPSM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 240 NLFEGGVSDGG--FRIEGGVSLPLPPQLSHSAAR--TYGIRPEDLDIA--ETGIPATVLTVEPTGAETHLSVRVGTQTAT 313
Cdd:PRK11650 241 NLLDGRVSADGaaFELAGGIALPLGGGYRQYAGRklTLGIRPEHIALSsaEGGVPLTVDTVELLGADNLAHGRWGGQPLV 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 644976330 314 IVLHRRVDLKPDQQIDLAPKSEKIHLFSAE-GRRMD 348
Cdd:PRK11650 321 VRLPHQERPAAGSTLWLHLPANQLHLFDADtGRRIE 356
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-342 |
7.65e-155 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 438.38 E-value: 7.65e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspSMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 241 LFEG---GVSDGGFRIEGG-VSLPLPPQLSHSAARTYGIRPEDLDIAETG----IPATVLTVEPTGAETHLSVRVGTQ-- 310
Cdd:COG3842 241 LLPGtvlGDEGGGVRTGGRtLEVPADAGLAAGGPVTVAIRPEDIRLSPEGpengLPGTVEDVVFLGSHVRYRVRLGDGqe 320
|
330 340 350
....*....|....*....|....*....|...
gi 644976330 311 -TATIVLHRRVDLKPDQQIDLAPKSEKIHLFSA 342
Cdd:COG3842 321 lVVRVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-345 |
6.57e-149 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 424.06 E-value: 6.57e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPSMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 241 LFE---GGVSDGGFRIE--GGVSLPLP---PQLSHSAARTYGIRPEDL---DIAETGIPATVLTVEPTGAETHLSVRVGT 309
Cdd:PRK11000 241 FLPvkvTATAIEQVQVElpNRQQVWLPvegRGVQVGANMSLGIRPEHLlpsDIADVTLEGEVQVVEQLGNETQIHIQIPA 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 644976330 310 QTATIVLHRR--VDLKPDQQIDLAPKSEKIHLFSAEGR 345
Cdd:PRK11000 321 IRQNLVYRQNdvVLVEEGATFAIGLPPERCHLFREDGT 358
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.45e-129 |
|
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: 368.89 E-value: 1.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-339 |
1.26e-119 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 349.06 E-value: 1.26e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN-DVAPKERDIAMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPsmNL 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV--NV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 242 FEGGVSDGGFRIeGGVSLPLPPQLSHSAARTYgIRPEDLDIA-----ETGIPATVLTVEPTGAETHLSVRVGTQTATIVL 316
Cdd:COG1118 240 LRGRVIGGQLEA-DGLTLPVAEPLPDGPAVAG-VRPHDIEVSrepegENTFPATVARVSELGPEVRVELKLEDGEGQPLE 317
|
330 340 350
....*....|....*....|....*....|
gi 644976330 317 -------HRRVDLKPDQQIDLAPKSEKIHL 339
Cdd:COG1118 318 aevtkeaWAELGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
3.61e-115 |
|
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: 333.43 E-value: 3.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-284 |
1.17e-110 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 327.29 E-value: 1.17e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYP 88
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK09452 100 HMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 169 RVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspSMNLFEGGV-- 246
Cdd:PRK09452 180 RKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFDATVie 257
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 644976330 247 --SDGGFRIE-GGVSLPLPPQLSHSAARTYGI--RPEDLDIAE 284
Cdd:PRK09452 258 rlDEQRVRANvEGRECNIYVNFAVEPGQKLHVllRPEDLRVEE 300
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-341 |
2.03e-110 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 325.84 E-value: 2.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspSMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 241 LFEGGVSDGG-FRIEGGVSLPLPPQLSHSAARTYGIRPEDLDI-----AETGIPATVLTVEPTGAETHLSVRV-GTQTAT 313
Cdd:TIGR03265 240 WLPGTRGGGSrARVGGLTLACAPGLAQPGASVRLAVRPEDIRVspagnAANLLLARVEDMEFLGAFYRLRLRLeGLPGQA 319
|
330 340 350
....*....|....*....|....*....|....
gi 644976330 314 IVLH------RRVDLKPDQQIDLAPKSEKIHLFS 341
Cdd:TIGR03265 320 LVADvsasevERLGIRAGQPIWIELPAERLRAFA 353
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-216 |
1.80e-107 |
|
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: 312.92 E-value: 1.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYA 85
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 166 AKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-327 |
3.92e-105 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 312.42 E-value: 3.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPsmNLFE 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 244 GGVSDGGFRIeGGVSLPLPPQLSHSAAR---TYGIRPEDLDIAETGIPA---TVLTVEPTGAetHLSVRVGTQTATIVLH 317
Cdd:PRK11432 245 ATLSGDYVDI-YGYRLPRPAAFAFNLPDgecTVGVRPEAITLSEQGEESqrcTIKHVAYMGP--QYEVTVDWHGQELLLQ 321
|
330
....*....|.
gi 644976330 318 -RRVDLKPDQQ 327
Cdd:PRK11432 322 vNATQLQPDLG 332
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
21-340 |
2.29e-95 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 287.66 E-value: 2.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND-----VAPKERDIAMVFQSYALYPHMTVREN 95
Cdd:NF040933 24 NVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPEDRNIGMVFQNWALYPNMTVFDN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSE 175
Cdd:NF040933 104 IAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVLLLDEPFSNLDARIRDSARAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 176 IKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspSMNLFEGGVSDGGFRIEG 255
Cdd:NF040933 184 VKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLIG--DINLLEGKVEEEGLVDGN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 256 GVSLPLPPQLSHSAARTYGIRPEDLDIAETGI----------PATVLTVEPTGAETHLSVR--VGTQTATIVLHRRVdLK 323
Cdd:NF040933 262 DLKIPLPNPKLEAGEVIIGIRPEDIDISESDMrlppgfvevgKGRVKVSSYAGGVFRVVVSpiDDDSIEIIVNSDRP-IE 340
|
330
....*....|....*..
gi 644976330 324 PDQQIDLAPKSEKIHLF 340
Cdd:NF040933 341 EGEEVNLYVRPDKIKIF 357
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-337 |
2.20e-92 |
|
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: 278.99 E-value: 2.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 34 LVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKL 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 114 VSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 194 QIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspSMNLFEGGV--SDGGFRIEGGV---------SLPLP 262
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIG--EINVFEATVieRKSEQVVLAGVegrrcdiytDVPVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 263 PQLSHSAArtygIRPEDLDIAE-------TGIPATVLTVEPTGAETHLSVRVGTQTATIVL------HRRVDLKPDQQ-- 327
Cdd:TIGR01187 239 KDQPLHVV----LRPEKIVIEEedeanssNAIIGHVIDITYLGMTLEVHVRLETGQKVLVSeffnedDPHMSPSIGDRvg 314
|
330
....*....|
gi 644976330 328 IDLAPKSEKI 337
Cdd:TIGR01187 315 LTWHPGSEVV 324
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
1.07e-91 |
|
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: 273.83 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQ 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGR----DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 159 EPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGS 236
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
7.10e-86 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 258.96 E-value: 7.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-305 |
1.29e-85 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 262.33 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGR----DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 159 EPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspS 238
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--E 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 239 MNLFEGGVSDGGFRIeGGVSLPLPPQLSHSAARTYGIRPEDLDI-----AETGIPATVLTVEPTGAETHLSV 305
Cdd:PRK10851 240 VNRLQGTIRGGQFHV-GAHRWPLGYTPAYQGPVDLFLRPWEVDIsrrtsLDSPLPVQVLEVSPKGHYWQLVV 310
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
1.15e-83 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 254.24 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERD 76
Cdd:COG1116 5 APALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 IAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 157 FDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRA--GRIEQI 215
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
1.49e-80 |
|
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: 244.69 E-value: 1.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPkerDIAM 79
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVM--RAGRIEQI 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-244 |
1.39e-79 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 247.83 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYA 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 166 AKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGspSMNLFEG 244
Cdd:PRK11607 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG--SVNVFEG 258
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-340 |
1.67e-78 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 244.21 E-value: 1.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYPHMTVRENMGF 98
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKE 178
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 179 LHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPsmNLFEGGVSDGGF-RI--EG 255
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGVAEKGGEgTIldTG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 256 GVSLPLPpqlSHSAARTY-GIRPEDLDIAETGI--------PATVLTVEPTGAETHLSVRVGtQTATIVLHRR----VDL 322
Cdd:NF040840 254 NIKIELP---EEKKGKVRiGIRPEDITISTEKVktsarnefKGKVEEIEDLGPLVKLTLDVG-IILVAFITRSsfldLEI 329
|
330
....*....|....*...
gi 644976330 323 KPDQQIDLAPKSEKIHLF 340
Cdd:NF040840 330 NEGKEVYASFKASAVHVF 347
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-235 |
7.54e-78 |
|
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: 238.39 E-value: 7.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYPHMTVRENMGFAL 100
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 101 KLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELH 180
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 181 QRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIG 235
Cdd:cd03299 177 KEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-236 |
1.27e-77 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 240.38 E-value: 1.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASV-IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQ 82
Cdd:COG1125 4 FENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEP--LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGS 236
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-237 |
8.21e-74 |
|
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: 228.34 E-value: 8.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS-VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMV 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEP--LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 159 EPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSP 237
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-211 |
6.49e-72 |
|
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: 221.29 E-value: 6.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND----VAPKERDIAMVF 81
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHMTVRENMGFAlklqgrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:cd03229 83 QDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-216 |
8.77e-68 |
|
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: 211.77 E-value: 8.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 28 DGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND------VAPKERDIAMVFQSYALYPHMTVRENMGFALK 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 102 LQGRDKATInkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQ 181
Cdd:cd03297 102 RKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 644976330 182 RLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
4.17e-67 |
|
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: 210.42 E-value: 4.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERD--- 76
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 ---IAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPK 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 154 VFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQiEAMTMADKIVVMRAGRI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-234 |
1.20e-66 |
|
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: 210.96 E-value: 1.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 7 DRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE------RDIAMV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFI 234
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
1.71e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 209.13 E-value: 1.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASV-AIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER 75
Cdd:COG1136 1 MSPLlELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 76 D------IAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 150 RHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQiEAMTMADKIVVMRAGRIE 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-328 |
3.59e-64 |
|
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: 207.26 E-value: 3.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND------VAPKERDIAMVFQSYALYPHMTVREN 95
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALKLQGRDKATINklVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSE 175
Cdd:COG4148 98 LLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 176 IKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNntFVAAFIGSPSMNLFEGGVS----DGG- 250
Cdd:COG4148 176 LERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEAGSVLEATVAahdpDYGl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 251 --FRIEGG-VSLPLPPQLSHSAARtYGIRPEDLDIA---ETGI------PATVLTVEPT-GAETHLSVRVGTQT--ATIV 315
Cdd:COG4148 254 trLALGGGrLWVPRLDLPPGTRVR-VRIRARDVSLAlepPEGSsilnilPGRVVEIEPAdGGQVLVRLDLGGQTllARIT 332
|
330
....*....|....*
gi 644976330 316 LH--RRVDLKPDQQI 328
Cdd:COG4148 333 RRsaDELGLAPGQTV 347
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-235 |
3.86e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 198.29 E-value: 3.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERDIA----- 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE---DLTDSKKDINklrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 --MVFQSYALYPHMTVRENMGFAL-KLQGRDKAtinklvsEAAGIlALEpLLERL---------PKQLSGGQRQRVAMGR 146
Cdd:COG1126 79 vgMVFQQFNLFPHLTVLENVTLAPiKVKKMSKA-------EAEER-AME-LLERVgladkadayPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 147 AIVRHPKVFLFDEPLSNPDAKlrvtMRSE----IKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPE----LVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
250
....*....|...
gi 644976330 223 DRPNNTFVAAFIG 235
Cdd:COG1126 225 ENPQHERTRAFLS 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-236 |
1.09e-61 |
|
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: 197.33 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDI 77
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSY--ALYPHMTVRENMGFALKLQGRDkaTINKLVSEAAGILALEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 155 FLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDqIEAMT-MADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAF 233
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
...
gi 644976330 234 IGS 236
Cdd:COG1124 239 LAA 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-235 |
1.84e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.51 E-value: 1.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVihgvSAD--IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQS 83
Cdd:COG3840 4 LDDLTYRYGDFPL----RFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFA----LKLQGRDKATinklVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:COG3840 80 NNLFPHLTVAQNIGLGlrpgLKLTAEQRAQ----VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIG 235
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
5.05e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.59 E-value: 5.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR--VMNDVAPKERdIAMVF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvARDPAEVRRR-IGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-225 |
9.68e-60 |
|
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: 191.78 E-value: 9.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQsyalYP-----HM 90
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ----NPddqlfAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRV 170
Cdd:COG1122 92 TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 171 TMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG1122 172 ELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
6.34e-59 |
|
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: 198.20 E-value: 6.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS-----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE---- 74
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 -RDIAMVFQ--SYALYPHMTVRENMGFALKLQGR-DKATINKLVSEAAGILALEP-LLERLPKQLSGGQRQRVAMGRAIV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 150 RHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDqIEAM-TMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-234 |
1.53e-58 |
|
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: 189.03 E-value: 1.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERD-----IA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALYPHMTVRENMGFALKLQGR-DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 158 DEPLSNPDAklrVTMRS---EIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLyDRPNNTFVAAFI 234
Cdd:COG1127 166 DEPTAGLDP---ITSAVideLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWVRQFL 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-211 |
1.16e-57 |
|
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: 185.75 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQsyalYP-HM 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ----NPdDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 ----TVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:cd03225 88 ffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644976330 167 KLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:cd03225 168 AGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
2.54e-56 |
|
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: 182.34 E-value: 2.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK----ERDIAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVRENMGFAL-KLQGRDKATINKLvseAAGILALEPLLER---LPKQLSGGQRQRVAMGRAIVRHPKVF 155
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEER---ALELLEKVGLADKadaYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 156 LFDEPLSNPDAKlrvtMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03262 158 LFDEPTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-234 |
4.94e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 182.60 E-value: 4.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 8 RVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDI----AMVFQS 83
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFA-LKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:PRK09493 86 FYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 163 NPDAKLR----VTMRSEIKElhqrlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFI 234
Cdd:PRK09493 166 ALDPELRhevlKVMQDLAEE-----GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-212 |
6.01e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 6.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQS 83
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPhMTVRENMGFALKLQGR--DKATINKLVSEaagiLALEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:COG4619 83 PALWG-GTVRDNLPFPFQLRERkfDRERALELLER----LGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
1.35e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 181.02 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS-VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDI 77
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 158 DEPLSN--PDAKLRVtMRSeIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG2884 162 DEPTGNldPETSWEI-MEL-LEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-216 |
5.07e-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: 179.62 E-value: 5.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER-----DIAMVFQSY--ALYPHM 90
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkEIQMVFQDPmsSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQG--RDKATINKLVSEAA-GILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:cd03257 100 TIGEQIAEPLRIHGklSKKEARKEAVLLLLvGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 644976330 168 LRVTMRSEIKELHQRLGTTIVYVTHDqIEAM-TMADKIVVMRAGRIEQIG 216
Cdd:cd03257 180 VQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-221 |
4.63e-54 |
|
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: 177.31 E-value: 4.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAMVFQS 83
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQGR-DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03261 86 GALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 163 NPDAK-LRVTMRSeIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:cd03261 166 GLDPIaSGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-218 |
2.47e-52 |
|
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: 173.69 E-value: 2.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHMTVREN--MGFA--LKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:COG1120 82 QEPPAPFGLTVRELvaLGRYphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 158 DEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-212 |
2.77e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 2.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAM 79
Cdd:COG3638 5 LRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVREN--------MGFAlklqgrdkATINKLVSEAAGILALEpLLERL---------PKQLSGGQRQRV 142
Cdd:COG3638 85 IFQQFNLVPRLSVLTNvlagrlgrTSTW--------RSLLGLFPPEDRERALE-ALERVgladkayqrADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 143 AMGRAIVRHPKVFLFDEPLSNPDAKL-RVTMRSeIKELHQRLGTTIVYVTHdQIE-AMTMADKIVVMRAGRI 212
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-234 |
5.97e-52 |
|
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: 172.35 E-value: 5.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQSY 84
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 85 ALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 165 DAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNT-FVAAFI 234
Cdd:COG4555 164 DVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEnLEDAFV 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
1.01e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.50 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE----- 74
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 RDIAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKV 154
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 155 FLFDEPLSNPDAK-----LRVtmrseIKELHQRLGTTIVYVTHD-----QIeamtmADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:COG1135 162 LLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHEmdvvrRI-----CDRVAVLENGRIVEQGPVLDVFAN 231
|
250
....*....|...
gi 644976330 225 PNNTFVAAFIGSP 237
Cdd:COG1135 232 PQSELTRRFLPTV 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
1.92e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 171.58 E-value: 1.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndVAPKERD 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP---VTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 IAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFL 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 157 FDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVM--RAGRI 212
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
2.17e-51 |
|
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: 170.45 E-value: 2.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE----- 74
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 RDIAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 155 FLFDEPLSNPDAKlrvTMRS---EIKELHQRLGTTIVYVTHdQIEAM-TMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:cd03258 162 LLCDEATSALDPE---TTQSilaLLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-225 |
7.34e-51 |
|
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: 176.63 E-value: 7.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISG---GEIRIDGRVMNDVAPKER--DIAMVFQS--YAL 86
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgrRIGMVFQDpmTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 87 YPhMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:COG1123 97 NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 167 KLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG1123 176 TTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-216 |
2.51e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 2.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN---DVAPKE----- 74
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 RDIAMVFQSYALYPHMTVRENMGFA-LKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPK 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 154 VFLFDEPLSNPDAKLRVTMRSEIKELhQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
3.66e-50 |
|
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: 166.97 E-value: 3.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDI-----SGGEIRIDGRVMN--DVAPKE-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYdlDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 RDIAMVFQSYALYPhMTVRENMGFALKLQG-RDKATINKLVSEAAGILAL-EPLLERL-PKQLSGGQRQRVAMGRAIVRH 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlgTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-226 |
4.34e-50 |
|
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: 170.68 E-value: 4.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 8 RVQKQYGAASVihGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVA------PKERDIAMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHMTVRENMGFALKLQGRDKATINKlvSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
7.60e-50 |
|
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: 165.80 E-value: 7.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 23 SADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYPHMTVRENMGFALKL 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 103 QGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 644976330 183 LGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
3.72e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 165.62 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVapkERDIAMVFQS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQGRDKATinklvsEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
1.70e-48 |
|
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: 161.03 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK-ERDIAMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMgfalklqgrdkatinklvseaagilalepllerlpkQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 644976330 163 NPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-211 |
2.46e-48 |
|
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: 162.03 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDI 77
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 158 DEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-223 |
3.27e-48 |
|
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: 162.35 E-value: 3.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAA-SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAM 79
Cdd:cd03256 3 VENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVRENMgfalkLQGR--DKATIN---KLVSEAAGILALEpLLERL---------PKQLSGGQRQRVAMG 145
Cdd:cd03256 83 IFQQFNLIERLSVLENV-----LSGRlgRRSTWRslfGLFPKEEKQRALA-ALERVglldkayqrADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 146 RAIVRHPKVFLFDEPLSNPDAKL-RVTMRSeIKELHQRLGTTIVYVTHdQIE-AMTMADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
1.03e-47 |
|
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: 161.06 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERD--- 76
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 ------IAMVFQSYALYPHMTVRENMGFALKLQGRDKATinklvSEAAGILA---LEPLLERLPKQLSGGQRQRVAMGRA 147
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAmTMADKIVVMRAGRIEQ 214
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-225 |
2.95e-46 |
|
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: 159.83 E-value: 2.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED---ISGGEIRIDGRVMNDVAPKE------RDIAMVFQ-S 83
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQdP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 Y-ALYPHMTVRENMGFALKL-QGRDKATINKLVSEA---AGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:COG0444 96 MtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELlerVGLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 159 EPLSnpdAkLRVTMRSEI----KELHQRLGTTIVYVTHDqIEAM-TMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG0444 176 EPTT---A-LDVTIQAQIlnllKDLQRELGLAILFITHD-LGVVaEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-225 |
3.56e-46 |
|
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: 156.86 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPkerDIAMVFQSYALYPHMTVRENMGF 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALK--LQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEI 176
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 644976330 177 KELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL-YDRP 225
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-224 |
5.11e-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: 5.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIA 78
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALYpHMTVRENMGFalklqGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRA 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITL-----GDPDATDEEII-EAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-225 |
1.04e-45 |
|
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: 157.23 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAMVFQsyalYPHM--- 90
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPEHqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 --TVRENMGFALKLQGRDKATINKLVSEAAGILAL-EPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:TIGR04521 97 eeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 168 LRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-223 |
2.22e-45 |
|
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: 155.15 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAA-SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAM 79
Cdd:TIGR02315 4 VENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVRENMgfalkLQGR--DKATINKLV---SEAAGILALEpLLERL---------PKQLSGGQRQRVAMG 145
Cdd:TIGR02315 84 IFQHYNLIERLTVLENV-----LHGRlgYKPTWRSLLgrfSEEDKERALS-ALERVgladkayqrADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 146 RAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-205 |
2.92e-45 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 153.54 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGrvMNDVAPKER--------DIAMV 80
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNG--QETPPLNSKkaskfrreKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQiEAMTMADKIV 205
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
1.18e-44 |
|
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: 154.13 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGrvMNDVAPKE-----RD 76
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlweirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 IAMVFQSyalyPH-----MTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRH 151
Cdd:TIGR04520 79 VGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-221 |
1.21e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 152.81 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 25 DIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYPHMTVRENMGF----AL 100
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLglnpGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 101 KLQGRDKATinklVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELH 180
Cdd:PRK10771 101 KLNAAQREK----LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 181 QRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-225 |
2.15e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 155.27 E-value: 2.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAMVFQ-SYA-LYPHMTVR 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFALKLQG-RDKATINKLVSEAAGILALEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSnpdAkLRVT 171
Cdd:COG4608 116 DIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS---A-LDVS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 172 MRSEI----KELHQRLGTTIVYVTHD-----QIeamtmADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG4608 192 IQAQVlnllEDLQDELGLTYLFISHDlsvvrHI-----SDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-221 |
2.46e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 160.33 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYpHMTVREN 95
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFalklqGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:COG1132 434 IRY-----GRPDATDEEVE-EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 165 DAklrvtmRSEiKELHQRL-----GTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:COG1132 508 DT------ETE-ALIQEALerlmkGRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-212 |
2.62e-44 |
|
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: 151.49 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSadIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQS 83
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFA----LKLQGRDKATINKlvseAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:cd03298 79 NNLFAHLTVEQNVGLGlspgLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-212 |
2.73e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 152.47 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN---DVAPKE----- 74
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 RDIAMVFQSYALYPHMTVRENMGFA-LKLQGRDKAtinKLVSEAAGILA---LEPLLERLPKQLSGGQRQRVAMGRAIVR 150
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKE---QAREKAMKLLArlrLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 151 HPKVFLFDEPLSNPDAKLRVTMRSEIKELHQrLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-212 |
3.53e-44 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 151.02 E-value: 3.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASV-IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND-----VAPKERDIAMVFQ 82
Cdd:cd03292 6 VTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 644976330 163 NPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.51e-43 |
|
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: 148.35 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 5 AIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 syalyphmtvrenmgfALKLQGrdkatinklvseaagilaLEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03214 81 ----------------ALELLG------------------LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 163 NPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-197 |
1.74e-43 |
|
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: 149.17 E-value: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINklVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 644976330 161 LSNPDAKLRVTMRSEIKElHQRLGTTIVYVTHDQIEA 197
Cdd:COG4133 159 FTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-212 |
3.13e-43 |
|
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: 148.74 E-value: 3.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER---DIAMVFQSYALYPH 89
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVREN--MGFALKLQGRDKATINKlvseaagILALEPLLERLPKQ----LSGGQRQRVAMGRAIVRHPKVFLFDEP--- 160
Cdd:cd03224 90 LTVEENllLGAYARRRAKRKARLER-------VYELFPRLKERRKQlagtLSGGEQQMLAIARALMSRPKLLLLDEPseg 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 161 LSnPdaKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03224 163 LA-P--KIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
8.64e-43 |
|
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: 145.99 E-value: 8.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAM 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYpHMTVRENMgfalklqgrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHDqIEAMTMADKIVVMRAGR 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-193 |
9.01e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 147.24 E-value: 9.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL--EDISG-GEIRIDGRVMNDVAPKERDIAMVFQ 82
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSAsGEVLLNGRRLTALPAEQRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFAL--KLQGRD-KATINKLVSEAAgilaLEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:COG4136 84 DDLLFPHLSVGENLAFALppTIGRAQrRARVEQALEEAG----LAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHD 193
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-236 |
1.54e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 148.41 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDG------------RVMNDVA 71
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgeLVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 72 PKER---DIAMVFQSYALYPHMTVRENMGFA-LKLQGRDKAtinKLVSEAAGILALEPLLERL---PKQLSGGQRQRVAM 144
Cdd:COG4598 89 QLQRirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKA---EAIERAEALLAKVGLADKRdayPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 145 GRAIVRHPKVFLFDEPLSNPDAK-----LRVtMRSEIKElhqrlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPL 219
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPElvgevLKV-MRDLAEE-----GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*..
gi 644976330 220 DLYDRPNNTFVAAFIGS 236
Cdd:COG4598 240 EVFGNPKSERLRQFLSS 256
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-211 |
2.90e-42 |
|
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: 144.31 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQs 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 yalyphmtvrenmgfalklqgrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 644976330 164 PDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:cd00267 111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
7.63e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.00 E-value: 7.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERDIAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPH--MTVRE--------NMGFALKLQGRDKAtinkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVR 150
Cdd:COG1121 81 PQRAEVDWDfpITVRDvvlmgrygRRGLFRRPSRADRE----AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 151 HPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQiGKPLDLYDRPN 226
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
9.57e-42 |
|
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: 9.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIA 78
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALyPHMTVRENMGFalklqGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRA 147
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRL-----GRPDASDEELE-AALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-236 |
1.45e-41 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 145.74 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVM---------------N 68
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrngplvpadeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 69 DVAPKERDIAMVFQSYALYPHMTVRENMGFA-LKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRA 147
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNN 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 644976330 228 TFVAAFIGS 236
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-236 |
1.72e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RD 76
Cdd:PRK11153 4 LKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 IAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFL 156
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 157 FDEPLSNPDAKlrvTMRS---EIKELHQRLGTTIVYVTHD-----QIeamtmADKIVVMRAGRIEQIGKPLDLYDRPNNT 228
Cdd:PRK11153 164 CDEATSALDPA---TTRSileLLKDINRELGLTIVLITHEmdvvkRI-----CDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*...
gi 644976330 229 FVAAFIGS 236
Cdd:PRK11153 236 LTREFIQS 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
1.74e-41 |
|
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: 142.02 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHMTVRENM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 97 GFALKLQGRDKATINKLVSEAAGILALEPLLERL----PKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-212 |
2.44e-41 |
|
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: 144.05 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDG-RVMNDVAPKERDIA 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 159 EPLSNPDAKLRVTMRSEIKELhQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
2.51e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 151.84 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQY--GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDI 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYpHMTVRENmgfaLKLqGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGR 146
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRL-ARPDATDEELW-AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 147 AIVRHPKVFLFDEPLSNPDAklrVTMRSEIKELHQRL-GTTIVYVTHDQiEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDA---ATEQALLADLLEALaGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-221 |
3.59e-41 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 144.46 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQS 83
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFalklqGR-----------DKAtinkLVSEAAGILALEPLLERLPKQLSGGQRQR--VAMgrAIVR 150
Cdd:COG4604 84 NHINSRLTVRELVAF-----GRfpyskgrltaeDRE----IIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 151 HPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-221 |
7.02e-41 |
|
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: 142.64 E-value: 7.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQ 82
Cdd:cd03263 3 IRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03263 83 FDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 163 NPDAKLRVTMRSEIKELhqRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:cd03263 163 GLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-233 |
1.30e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 144.41 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 7 DRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE------RDIAMV 80
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAF 233
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-225 |
3.60e-39 |
|
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: 138.58 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER---DIAMVFQSYALYPH 89
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVREN--MGFALklqGRDKATINKLVSEaagILALEPLLERLPKQ----LSGGQRQRVAMGRAIVRHPKVFLFDEP--- 160
Cdd:COG0410 93 LTVEENllLGAYA---RRDRAEVRADLER---VYELFPRLKERRRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPslg 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 161 LSnPdaKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG0410 167 LA-P--LIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
14-221 |
1.11e-38 |
|
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: 138.40 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAMVFQ-SY-AL 86
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 87 YPHMTVRENMGFALK-LQGRDKATINKLVSEAAGILALEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 165 DAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI-EQIGKPLDL 221
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDVAQLL 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-212 |
1.26e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 138.28 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAAS---------VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVA 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 72 PKE-----RDIAMVFQSY--ALYPHMTVRENMGFALK-LQGRDKATINKLVSEAAGILALEP-LLERLPKQLSGGQRQRV 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 143 AMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-210 |
1.50e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 137.91 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVApKERdiAMVFQSYA 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER--GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644976330 166 AKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAG 210
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-222 |
3.28e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.87 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDI----AMVFQ--SYALYPHmTVREN 95
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-TIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALKLQGRDKATINKLVSEAAGILAL--EPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMR 173
Cdd:PRK13637 105 IAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 644976330 174 SEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13637 185 NKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-212 |
7.74e-38 |
|
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: 135.26 E-value: 7.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 5 AIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER---DIAMVF 81
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHMTVRENM----------GFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRH 151
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
1.14e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.19 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSyalyPH-----M 90
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIFQN----PDnqfigA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRV 170
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 171 TMRSEIKELHQRLGTTIVYVTHDQIEAmTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-207 |
1.45e-36 |
|
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: 131.12 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERDIAMVFQSYAL---YPh 89
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRE--------NMGFALKLQGRDKAtinkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:cd03235 85 ISVRDvvlmglygHKGLFRRLSKADKA----KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVM 207
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
18-212 |
1.51e-36 |
|
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: 131.32 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER------DIAMVFQSYALYPHMT 91
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVT 171
Cdd:TIGR02211 100 ALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 172 MRSEIKELHQRLGTTIVYVTHDqIEAMTMADKIVVMRAGRI 212
Cdd:TIGR02211 180 IFDLMLELNRELNTSFLVVTHD-LELAKKLDRVLEMKDGQL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-212 |
3.01e-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: 130.41 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVFQSYALYP 88
Cdd:cd03268 6 LTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQGRDKATINklvsEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD--- 165
Cdd:cd03268 86 NLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdg 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 644976330 166 -AKLRVTMRSeikelHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03268 162 iKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.71e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 129.48 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIdGRVMNDVAPK------- 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSlsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 74 ----ERDIAMVFQSYALYPHMTVREN-MGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAI 148
Cdd:PRK11264 80 irqlRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 149 VRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-217 |
2.34e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.92 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 36 GPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND------VAPKERDIAMVFQSYALYPHMTVRENMGFALKlqGRDKAT 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 110 INKLVSeaagILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVY 189
Cdd:PRK11144 109 FDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180
....*....|....*....|....*...
gi 644976330 190 VTHDQIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-218 |
7.88e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 7.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND--VAPKERDIAM 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSyalyPH-----MTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKV 154
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 155 FLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTmADKIVVMRAGRIEQIGKP 218
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-234 |
8.24e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 128.04 E-value: 8.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISG-----GEIRIDGRVM--NDVAPKE--RDIAMVFQS 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEvrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVRENMGFALKLQG--RDKATINKLVSEAAGILAL-EPLLERL---PKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 158 DEPLSNPDAklrvTMRSEIKELHQRLGT--TIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFI 234
Cdd:PRK14267 174 DEPTANIDP----VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-212 |
1.67e-34 |
|
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: 125.45 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKER--DIAMVFQS--YAL 86
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERrkSIGYVMQDvdYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 87 YPHmTVRENMGFALKLQGRDKATINKLVSEaagiLALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:cd03226 85 FTD-SVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 644976330 167 KLRVTMRSEIKELhQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03226 160 KNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.88e-34 |
|
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: 125.77 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVtLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 163 NPDAKLRVTMRSEIKELHQrlGTTIVYVTH--DQIEAmtMADKIVVMRAGRIEQIG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVES--LCNQVAVLNKGKLVFEG 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-224 |
2.04e-34 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 126.19 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMVFQSYALYpHMTVREN 95
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGVVPQDTVLF-NDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFalklqGRDKATiNKLVSEAAGILALEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:cd03253 95 IRY-----GRPDAT-DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 165 DAklrVTMRsEIKELHQRL--GTTIVYVTHDQIEAMTmADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:cd03253 169 DT---HTER-EIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
2.87e-34 |
|
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: 125.56 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 163 NPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-225 |
3.17e-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: 131.73 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 20 HGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDiSGGEIRIDGRVMNDVAPKE-----RDIAMVFQS-YA-LYPHMTV 92
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGFALKLQ--GRDKATINKLVSEAAGILALEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSnpdaKLR 169
Cdd:COG4172 382 GQIIAEGLRVHgpGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS----ALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 170 VTMRSEI----KELHQRLGTTIVYVTHDQ--IEAmtMADKIVVMRAGRI-EQiGKPLDLYDRP 225
Cdd:COG4172 458 VSVQAQIldllRDLQREHGLAYLFISHDLavVRA--LAHRVMVMKDGKVvEQ-GPTEQVFDAP 517
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-212 |
4.63e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED-ISG----GEIRIDGRvmnDV-APKE------RDIAMV 80
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGE---DIyDPDVdvvelrRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPhMTVRENMGFALKLQG-RDKATINKLVSEAAGILAL-EPLLERLPKQ---LSGGQRQRVAMGRAIVRHPKVF 155
Cdd:COG1117 98 FQKPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALwDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 156 LFDEPLSN--PDAklrvTMRSE--IKELHQRLgtTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG1117 177 LMDEPTSAldPIS----TAKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-212 |
4.89e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 4.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-RD--IAMVFQSYALY 87
Cdd:COG1129 12 KSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAIIHQELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 PHMTVRENMgfALKLQGRDKATIN--KLVSEAAGILA-----LEPllERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:COG1129 92 PNLSVAENI--FLGREPRRGGLIDwrAMRRRARELLArlgldIDP--DTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 161 ---LSNPDAK--LRVtmrseIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG1129 168 tasLTEREVErlFRI-----IRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-226 |
5.28e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.38 E-value: 5.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVM--NDVAPKERDIAMVFQSyalyPH-----MT 91
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIGMVFQN----PDnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVT 171
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 172 MRSEIKELHQRLGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-228 |
8.35e-34 |
|
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: 124.40 E-value: 8.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED----ISGGEIRIDGRVMNDVAPKERDIAMVFQS--YALYPHMTV 92
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGFALKLQGRDKATINKLVSE---AAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLR 169
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEaleAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 170 VTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNT 228
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-214 |
8.99e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 124.54 E-value: 8.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAP------KERDIAMVFQSYALYPHMT 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVT 171
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 644976330 172 MRSEIKELHQRLGTTIVYVTHDQIEAMTMaDKIVVMRAGRIEQ 214
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-222 |
9.52e-34 |
|
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: 124.57 E-value: 9.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPhMTVREN 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFalklqGRDKATInKLVSEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:cd03249 97 IRY-----GKPDATD-EEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 165 DAKlrvtmrSEiKELHQ-----RLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:cd03249 171 DAE------SE-KLVQEaldraMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-224 |
1.21e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 123.87 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmTVREN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFalklqGRDKATiNKLVSEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:cd03254 97 IRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 165 DAKLRVTMRSEIKELHQrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:cd03254 171 DTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-212 |
1.52e-33 |
|
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: 123.16 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMnDVAPKERdIAMVFQSYALYP 88
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:cd03269 84 KMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 644976330 169 RVTMRSEIKELhQRLGTTIVYVTH--DQIEAmtMADKIVVMRAGRI 212
Cdd:cd03269 164 VELLKDVIREL-ARAGKTVILSTHqmELVEE--LCDRVLLLNKGRA 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
2.53e-33 |
|
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: 121.00 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE---RDIAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQsyalyphmtvrenmgfalklqgrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-225 |
3.40e-33 |
|
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: 129.03 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKS----TLLRMLAGLEDISGGEIRIDGRVMNDVAPKE------RDIAMVFQ--SYA 85
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQepMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKL-QGRDKATINKLVSEA---AGILALEPLLERLPKQLSGGQRQRV--AMgrAIVRHPKVFLFDE 159
Cdd:COG4172 105 LNPLHTIGKQIAEVLRLhRGLSGAAARARALELlerVGIPDPERRLDAYPHQLSGGQRQRVmiAM--ALANEPDLLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 160 PLSnpdAkLRVTMRSEI----KELHQRLGTTIVYVTHDqieaMT----MADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:COG4172 183 PTT---A-LDVTVQAQIldllKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-218 |
1.40e-32 |
|
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: 127.23 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQY-----GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIdgRV------MNDVAPKERD- 76
Cdd:TIGR03269 285 VSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--RVgdewvdMTKPGPDGRGr 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 ----IAMVFQSYALYPHMTVRENMGFALKLQ-----GRDKATInklVSEAAGIL--ALEPLLERLPKQLSGGQRQRVAMG 145
Cdd:TIGR03269 363 akryIGILHQEYDLYPHRTVLDNLTEAIGLElpdelARMKAVI---TLKMVGFDeeKAEEILDKYPDELSEGERHRVALA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 146 RAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
1.70e-32 |
|
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: 121.18 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAA--SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAM 79
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYpHMTVRENMGFalklqGRDKATiNKLVSEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAI 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY-----GRPGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 149 VRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLgTTIVyVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFV-IAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-212 |
4.37e-32 |
|
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: 118.81 E-value: 4.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISG--GEIRIDGRVMNDVAPKERdIAMVFQSYALYPHMTVREN 95
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALKLQGrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSE 175
Cdd:cd03213 103 LMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 644976330 176 IKELHQrLGTTIVYVTHD-QIEAMTMADKIVVMRAGRI 212
Cdd:cd03213 154 LRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-212 |
5.64e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.37 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVA-------PKERdia 78
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 mvfqsyALYPHMTVRENMGFALKLQGRDKATINKlvseaagilALEPLLERLP---------KQLSGGQRQRVAMGRAIV 149
Cdd:COG4152 81 ------GLYPKMKVGEQLVYLARLKGLSKAEAKR---------RADEWLERLGlgdrankkvEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 150 RHPKVFLFDEPLS--NPDAklRVTMRSEIKELHQRlGTTIVYVTH--DQIEAmtMADKIVVMRAGRI 212
Cdd:COG4152 146 HDPELLILDEPFSglDPVN--VELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRK 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-234 |
5.99e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.46 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN---------DVAPKE 74
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 R------DIAMVFQSYALYPHMTVREN-MGFALKLQGRDKATI-NKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGR 146
Cdd:PRK10619 86 QlrllrtRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEArERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 147 AIVRHPKVFLFDEPLSNPDAKLrvtmRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|.
gi 644976330 224 RPNNTFVAAFI 234
Cdd:PRK10619 242 NPQSPRLQQFL 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-212 |
7.23e-32 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 117.70 E-value: 7.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVF 81
Cdd:cd03246 3 VENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 QSYALYPHmTVRENMgfalklqgrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:cd03246 83 QDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRlGTTIVYVTHdQIEAMTMADKIVVMRAGRI 212
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
7.54e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 125.09 E-value: 7.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmT 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLQGRDkatinkLVSEAAGILALEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:TIGR02857 412 IAENIRLARPDASDA------EIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHDqIEAMTMADKIVVM 207
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-212 |
2.53e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 118.01 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER---DIAMVFQSYALYPH 89
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVREN--MGFALkLQGRDKATInklvseaAGILALEPLLE----RLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:TIGR03410 90 LTVEENllTGLAA-LPRRSRKIP-------DEIYELFPVLKemlgRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-193 |
3.32e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.57 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER------DIAMVFQSYALYPHM 90
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRV 170
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|...
gi 644976330 171 TMRSEIKELHQRLGTTIVYVTHD 193
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHD 206
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-214 |
2.63e-30 |
|
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: 121.08 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQYGAASVI-HGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIA 78
Cdd:COG5265 356 GEVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALYpHMTVRENMGFalklqGRDKATINKlVSEAAGILALEPLLERLPKQ-----------LSGGQRQRVAMGRA 147
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAY-----GRPDASEEE-VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVY------VTHdqieamtmADKIVVMRAGRI-EQ 214
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlstIVD--------ADEILVLEAGRIvER 573
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-212 |
3.08e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 114.61 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYpHMTVREN 95
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFalklqGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:cd03245 98 ITL-----GAPLADDERIL-RAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 165 DaklrvtMRSEiKELHQRL-----GTTIVYVTHdQIEAMTMADKIVVMRAGRI 212
Cdd:cd03245 172 D------MNSE-ERLKERLrqllgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-234 |
3.32e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.91 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN--------DVAPKERDIAMVFQSYALYP 88
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQG-RDKATINKLVSEAAGILAL-EPLLERL---PKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 164 PDAKLRVTMRSEIKELHQRLgtTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFI 234
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-216 |
5.40e-30 |
|
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: 120.24 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERDiamvfqsyALYPHM------- 90
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA---DLSQWDRE--------ELGRHIgylpqdv 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 -----TVREN---MGfalklqgrdKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRH 151
Cdd:COG4618 416 elfdgTIAENiarFG---------DADPEKVV-AAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQiEAMTMADKIVVMRAGRIEQIG 216
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-211 |
6.48e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGaaSVI--HGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndVAPKE-RD-----IAMVFQ 82
Cdd:COG3845 13 KRFG--GVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP---VRIRSpRDaialgIGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVREN--MGF-ALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:COG3845 88 HFMLVPNLTVAENivLGLePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 160 P---LSNPDA-KLRVTMRSEIKElhqrlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:COG3845 168 PtavLTPQEAdELFEILRRLAAE-----GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
8.58e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.62 E-value: 8.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL-----EDISGGEIRIDGRVM--NDVAPK 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 74 ERDIAMVFQSYALYPHMTVRENMGFALKLQ--GRDKATINKLVSEAAGILAL-EPLLERL---PKQLSGGQRQRVAMGRA 147
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLgtTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNN 227
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*..
gi 644976330 228 TFVAAFI 234
Cdd:PRK14247 239 ELTEKYV 245
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-212 |
1.84e-29 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.20 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYpHMTVREN 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFalklqGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:TIGR03375 559 IAL-----GAPYADDEEIL-RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 165 DaklrvtMRSEiKELHQRL-----GTTIVYVTHdQIEAMTMADKIVVMRAGRI 212
Cdd:TIGR03375 633 D------NRSE-ERFKDRLkrwlaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-226 |
2.13e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN------DVAPKERDIAMVFQsyalYP-HM---- 90
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPeHQlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQGRDKATINKLVSEAAGILAL-EPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLR 169
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 170 VTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-218 |
3.69e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.80 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFA----LKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFL 156
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 157 FDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-232 |
8.86e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.65 E-value: 8.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER-----DIAMVFQS--YALYPHMTVR 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFALKL--QGRDKATINKLVSEAAGILALEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRV 170
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 171 TMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAA 232
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKA 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-207 |
1.21e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.63 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmndvapkeRDIAMVFQSYALYPHM-- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRE--NMGF--ALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:NF040873 73 TVRDlvAMGRwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 167 KLRVTMRSEIKELHQRlGTTIVYVTHDqIEAMTMADKIVVM 207
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-240 |
1.86e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 112.75 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDV--APKE------RDIAMVFQS-YA-LYPHM 90
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ---DLlkADPEaqkllrQKIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQGRDKATINKlvSEAAGILA---LEP-LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:PRK11308 110 KVGQILEEPLLINTSLSAAERR--EKALAMMAkvgLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 167 KLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGS-PSMN 240
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSAtPRLN 262
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-217 |
2.72e-28 |
|
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: 115.14 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGfalklQGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:TIGR01842 408 VAENIA-----RFGENADPEKII-EAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVyVTHdQIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKARGITVVV-ITH-RPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-222 |
3.04e-28 |
|
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: 109.55 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER---DIAMVFQSYA 85
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 166 AKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:cd03218 166 PIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-224 |
4.66e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.40 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndVAPKErdIAMVFQsyalyPHMTVRENMG 97
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---SALLE--LGAGFH-----PELTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 FALKLQGRDKATINKLVSEaagILA---LEPLLErLP-KQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMR 173
Cdd:COG1134 111 LNGRLLGLSRKEIDEKFDE---IVEfaeLGDFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 174 SEIKELHQRlGTTIVYVTHD--QIEamTMADKIVVMRAGRIEQIGKP---LDLYDR 224
Cdd:COG1134 187 ARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPeevIAAYEA 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-218 |
7.96e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.09 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 12 QYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYAL-YP 88
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 hMTVRE--NMGFALKLQGRDKATInkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVR------HPKVFLFDEP 160
Cdd:PRK13548 91 -FTVEEvvAMGRAPHGLSRAEDDA--LVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 161 LSNPDakLR---VTMRSeIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:PRK13548 168 TSALD--LAhqhHVLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
9.43e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSyalyPH-----MTVR 93
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PDdqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMR 173
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 174 SEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.02e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 110.28 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERD-IAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-228 |
1.09e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.97 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGgEIRIDGRV----------MNDVAPKERDIAMVFQ 82
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRVeffnqniyerRVNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPhMTVRENMGFALKLQG-RDKATINKLVSEAAGILAL-EPLLERLPK---QLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:PRK14258 96 KPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 158 DEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVM-----RAGRIEQIGKPLDLYDRPNNT 228
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHDS 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-222 |
1.14e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.41 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN--DVAPKERDIAMVFQSY-ALYPHMTVREN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 644976330 176 IKELHQRLGTTIVYVTHDQIEAMTmADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-212 |
1.19e-27 |
|
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: 108.63 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGleDI---SGGEIRIDGRVMNDVAPKE--RDIA 78
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLpptYGNDVRLFGERRGGEDVWElrKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVfqSYAL----YPHMTVRE--------NMGFALKLQGRDKAtinkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGR 146
Cdd:COG1119 82 LV--SPALqlrfPRDETVLDvvlsgffdSIGLYREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 147 AIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTH---DQIEAMTmadKIVVMRAGRI 212
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDGRV 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-261 |
1.20e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.45 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN------DVAPKERDIAMVFQsyalYPHM---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 -TVRENMGFALKLQGRDKATINKLVSEAAGILAL-EPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 169 RVTMRSEIKELHQrLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNntFVAAF-IGSPSMNLFEGGVS 247
Cdd:PRK13649 181 RKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVD--FLEEKqLGVPKITKFAQRLA 257
|
250
....*....|....
gi 644976330 248 DGGFRIEggvSLPL 261
Cdd:PRK13649 258 DRGISFS---SLPI 268
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-225 |
1.67e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 113.51 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN--DVAPKERDIA 78
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALYPHmTVRENMGFALKLqGRDKATinklvsEAAGILALEPLLERLPKQ-----------LSGGQRQRVAMGRA 147
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPL-TLDEAW------EAARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKlrvtMRSEIKELHQRLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNR----TQAIVSESLERLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-193 |
2.63e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 106.88 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDI 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 644976330 158 DEPLSNPDAKLRVTMRSEIKELHqRLGTTIVYVTHD 193
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHD 196
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-218 |
2.70e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 12 QYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPH 89
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIV-------RHPKVFLFDEPLS 162
Cdd:COG4559 90 FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 163 NPDAK--LRVtMRSeIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:COG4559 170 ALDLAhqHAV-LRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-212 |
9.11e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 9.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER--DIAMVFQSYAL--YPHMTVR 93
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENM----------GFALKLQGRDKATINKLVSEAAgiLALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:COG1101 101 ENLalayrrgkrrGLRRGLTKKRRELFRELLATLG--LGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 164 PDAK-----LRVTMRSeIKElhQRLgTTIVyVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG1101 179 LDPKtaalvLELTEKI-VEE--NNL-TTLM-VTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-227 |
1.62e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.63 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISgGEIRIDGRVM----NDVAPK------ERDIAMVFQ 82
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLN-PEVTITGSIVynghNIYSPRtdtvdlRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPhMTVRENMGFALKLQG-RDKATINKLVSEA-AGILALEPLLERLPKQ---LSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGiKDKQVLDEAVEKSlKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 158 DEPLSNPD----AKLRVTMrseikeLHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNN 227
Cdd:PRK14239 173 DEPTSALDpisaGKIEETL------LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-211 |
1.82e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 104.09 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 10 QKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmndvapkerdIAMVFQSyALYPH 89
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRENMGFALKLqgrDKATINKlVSEAAgilALEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:cd03250 80 GTIRENILFGKPF---DEERYEK-VIKAC---ALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 159 EPLSNPDAKlrvTMRSEIKEL---HQRLGTTIVYVTHdQIEAMTMADKIVVMRAGR 211
Cdd:cd03250 153 DPLSAVDAH---VGRHIFENCilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
4.46e-26 |
|
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: 103.73 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmTVREN 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGF-----------ALKlqgrdKATINKLVSEAAGILALEplLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN- 163
Cdd:cd03244 98 LDPfgeysdeelwqALE-----RVGLKEFVESLPGGLDTV--VEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASv 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 164 ---PDAKLRVTMRSEIKelhqrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:cd03244 171 dpeTDALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-226 |
6.91e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVA--PKERDI-AMVFQS-YALYPHMTVRENMGFALK 101
Cdd:PRK13644 25 IKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLvGIVFQNpETQFVGRTVEEDLAFGPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 102 LQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQ 181
Cdd:PRK13644 105 NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644976330 182 RlGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:PRK13644 185 K-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-223 |
9.67e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.17 E-value: 9.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvaP-KER-----DIAMVF-QSYALYPHMT 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PfKRRkefarRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENmgfaLKLQGR----DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQR--VAMgrAIVRHPKVFLFDEP---Ls 162
Cdd:COG4586 113 AIDS----FRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPtigL- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 163 npD--AKLRVtmRSEIKELHQRLGTTIVYVTHD--QIEAmtMADKIVVMRAGRIeqigkpldLYD 223
Cdd:COG4586 186 --DvvSKEAI--REFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI--------IYD 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-216 |
9.97e-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: 102.61 E-value: 9.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndVAPKErdIAMVFQsyalyPHMTVRENMG 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---SSLLG--LGGGFN-----PELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 FALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIK 177
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 644976330 178 ELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:cd03220 187 ELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
1.01e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.30 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAID--RVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER-DI 77
Cdd:PRK13536 37 MSTVAIDlaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENM---GFALKLQGRD-KATINKLVSEAagilALEPLLERLPKQLSGGQRQRVAMGRAIVRHPK 153
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLlvfGRYFGMSTREiEAVIPSLLEFA----RLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 154 VFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-203 |
1.25e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.71 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGeIRIDGRVM--------NDVAPKE--RDIAMVFQ 82
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPVEvrRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHmTVRENMGFALKLQGRdKATINKLVSEAAGILALEPLLERLPKQ----LSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 644976330 159 EPLS--NPDAKLRVtmRSEIKELHQRLgtTIVYVTHDQIEAMTMADK 203
Cdd:PRK14243 177 EPCSalDPISTLRI--EELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-211 |
1.86e-25 |
|
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: 102.13 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRI--DGRVMNDVAPKERDIAMVFQSYALY-------- 87
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 PHMTVRENMGFALKLQGRDKATINKlvsEAAGILALEPLLERL----PKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARA---RARELLARLNLPERLwdlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 644976330 164 PDAKLRVTMRSEIKELHQRlGTTIVYVTHDqIEAM-TMADKIVVMRAGR 211
Cdd:COG4778 183 LDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPFS 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-224 |
1.91e-25 |
|
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: 102.56 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGA--ASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAM 79
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYpHMTVRENMGFAlklqgrDKATINKLVSEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAI 148
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 149 VRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-212 |
2.39e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.12 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERD---------IAMVFQSYALYP 88
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ---DVATLDADalaqlrrehFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644976330 169 RVTMRSEIKELHQRlGTTIVYVTHD-QIEAmtMADKIVVMRAGRI 212
Cdd:PRK10535 180 GEEVMAILHQLRDR-GHTVIIVTHDpQVAA--QAERVIEIRDGEI 221
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
15-225 |
2.47e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 106.95 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 15 AASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVaPKER---DIAMVFQSYALYpHMT 91
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMG--------FALKLQGRDkATINKLVSEAAGilALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:TIGR03796 569 VRDNLTlwdptipdADLVRACKD-AAIHDVITSRPG--GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSA 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 164 PDAklrVTMRSEIKELHQRlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:TIGR03796 646 LDP---ETEKIIDDNLRRR-GCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-214 |
3.05e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 5 AIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQ 82
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHmTVRENMGFALKLQGrDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:PRK10247 89 TPTLFGD-TVYDNLIFPWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 163 NPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEaMTMADKIVVM--RAGRIEQ 214
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQE 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-212 |
3.08e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.40 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL----------EDISGGEIRIDGRVMNDVAPK 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 74 ERDIAMVFQSYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPL----LERLPKQ----LSGGQRQRVAMG 145
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALtrvgMVHFAHQrvstLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 146 RAIVRHPKVFLFDEPLSNPDAK-LRVTMRSeIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-226 |
6.48e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQS---YALYP 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 hmTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK13652 95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 169 RVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-212 |
9.67e-25 |
|
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: 100.48 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK-ERDIAMVF-QSYAL 86
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 87 YPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 644976330 167 KLRVTMRSEIKELHQRLGTTIVYVTHD--QIEAmtMADKIVVMRAGRI 212
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYmkDIEA--LARRVLVIDKGRL 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-256 |
9.88e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.38 E-value: 9.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-----RDIAMVFQSYALYP 88
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQGRDKATI------NKLvsEAAGILALEPLLerlPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLlhstvmMKL--EAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 163 NPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNntfvaafigsPSMNLF 242
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD----------PRVRQF 242
|
250
....*....|....*.
gi 644976330 243 EGGVSDG--GFRIEGG 256
Cdd:PRK11831 243 LDGIADGpvPFRYPAG 258
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-192 |
1.03e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.56 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERdIAMVFQSYALYPHMTVRENMG 97
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 FALKLQGRDKATInklvSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKlRVTMRSEIK 177
Cdd:PRK13539 96 FWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELI 170
|
170
....*....|....*
gi 644976330 178 ELHQRLGTTIVYVTH 192
Cdd:PRK13539 171 RAHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-223 |
1.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.98 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 8 RVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSya 85
Cdd:PRK13648 14 SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 lyPH-----MTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:PRK13648 92 --PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTmADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-212 |
1.79e-24 |
|
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: 99.47 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMVFQSYALYPHmTVREN 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALK-------LQGRDKATINKLVSEaagiLALEPLLERLPK--QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:cd03248 108 IAYGLQscsfecvKEAAQKAHAHSFISE----LASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 644976330 167 KLRVTMRSEIKELHQRlgTTIVYVTHdQIEAMTMADKIVVMRAGRI 212
Cdd:cd03248 184 ESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-222 |
2.77e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.58 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 15 AASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN------DVAPKERDIAMVFQsyalYP 88
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HM-----TVRENMGFALKLQGRDKATINKLVSEAAGILAL-EPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:PRK13643 94 ESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 163 NPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-321 |
3.89e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 12 QYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPH 89
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRE--NMGFALKLQ--GRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEplsnPD 165
Cdd:PRK09536 92 FDVRQvvEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDE----PT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 166 AKLRVTMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPnnTFVAAFIGSPSM--N 240
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD--TLRAAFDARTAVgtD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 241 LFEGGVSDGGFRIEGGVSLPLPPQL-----SHSAARTYGirpedlDIAETGIPATVLTVePTGAETH-LSVRVGTQTATI 314
Cdd:PRK09536 246 PATGAPTVTPLPDPDRTEAAADTRVhvvggGQPAARAVS------RLVAAGASVSVGPV-PEGDTAAeTAARVGCEAVTV 318
|
....*..
gi 644976330 315 VLHRRVD 321
Cdd:PRK09536 319 PPFKPIE 325
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-225 |
4.51e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMVFQSYALYPHmTVREN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFALKLQGRDKATInklVSEAAGIlalEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:TIGR00958 575 IAYGLTDTPDEEIMA---AAKAANA---HDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 165 DAKLRVTmrseIKELHQRLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:TIGR00958 649 DAECEQL----LQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-212 |
4.67e-24 |
|
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: 97.12 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 15 AASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERD---IAMV---FQSYALYP 88
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGfalklqgrdkatinklvseaagilalepllerLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:cd03215 92 DLSVAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 644976330 169 RVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-192 |
4.86e-24 |
|
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: 97.43 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK-ERDIAMVFQSYALYPHMTV 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGF-ALKLQGRDKATINKLvsEAAGILALEPLLERlpkQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKlRVT 171
Cdd:TIGR01189 91 LENLHFwAAIHGGAQRTIEDAL--AAVGLTGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVA 164
|
170 180
....*....|....*....|.
gi 644976330 172 MRSEIKELHQRLGTTIVYVTH 192
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-218 |
5.96e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.91 E-value: 5.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHM 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVREnmgfaLKLQGR-------------DKATINKLVsEAAGI--LALEPLlerlpKQLSGGQRQRVAMGRAIVRHPKVF 155
Cdd:PRK10253 97 TVQE-----LVARGRyphqplftrwrkeDEEAVTKAM-QATGIthLADQSV-----DTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 156 LFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-212 |
8.68e-24 |
|
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: 97.73 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED---ISGGEIRIDGRVMNDVAPKERdIAMVFQSYA 85
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGR---DKATINKLV-SEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLPrksSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-234 |
8.88e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 102.51 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYG-AASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAM 79
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSyalyPHM---TVRENmgfaLKLQGRDKATINKLVsEAAGILALEPLLERLPK-----------QLSGGQRQRVAMG 145
Cdd:TIGR01193 553 LPQE----PYIfsgSILEN----LLLGAKENVSQDEIW-AACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 146 RAIVRHPKVFLFDEPLSNPDAklrVTMRSEIKELHQRLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRp 225
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR- 698
|
....*....
gi 644976330 226 nNTFVAAFI 234
Cdd:TIGR01193 699 -NGFYASLI 706
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-212 |
1.07e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE---RDIAMV---FQSY 84
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 85 ALYPHMTVRENMGFA-LKLQGR----DKATINKLVSEAAGILALE-PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:COG1129 340 GLVLDLSIRENITLAsLDRLSRggllDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 159 EPlsnpdaklrvTM------RSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG1129 420 EP----------TRgidvgaKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-206 |
1.08e-23 |
|
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: 97.86 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 25 DIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGrvmNDVAPKERDIAMVFQsyalyphMTVREnmgfALKLQG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL---DTVSYKPQYIKADYE-------GTVRD----LLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 105 RDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLG 184
Cdd:cd03237 87 KDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|..
gi 644976330 185 TTIVYVTHDQIEAMTMADKIVV 206
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIV 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
1.24e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVA--------- 71
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DIThlpmhkrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 72 ------PKErdiAMVFQsyalypHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMG 145
Cdd:COG1137 78 lgigylPQE---ASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 146 RAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQR-LGttiVYVT-HDQIEAMTMADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
...
gi 644976330 224 RPN 226
Cdd:COG1137 226 NPL 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-212 |
1.75e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 97.22 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDiSGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHMTVRENMGF 98
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKLQGRDkATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVR-------HPKVFLFDEPLSNPDAKLRVT 171
Cdd:COG4138 93 HQPAGASS-EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 172 MRSEIKELHQrLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG4138 172 LDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
2.52e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerDIAMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL---------RIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKLV-----------------------------SEAAGILA----LEPLLERLPK 132
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEELEaklaepdedlerlaelqeefealggweaeARAEEILSglgfPEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 133 QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK----LRvtmrseiKELHQRLGTTIVyVTHD 193
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLE-------EFLKNYPGTVLV-VSHD 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-234 |
2.53e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 98.66 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED----ISGGEIRIDGRVMNDVAPKER------DIAMVFQS--YALYPH 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRENMGFALKL-QGRDKATINKLVSE---AAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSnpd 165
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRAIDllnQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT--- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 166 aKLRVTMRSEI----KELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFI 234
Cdd:PRK11022 183 -ALDVTIQAQIiellLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-222 |
2.69e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDG---RVMNDVAPKERDIAMVFQSyalyPH----- 89
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLR 169
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 170 VTMRSEIKELHQRLGTTIVYVTHDQIEAMTmADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-223 |
3.17e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 96.07 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 29 GEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAPKERDIAMVFQSYAL---YP---HMTVRENMGFALKL 102
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPisvAHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 103 QGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQR 182
Cdd:TIGR03771 83 LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 183 lGTTIVYVTHDQIEAMTMADKIVVMRaGRIEQIGKPLDLYD 223
Cdd:TIGR03771 163 -GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-193 |
4.48e-23 |
|
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: 99.74 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-RDIAMVFQSYALYPHMTV 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVSVCAQDAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMgfalkLQGRDKATINKL--VSEAAGilaLEPLLERLP-----------KQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:TIGR02868 426 RENL-----RLARPDATDEELwaALERVG---LADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHD 193
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-229 |
6.43e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAasvIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVA-----PKERDIAMV 80
Cdd:PRK10261 330 LNRVTREVHA---VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQS-YA-LYPHMTVRENMGFALK----LQGRDKATINKLVSEAAGILALEPLleRLPKQLSGGQRQRVAMGRAIVRHPKV 154
Cdd:PRK10261 407 FQDpYAsLDPRQTVGDSIMEPLRvhglLPGKAAAARVAWLLERVGLLPEHAW--RYPHEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 155 FLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTF 229
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-221 |
7.74e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMVFQSYALYPHMTVRE 94
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NMGF-------ALklqGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:PRK10575 105 LVAIgrypwhgAL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 168 LRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
8.17e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 8.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE---RDI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVREN--MG--FALKLQGRDKatinklvseAAGILALEP-LLERLPKQ---LSGGQRQRVAMGRAIV 149
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENlaMGgfFAERDQFQER---------IKWVYELFPrLHERRIQRagtMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 150 RHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI--EQIGKPL 219
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDAL 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-225 |
8.96e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.02 E-value: 8.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL---EDISGGEIRIDGRVMN-----DVAPKerdIAMVFQSY-ALYP 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTaktvwDIREK---VGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 HMTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 169 RVTMRSEIKELHQRLGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-225 |
9.42e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.63 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN--DVAPKERDIAMVFQ--SYALYPHMTVRENMG 97
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 FALKL------QGRDKATINKLvsEAAGILALEplLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLsnpdAKLRVT 171
Cdd:PRK15112 112 FPLRLntdlepEQREKQIIETL--RQVGLLPDH--ASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL----ASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 172 MRSEI----KELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:PRK15112 184 MRSQLinlmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-217 |
1.02e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 99.43 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 15 AASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMVFQSYALYPHmTV 92
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGfalklQGRDKATINKLVSeAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:TIGR01846 548 RDNIA-----LCNPGAPFEHVIH-AAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 162 SNPDAKLRVTMRSEIKELHQrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:TIGR01846 622 SALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGR 674
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-216 |
1.02e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGL---EdisgGEIRIDGRVMNDVAPKE--RDIAMVFQSYALyPHMTVRENM 96
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpyQ----GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 97 gfalkLQGRDKAT---INKLVsEAAGILALeplLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:PRK11174 444 -----LLGNPDASdeqLQQAL-ENAWVSEF---LPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 163 NPDAklrvtmRSE---IKELHQ-RLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK11174 515 SLDA------HSEqlvMQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-224 |
1.54e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 98.64 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 16 ASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND--VAPKERDIAMVFQSYALYPHmTVR 93
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVALVSQDVVLFND-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFAlKLQGRDKATINKLVSEAAgilaLEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:TIGR02203 424 NNIAYG-RTEQADRAEIERALAAAY----AQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 163 NPDAKLRVTMRSEIKELHQrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-235 |
1.83e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.06 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVM---NDVAPKERDI 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENMgFALKLQGR----DKATINKLVSEAAGILALE-----PLlerlpKQLSGGQRQRVAMGRAI 148
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENL-YLGQLPHKggivNRRLLNYEAREQLEHLGVDidpdtPL-----KYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 149 VRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRieQIGKPLDLYDRPNNT 228
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQVDRDQ 232
|
....*..
gi 644976330 229 FVAAFIG 235
Cdd:PRK11288 233 LVQAMVG 239
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-256 |
1.97e-22 |
|
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: 98.86 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerdiAMVFQSyALYPHMTVRENMGF 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKLQ-GRDKATInklvsEAAgilALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:TIGR00957 722 GKALNeKYYQQVL-----EAC---ALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 167 KL-RVTMRSEIKELHQRLGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGKPLDLYDRpNNTFvAAFIGSPSMNLFEGG 245
Cdd:TIGR00957 794 HVgKHIFEHVIGPEGVLKNKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAF-AEFLRTYAPDEQQGH 870
|
250
....*....|.
gi 644976330 246 VSDGGFRIEGG 256
Cdd:TIGR00957 871 LEDSWTALVSG 881
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
5.18e-22 |
|
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: 91.61 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS--VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERD-IAMV 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYpHMTVRENMGfalklqgrdkatinklvseaagilalepllerlpKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 161 LSNPDAKlrvTMRSEIKELHQRL-GTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:cd03247 126 TVGLDPI---TERQLLSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-218 |
5.67e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.04 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLA-----GLEdiSGGEIRIDGRVMNdvAPKERDI-AMVFQSYALYPHM 90
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVK--GSGSVLLNGMPID--AKEMRAIsAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFA--LKLQGRDKATINKL-VSEAAGILALEPL------LERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:TIGR00955 115 TVREHLMFQahLRMPRRVTKKEKRErVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRlGTTIVYVTHD-QIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-222 |
6.52e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAAS-----VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL------EDISGG-EIRIDGRVMNDVA 71
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIVGDyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 72 PKERDIAMVFQ--SYALYPHmTVRENMGFALKLQGRDKATINKLVSEAAGILAL-EPLLERLPKQLSGGQRQRVAMGRAI 148
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 149 VRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
19-216 |
1.38e-21 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 95.73 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMVFQSYALYpHMTVRENM 96
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTREslRKSIATVFQDAGLF-NRSIRENI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 97 GFalklqGRDKATINKLVSEAAGILALEPLLERLP----------KQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:TIGR01192 430 RL-----GREGATDEEVYEAAKAAAAHDFILKRSNgydtlvgergNRLSGGERQRLAIARAILKNAPILVLDEATSALDV 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 644976330 167 KLRVTMRSEIKELHQRLGTTIvyVTHdQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:TIGR01192 505 ETEARVKNAIDALRKNRTTFI--IAH-RLSTVRNADLVLFLDQGRLIEKG 551
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-223 |
2.10e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAP---KERDIAMVFQSYA 85
Cdd:PRK15439 17 ISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKLVSEaagiLALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:PRK15439 97 LFPNLSVKENILFGLPKRQASMQKMKQLLAA----LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 166 AKLRVTMRSEIKELhQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYD 223
Cdd:PRK15439 173 PAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-255 |
2.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN------DVAPKERDIAMVFQsyalYPHM----- 90
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAqlfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQG-RDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLR 169
Cdd:PRK13641 102 TVLKDVEFGPKNFGfSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 170 VTMRSEIKElHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPnNTFVAAFIGSPSMNLFEGGVSDG 249
Cdd:PRK13641 182 KEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATSRFASKLEKG 259
|
....*.
gi 644976330 250 GFRIEG 255
Cdd:PRK13641 260 GFKFSE 265
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-222 |
3.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.22 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 10 QKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL----------EDISGGEIRIDGRVMNDVAPKE----- 74
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 ---RDIAMVFQ--SYALYPHmTVRENMGF---ALKLQGRDKATINKLVSEAAGILalEPLLERLPKQLSGGQRQRVAMGR 146
Cdd:PRK13631 113 elrRRVSMVFQfpEYQLFKD-TIEKDIMFgpvALGVKKSEAKKLAKFYLNKMGLD--DSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 147 AIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
4.08e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.29 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN----DVAPKERDIAMVFQS-----YAly 87
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddqlFA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 PhmTVRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:PRK13639 94 P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 168 LRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-222 |
4.16e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDG-RVMNDVAPKE-----RDIAMVFQsyalYPHM-- 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYirpvrKRIGMVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 ---TVRENMGFALKLQGRDKatinKLVSEAAGILALE-----PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:PRK13646 99 fedTVEREIIFGPKNFKMNL----DEVKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 163 NPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-212 |
4.58e-21 |
|
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: 89.63 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGledISGGEIRIDGRVM-NDVAPKE------ 74
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHyNGIPYKEfaekyp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 RDIAMVFQSYALYPHMTVRENMGFALKLQGrdkatiNKLVSeaaGIlalepllerlpkqlSGGQRQRVAMGRAIVRHPKV 154
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCKG------NEFVR---GI--------------SGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 155 FLFDEPLSNPDAKLRVTMRSEIKELHQRLG-TTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-192 |
6.20e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIdgrvmndvaPKERDIAMVFQSyalyPHM---TVRE 94
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQR----PYLplgTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NMGFALKLQGRDKATINKLVsEAAGilaLEPLLERL------PKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:COG4178 445 ALLYPATAEAFSDAELREAL-EAVG---LGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180
....*....|....*....|....*
gi 644976330 169 RVTMrseIKELHQRL-GTTIVYVTH 192
Cdd:COG4178 521 EAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-220 |
9.83e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEI--------------RIDGRVMNDVAPK---------- 73
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLVIQKtrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 74 --ERDIAMVFQ--SYALYpHMTVRENMGFALKLQGRDKATINKLVSEAAGILAL-EPLLERLPKQLSGGQRQRVAMGRAI 148
Cdd:PRK13651 102 eiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 149 VRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLD 220
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-216 |
1.09e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.10 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAMV 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYpHMTVRENmgfaLKLqGRDKATiNKLVSEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIV 149
Cdd:PRK13657 415 FQDAGLF-NRSIEDN----IRV-GRPDAT-DEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 150 RHPKVFLFDEPLSNPDAKLRVTMRSEIKEL-HQRlgTTIVyVTHdQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELmKGR--TTFI-IAH-RLSTVRNADRILVFDNGRVVESG 551
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-218 |
2.06e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDiSGGEIRIDGRVMNDVAPKERD-------------IAM-VFQSYALY 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELArhraylsqqqtppFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 PHmtvrenmgfalklQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVR-------HPKVFLFDEP 160
Cdd:PRK03695 94 QP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQrLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-214 |
4.95e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQY--GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE-RD-I 77
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHmTVRENMGFALklqgrDKATINKLvSEAAGILALEPLLERLP----------KQLSGGQRQRVAMGRA 147
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAA-----PNASDEAL-IEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKlrvTMRsEIKEL---HQRlGTTIVYVTHdQIEAMTMADKIVVMRAGRI-EQ 214
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAE---TER-QILELlaeHAQ-NKTVLMITH-RLTGLEQFDRICVMDNGQIiEQ 554
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-224 |
6.25e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 12 QYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMN----DVAPKERDIAMVFQSYALY 87
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 PHMT-VRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:PRK13638 90 IFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 167 KLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDR 224
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-225 |
6.73e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.01 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL---EDISGGEIRIDGRVMNDVAPKE------RDIAMVFQS- 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 -YALYPHMTVRENMGFALKL-QGRDKATInklVSEAAGILALEPLLE---RL---PKQLSGGQRQRVAMGRAIVRHPKVF 155
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLhKGMSKAEA---FEESVRMLDAVKMPEarkRMkmyPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 156 LFDEPLSnpdaKLRVTMRSEI----KELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:PRK09473 184 IADEPTT----ALDVTVQAQImtllNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-214 |
1.12e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKS----TLLRMLAGLEDI-SGGEIRIDGR-VMNDVAPKER-----DIAMVFQS--Y 84
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGEsLLHASEQTLRgvrgnKIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 85 ALYPHMTVRENMGFALKLQG--RDKATINKLVS--EAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLHRgmRREAARGEILNclDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 161 LSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGR-IEQ 214
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQ 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-238 |
1.16e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED-ISG----GEIRIDGRVM---NDVAPKERDIAMVFQSY 84
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSGyrysGDVLLGGRSIfnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 85 ALYPhMTVRENM--GF-ALKLQGRD--KATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:PRK14271 111 NPFP-MSIMDNVlaGVrAHKLVPRKefRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLgtTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAFIGSPS 238
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLS 266
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-236 |
1.29e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.91 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 10 QKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVM----------NDVAPKE----- 74
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielSEQSAAQmrhvr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 75 -RDIAMVFQS--YALYPHMTVRENMGFALKLQ---GRDKATIN-KLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRA 147
Cdd:PRK10261 103 gADMAMIFQEpmTSLNPVFTVGEQIAESIRLHqgaSREEAMVEaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNN 227
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
....*....
gi 644976330 228 TFVAAFIGS 236
Cdd:PRK10261 263 PYTRALLAA 271
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-218 |
1.58e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.27 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED--ISGGEIRIDGRVMNDVAPKER---DIAMVFQSYALYPHMTV 92
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGFALKLQGRDKATI---NKLVSEAAGILALEP-LLER-LPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS--NPD 165
Cdd:COG0396 95 SNFLRTALNARRGEELSArefLKLLKEKMKELGLDEdFLDRyVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSglDID 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 166 AkLRVtMRSEIKELHQRlGTTIVYVTH-----DQIEamtmADKIVVMRAGRIEQIGKP 218
Cdd:COG0396 175 A-LRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-201 |
3.10e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.47 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 20 HGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNdvapKERDiamVFQSYALY--------PHMT 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLQG--RDKATINKLvsEAAGILALEPLLERlpkQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKlr 169
Cdd:PRK13538 91 ALENLRFYQRLHGpgDDEALWEAL--AQVGLAGFEDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-- 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 644976330 170 vtmrsEIKELHQRL------GTTIVYVTHDQIEAMTMA 201
Cdd:PRK13538 164 -----GVARLEALLaqhaeqGGMVILTTHQDLPVASDK 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-214 |
3.50e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKST----LLRMLAglediSGGEIRIDGRVMNDVAPKE-----RDIAMVFQ--SYA 85
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQgrdKATINKLVSEAAGILALEPL------LERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVH---QPTLSAAQREQQVIAVMEEVgldpetRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 160 PLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGR-IEQ 214
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQ 507
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-211 |
7.16e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDiSG---GEIRIDGRVMndVAPKERD-----IAMVFQ 82
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP-HGtyeGEIIFEGEEL--QASNIRDteragIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALYPHMTVRENMGFALKLqgrdkaTINKLVSEAAGILALEPLLERLP---------KQLSGGQRQRVAMGRAIVRHPK 153
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEI------TPGGIMDYDAMYLRAQKLLAQLKldinpatpvGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 154 VFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
1.10e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmnDVA--PKERDiamvf 81
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV--KIGyfDQHQE----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 82 qsyALYPHMTVRENMGfalklQGRDKATInklvSEAAGIL---------ALEPLlerlpKQLSGGQRQRVAMGRAIVRHP 152
Cdd:COG0488 389 ---ELDPDKTVLDELR-----DGAPGGTE----QEVRGYLgrflfsgddAFKPV-----GVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 644976330 153 KVFLFDEPLSNPDaklrVTMRSEIKELHQRLGTTIVYVTHDQ--IEamTMADKIVVMRAGRIE 213
Cdd:COG0488 452 NVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-192 |
1.36e-18 |
|
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: 82.54 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK-ERDIAMVFQSYALYPHMTV 92
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGFALKLQGRDKatinklVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD----AKL 168
Cdd:cd03231 91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARF 164
|
170 180
....*....|....*....|....
gi 644976330 169 RVTMRSeikelHQRLGTTIVYVTH 192
Cdd:cd03231 165 AEAMAG-----HCARGGMVVLTTH 183
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
1.60e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMnDVAPK-----ERDIAMVFQS--YALYPhMT 91
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmklRESVGMVFQDpdNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVT 171
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 172 MRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-218 |
2.71e-18 |
|
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: 82.07 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmTVRE 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NmgfalkLQGRDKATINKL-----VSEAAgilalepllerlpKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN----PD 165
Cdd:cd03369 101 N------LDPFDEYSDEEIygalrVSEGG-------------LNLSQGQRQLLCLARALLKRPRVLVLDEATASidyaTD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 166 AKLRVTMRSEIKelhqrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:cd03369 162 ALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-215 |
4.80e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE---RDIAMVFQSY---ALYPHMTVREN 95
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MGFA--LKLQGR-------DKATINKLVSEAAGILALE-PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:PRK09700 362 MAISrsLKDGGYkgamglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 166 aklrVTMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRIEQI 215
Cdd:PRK09700 442 ----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-212 |
5.05e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.28 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR--VMNDVA----PKER-----DIAM 79
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLYalseAERRrllrtEWGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYA--LYPHMTVRENMGFALKLQG-RDKATINklvSEAAGILA-LEPLLER---LPKQLSGGQRQRVAMGRAIVRHP 152
Cdd:PRK11701 94 VHQHPRdgLRMQVSAGGNIGERLMAVGaRHYGDIR---ATAGDWLErVEIDAARiddLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 153 KVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-192 |
5.18e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.43 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvMNDVAPKERDIAMVFQSYALYPHMTVRENMGFALKLQGR 105
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 106 DKatiNKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKlRVTMRSEIKELHQRLGT 185
Cdd:PRK13543 113 RA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAHLRGGG 188
|
....*..
gi 644976330 186 TIVYVTH 192
Cdd:PRK13543 189 AALVTTH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-221 |
5.31e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.07 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMND--VAPKERDIAMVFQSYALYpHMTVRENMGFA 99
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANNIAYA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 100 LKlqgrDKATINKLVSEAAGILALEpLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK11176 441 RT----EQYSREQIEEAARMAYAMD-FINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 169 RVTMRSEIKELhQRLGTTIVyVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:PRK11176 516 ERAIQAALDEL-QKNRTSLV-IAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
6.00e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 1 MASVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDV---APKERDI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENMGFALKL-------QGRDKAtiNKLVSEaagiLALEPLLERLPKQLSGGQRQRVAMGRAIVR 150
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrddlsaeQREDRA--NELMEE----FHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 151 HPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-224 |
8.16e-18 |
|
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: 80.65 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED--ISGGEIRIDGRVMNDVAPKER---DIAMVFQSYALYPHMTV 92
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RE-----NMGFalklqgrdkatinklvseaagilalepllerlpkqlSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:cd03217 95 ADflryvNEGF------------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 168 -LRVTMRsEIKELHQRlGTTIVYVTH-DQIEAMTMADKIVVMRAGRIEQIGkPLDLYDR 224
Cdd:cd03217 139 aLRLVAE-VINKLREE-GKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-217 |
8.30e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.55 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISG--GEIRIDGRVMndVAPKERDIAMVFQSYALYPHMTVRE 94
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP--TKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NMGFAL------KLQGRDKATINKLVSEAAGILALEPLL--ERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:PLN03211 160 TLVFCSllrlpkSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 167 KLRVTMRSEIKELHQRlGTTIVYVTHD-QIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:PLN03211 240 TAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-195 |
9.98e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 80.38 E-value: 9.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQSYALYPHMT 91
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGFALKLqgrdkATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVT 171
Cdd:PRK13540 91 LRENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....
gi 644976330 172 MRSEIKElHQRLGTTIVYVTHDQI 195
Cdd:PRK13540 166 IITKIQE-HRAKGGAVLLTSHQDL 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-211 |
1.01e-17 |
|
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: 84.11 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL--EDISGGEIRIDGR--VMNDVAPKERD-IAMVFQS 83
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSplKASNIRDTERAgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHMTVREN--MGFALKLQGrdkatinKLVSEAAGILALEPLLERLP----------KQLSGGQRQRVAMGRAIVRH 151
Cdd:TIGR02633 87 LTLVPELSVAENifLGNEITLPG-------GRMAYNAMYLRAKNLLRELQldadnvtrpvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.03e-17 |
|
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: 84.08 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED---ISG------------GEIRIDGRV-- 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyepTSGriiyhvalcekcGYVERPSKVge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 67 -----MNDVAPKERD---------------IAMVFQ-SYALYPHMTVRENMGFALKLQGRDKATINKLVSEAAGILALEP 125
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 126 LLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIV 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*....
gi 644976330 206 VMRAGRIEQIGKPLDLYDR 224
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAV 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
1.46e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER-DIAMVFQSY-----ALYPHMTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGF-ALKLQGRDKATINKlvseAAGILALE----------PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:PRK10762 348 KENMSLtALRYFSRAGGSLKH----ADEQQAVSdfirlfniktPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 162 SNPDaklrVTMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK10762 424 RGVD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-236 |
1.60e-17 |
|
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: 81.03 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVA------PKERDIA-----M 79
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlseAERRRLMrtewgF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHMTVREN-------MGFALKLQGRDKATINKLVSEaagiLALEP-LLERLPKQLSGGQRQRVAMGRAIVRH 151
Cdd:TIGR02323 91 VHQNPRDGLRMRVSAGanigerlMAIGARHYGNIRATAQDWLEE----VEIDPtRIDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVA 231
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQ 246
|
....*
gi 644976330 232 AFIGS 236
Cdd:TIGR02323 247 LLVSS 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-225 |
1.72e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.90 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKS----TLLRML-AGLEDiSGGEIRIDGRVMNDVAPKERDIAMVFQS--YALYPHMT 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VREN---MGFALKLQGRDKATINKLvsEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:PRK10418 98 MHTHareTCLALGKPADDATLTAAL--EAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 169 RVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRP 225
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-235 |
1.82e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVM--NDVAPKERDIAMVfQSYALYPHMTVRENmgfa 99
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRVGYMS-QAFSLYGELTVRQN---- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 100 LKLQGR----DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSE 175
Cdd:NF033858 360 LELHARlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644976330 176 IKELHQRLGTTIVYVTHDQIEAMTmADKIVVMRAGRIEQIGKPLDLYD-RPNNTFVAAFIG 235
Cdd:NF033858 440 LIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAaRGAATLEEAFIA 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
1.90e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK---ERDIAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENMgFALKLQGR--------DKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHP 152
Cdd:PRK09700 86 YQELSVIDELTVLENL-YIGRHLTKkvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 153 KVFLFDEP---LSNPDA-KLRVTMRSEIKElhqrlGTTIVYVTHDQIEAMTMADKIVVMRAG 210
Cdd:PRK09700 165 KVIIMDEPtssLTNKEVdYLFLIMNQLRKE-----GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-217 |
2.15e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGA-ASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK--ERDIAM 79
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALYPHmTVRENMGFalklqGRDkatinklVSEAAGILALE-----PLLERLPK-----------QLSGGQRQRVA 143
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTL-----GRD-------ISEEQVWQALEtvqlaELARSLPDglytplgeqgnNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 144 MGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlgTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-235 |
8.02e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVM-----NDVAPKerDIAMVFQSYALYPHMTVR 93
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpgHQIARM--GVVRTFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFA-------------LKLQGRDKATINKLvSEAAGIL---ALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:PRK11300 99 ENLLVAqhqqlktglfsglLKTPAFRRAESEAL-DRAATWLervGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 158 DEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLydRPNNTFVAAFIG 235
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI--RNNPDVIKAYLG 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-221 |
1.34e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.21 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 28 DGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQSYALYPHMTVRENMGFALKLQGRd 106
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR- 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 107 katinklvSEAAGILALEPLLERL---------PKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIk 177
Cdd:TIGR01257 1034 --------SWEEAQLEMEAMLEDTglhhkrneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 644976330 178 eLHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:TIGR01257 1105 -LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-216 |
1.63e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.53 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmTVRE 94
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NMgfALklqGRDKATINKlVSEAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:PRK10789 408 NI--AL---GRPDATQQE-IEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 164 PDAKlrvTMRSEIKELHQ-RLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK10789 482 VDGR---TEHQILHNLRQwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-205 |
3.68e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMndvapkerdIAMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR---------IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 YALYPHM--TVRENMgfALKLQGRDKATINKLVSEAAGILALEPLlerlpKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:PRK09544 76 LYLDTTLplTVNRFL--RLRPGTKKEDILPALKRVQAGHLIDAPM-----QKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 644976330 162 SNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIV 205
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-207 |
4.34e-16 |
|
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: 77.02 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 13 YGAAS-VIHGVSAdIEDGEFVTLVGPSGCGKSTLLRMLAG------------------LEDISGGEIRIdgrVMNDVAPK 73
Cdd:cd03236 10 YGPNSfKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSELQN---YFTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 74 ERDIAMVFQSYALYPHmTVRENMGFALKlQGRDKATINKLVSEaagiLALEPLLERLPKQLSGGQRQRVAMGRAIVRHPK 153
Cdd:cd03236 86 DVKVIVKPQYVDLIPK-AVKGKVGELLK-KKDERGKLDELVDQ----LELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 154 VFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVM 207
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-215 |
5.36e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHMtvrenmgfaLKLQ 103
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQL---------LGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 104 GRDKATinKLVSEAAGILALEPLLE----RLPK-QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKE 178
Cdd:PRK10522 417 GKPANP--ALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLP 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 644976330 179 LHQRLGTTIVYVTHDQiEAMTMADKIVVMRAGRIEQI 215
Cdd:PRK10522 495 LLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSEL 530
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
6.09e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIA-MVF-----QSYALYPHMTVREN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 M-----------GFALKlQGRDKATINKLvseaagILALE---PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPL 161
Cdd:PRK11288 352 InisarrhhlraGCLIN-NRWEAENADRF------IRSLNiktPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 162 SNPDaklrVTMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK11288 425 RGID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-206 |
6.24e-16 |
|
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: 78.67 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 25 DIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerdiamvfqSY------ALYPhMTVRENMGF 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI----------------SYkpqyisPDYD-GTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKlqgrDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKE 178
Cdd:COG1245 425 ANT----DDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180
....*....|....*....|....*....
gi 644976330 179 LHQRLGTTIVYVTHDqIEAMTM-ADKIVV 206
Cdd:COG1245 501 FAENRGKTAMVVDHD-IYLIDYiSDRLMV 528
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-216 |
9.13e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 78.63 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLR-MLAGLEDISGGEIRIDGRVmndvapkerdiAMVFQSYALYpHMTVRENMGFAL 100
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 101 KLqgrDKATINKlvseAAGILALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL- 168
Cdd:PLN03130 704 PF---DPERYER----AIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVg 776
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 644976330 169 RVTMRSEIK-ELHqrlGTTIVYVThDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PLN03130 777 RQVFDKCIKdELR---GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-206 |
1.40e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 58 GEIRIDGRVMNDVAPKE-RDIAMVFQSYALYPHMTVRENMGFalklqGRDKATINKlVSEAAGILALEPLLERLP----- 131
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKF-----GKEDATRED-VKRACKFAAIDEFIESLPnkydt 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 132 ------KQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHdQIEAMTMADKIV 205
Cdd:PTZ00265 1351 nvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIV 1429
|
.
gi 644976330 206 V 206
Cdd:PTZ00265 1430 V 1430
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-215 |
1.61e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.48 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED----ISGGEIRIDGRVMNDVAPKER------DIAMVFQ- 82
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 -SYALYPHMTVRENMGFAL-----------KLQGRDKATINKLvsEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVR 150
Cdd:COG4170 98 pSSCLDPSAKIGDQLIEAIpswtfkgkwwqRFKWRKKRAIELL--HRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 151 HPKVFLFDEPLsnpdAKLRVTMRSEIKELHQRL----GTTIVYVTHDqIEAMT-MADKIVVM------RAGRIEQI 215
Cdd:COG4170 176 QPRLLIADEPT----NAMESTTQAQIFRLLARLnqlqGTSILLISHD-LESISqWADTITVLycgqtvESGPTEQI 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-220 |
1.65e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.90 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRidgrvmndvapKERDIAMVFQSyALYPHMTVRENMG 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 F-----ALKLQgrDKATINKLVSEAAGILA-LEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL--R 169
Cdd:PTZ00243 743 FfdeedAARLA--DAVRVSQLEADLAQLGGgLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeR 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 170 VTMRSEIKELHqrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLD 220
Cdd:PTZ00243 821 VVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-210 |
2.00e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.29 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLL-RMLAGLEDISG----GEIRIDGRVMNDVAPKER-DIAMVFQSYALYpHM 90
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRySVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMGFALKLQGRDKatinKLVSEAAgilALEPLLERLPK-----------QLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:cd03290 94 TVEENITFGSPFNKQRY----KAVTDAC---SLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 160 PLSNPDAKLR-VTMRSEIKELHQRLGTTIVYVTHdQIEAMTMADKIVVMRAG 210
Cdd:cd03290 167 PFSALDIHLSdHLMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-229 |
2.27e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQY--GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIA 78
Cdd:PTZ00243 1308 SLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 79 MVFQSYALYPHmTVRENMG-F----------ALKLQG-RDkatinKLVSEAAGILALepLLERlPKQLSGGQRQRVAMGR 146
Cdd:PTZ00243 1388 MIPQDPVLFDG-TVRQNVDpFleassaevwaALELVGlRE-----RVASESEGIDSR--VLEG-GSNYSVGQRQLMCMAR 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 147 AIVRHPKVF-LFDEPLSNPDAKL----RVTMRSEIKelhqrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:PTZ00243 1459 ALLKKGSGFiLMDEATANIDPALdrqiQATVMSAFS------AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
....*...
gi 644976330 222 YDRPNNTF 229
Cdd:PTZ00243 1532 VMNRQSIF 1539
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
26-212 |
3.08e-15 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 76.53 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDI-AMVFQSYALYPHMtVRENMGfalKLQ 103
Cdd:TIGR01194 365 IAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAaVSADSRDDYRDLfSAIFADFHLFDDL-IGPDEG---EHA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 104 GRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRL 183
Cdd:TIGR01194 441 SLDNAQQYLQRLEIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQ 520
|
170 180
....*....|....*....|....*....
gi 644976330 184 GTTIVYVTHDQiEAMTMADKIVVMRAGRI 212
Cdd:TIGR01194 521 GKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-212 |
3.61e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKERDIAMVF------QSYALYPHMT 91
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMgfALKLQGR---------DKATINKL---VSEAAGILAlePLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:COG3845 353 VAENL--ILGRYRRppfsrggflDRKAIRAFaeeLIEEFDVRT--PGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 160 P---LsnpDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:COG3845 429 PtrgL---DVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-192 |
3.76e-15 |
|
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: 72.19 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 23 SADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIdgrvmndvaPKERDIAMVFQSyalyPHMTvrenmgfalkl 102
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 103 qgrdkatinklvseaAGILAlEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKElhqr 182
Cdd:cd03223 77 ---------------LGTLR-EQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE---- 136
|
170
....*....|
gi 644976330 183 LGTTIVYVTH 192
Cdd:cd03223 137 LGITVISVGH 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-234 |
3.25e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRI------DGRVMNDVAPKerdI 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRRAVCPR---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYA--LYPHMTVRENMGFALKLQGRDKAT----INKLVsEAAGilaLEPLLERLPKQLSGGQRQRVAMGRAIVRH 151
Cdd:NF033858 79 AYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAErrrrIDELL-RATG---LAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 152 PKVFLFDE------PLSnpdaklrvtmRSEIKEL-----HQRLGTTIVYVTHDQIEAMTMaDKIVVMRAGRIEQIGKPLD 220
Cdd:NF033858 155 PDLLILDEpttgvdPLS----------RRQFWELidrirAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAE 223
|
250
....*....|....*
gi 644976330 221 LYDRPN-NTFVAAFI 234
Cdd:NF033858 224 LLARTGaDTLEAAFI 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-206 |
3.61e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 11 KQYGAASVIhgVSA-DIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerdiamvfqSY----- 84
Cdd:PRK13409 348 KKLGDFSLE--VEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI----------------SYkpqyi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 85 -ALYPhMTVRENMGFAlklqgRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:PRK13409 410 kPDYD-GTVEDLLRSI-----TDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVV 206
Cdd:PRK13409 484 LDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-208 |
5.67e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 2 ASVAIDRVQKQY-GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDvAPKERDIAMV 80
Cdd:PRK15056 5 AGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYAL---YP-------HMTVRENMGFALKLQGRDKAtinkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVR 150
Cdd:PRK15056 84 PQSEEVdwsFPvlvedvvMMGRYGHMGWLRRAKKRDRQ----IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 151 HPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMR 208
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-194 |
7.26e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 8 RVQKQYgaasVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDgrVMNDVAPKERDIAmvfqsyaly 87
Cdd:COG2401 39 RVVERY----VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPDNQFGREASLI--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 phmtvrENMGfalklQGRDKATINKLVSeAAGiLALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:COG2401 104 ------DAIG-----RKGDFKDAVELLN-AVG-LSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*..
gi 644976330 168 LRVTMRSEIKELHQRLGTTIVYVTHDQ 194
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-222 |
9.38e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLR-MLAGLEDISGGEIRIDGRVMndVAPKerdIAMVFQSyalyphmTVRENMGFAL 100
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVA--YVPQ---VSWIFNA-------TVRENILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 101 KLQgrdkatiNKLVSEAAGILALEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL- 168
Cdd:PLN03232 704 DFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVa 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 169 RVTMRSEIKelHQRLGTTIVYVThDQIEAMTMADKIVVMRAGRIEQIGKPLDLY 222
Cdd:PLN03232 777 HQVFDSCMK--DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-211 |
1.00e-13 |
|
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: 67.47 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerdiamvfqSYA 85
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------KIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPhmtvrenmgfalklqgrdkatinklvseaagilalepllerlpkQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:cd03221 67 YFE--------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 644976330 166 AKLRVTMRSEIKELHQrlgtTIVYVTHDQ--IEAmtMADKIVVMRAGR 211
Cdd:cd03221 103 LESIEALEEALKEYPG----TVILVSHDRyfLDQ--VATKIIELEDGK 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-207 |
1.13e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 71.74 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 27 EDGEFVTLVGPSGCGKSTLLRMLAG------------------------------LEDISGGEIRIdgrVMN----DVAP 72
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelqdyFKKLANGEIKV---AHKpqyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 73 KerdiamVFQSyalyphmTVREnmgfALKlqgrdKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHP 152
Cdd:COG1245 174 K------VFKG-------TVRE----LLE-----KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 153 KVFLFDEPLSNPDAKLRVTMRSEIKELhQRLGTTIVYVTHDQIEAMTMADKIVVM 207
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-212 |
1.27e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKER-DIAMVF-----QSYALYPHMTVREN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 --------MGFALKlQGRDKATINKLvSEAAGILALEPllERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDak 167
Cdd:PRK15439 362 vcalthnrRGFWIK-PARENAVLERY-RRALNIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 644976330 168 lrVTMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK15439 436 --VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-250 |
1.36e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQY--GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGrvmNDVAP-----KER 75
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAKfgltdLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 76 DIAMVFQSYALYPHmTVRENM------GFALKLQGRDKATINKLVSEAAgiLALEPLLERLPKQLSGGQRQRVAMGRAIV 149
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIdpfsehNDADLWEALERAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 150 RHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTF 229
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFK--SCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
250 260 270
....*....|....*....|....*....|.
gi 644976330 230 V----------AAFIGSPSMNLFEGGVSDGG 250
Cdd:PLN03232 1465 FrmvhstgpanAQYLSNLVFERRENGMSLGG 1495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-207 |
2.76e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAG------------------------------LEDISGGEIRIDgrvmndVAPKER 75
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyFKKLYNGEIKVV------HKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 76 D-IAMVFQSyalyphmTVREnmgfALKlqgrdKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKV 154
Cdd:PRK13409 170 DlIPKVFKG-------KVRE----LLK-----KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 155 FLFDEPLSNPDAKLRVTMRSEIKELHQrlGTTIVYVTHDQIEAMTMADKIVVM 207
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-166 |
3.75e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 67.27 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDIS--GGEIRIDGRVMNDVAPkeRDIAMVFQSYALYPHMTVRENM 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 97 GFALKLQGrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDA 166
Cdd:cd03232 101 RFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-210 |
5.32e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 29 GEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPK---ERDIAMVFQSYALYPHMTVRENMgfalkLQGR 105
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqEAGIGIIHQELNLIPQLTIAENI-----FLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 106 DKATI------NKLVSEAAGILA---LEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP---LSNPDAKlrvTMR 173
Cdd:PRK10762 105 EFVNRfgridwKKMYAEADKLLArlnLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPtdaLTDTETE---SLF 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 644976330 174 SEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAG 210
Cdd:PRK10762 182 RVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-218 |
6.26e-13 |
|
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: 69.44 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndVAPKERD-----IAMVFQSYALYPHmtvrenm 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDR------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 97 gfalkLQGRDKATINKLVSEaagilalepLLERL--------------PKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:COG4615 421 -----LLGLDGEADPARARE---------LLERLeldhkvsvedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 163 NPDAKLR-VTMRSEIKELHQRlGTTIVYVTHDQiEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:COG4615 487 DQDPEFRrVFYTELLPELKAR-GKTVIAISHDD-RYFDLADRVLKMDYGKLVELTGP 541
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-242 |
7.44e-13 |
|
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: 70.04 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGR-VMNDVAPKERDIAMVFQSYALYPHMTVRENMGFALKLQG 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 105 RDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELhQRLG 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREG 2120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 644976330 185 TTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTFVAAF-IGSPSMNLF 242
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLL 2179
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-210 |
2.12e-12 |
|
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: 68.40 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmndvapkerdIAMVFQSYALYPHmTVRENMG 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 FALKL-QGRDKATINKLVSEAAgiLALEPLLERLPK-----QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDaklrVT 171
Cdd:TIGR01271 509 FGLSYdEYRYTSVIKACQLEED--IALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 172 MRSEIKE--LHQRLGTTIVYVTHDQIEAMTMADKIVVMRAG 210
Cdd:TIGR01271 583 TEKEIFEscLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-205 |
2.31e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAG---LEDisgGEIRID-----------------GRVMNDVAPKERDIAMVFQSYA 85
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEqdlivarlqqdpprnveGTVYDFVAEGIEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 86 LYPHMTVRENMGFALKLQGRDKATINKL--------VSEAAGILALEPllERLPKQLSGGQRQRVAMGRAIVRHPKVFLF 157
Cdd:PRK11147 103 DISHLVETDPSEKNLNELAKLQEQLDHHnlwqlenrINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 158 DEPLSNPDAklrvtmrSEIKELHQRLGT---TIVYVTHDQIEAMTMADKIV 205
Cdd:PRK11147 181 DEPTNHLDI-------ETIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIV 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-210 |
4.28e-12 |
|
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: 65.65 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 15 AASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmndvapkerdIAMVFQSYALYPHmTVRE 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NMGFALKL-QGRDKATINKlvseaagiLALEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFDEPLS 162
Cdd:cd03291 117 NIIFGVSYdEYRYKSVVKA--------CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 163 NPDaklrVTMRSEIKE---LHQRLGTTIVYVThDQIEAMTMADKIVVMRAG 210
Cdd:cd03291 189 YLD----VFTEKEIFEscvCKLMANKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-193 |
6.07e-12 |
|
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: 66.50 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 34 LVGPSGCGKSTLLRMLAGLEDISGGEIRIdgrvmndvAPKERdIAMVFQSYALYPHMTVREN--MGFALKLQGRDK---- 107
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QPGIK-VGYLPQEPQLDPTKTVRENveEGVAEIKDALDRfnei 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 108 --------ATINKLVSE---------AAGILALEPLLE------RLP------KQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:TIGR03719 107 sakyaepdADFDKLAAEqaelqeiidAADAWDLDSQLEiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLD 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 644976330 159 EPLSNPDAK----LRvtmrseiKELHQRLGtTIVYVTHD 193
Cdd:TIGR03719 187 EPTNHLDAEsvawLE-------RHLQEYPG-TVVAVTHD 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-212 |
7.61e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDIS----GGEIRIDGRVMNDVAPKER-DIAMVFQSYALYPHMTVRENM 96
Cdd:TIGR00956 80 MDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 97 GFALKLQG--------RDKATINKLVSEAAGILALE-----PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:TIGR00956 160 DFAARCKTpqnrpdgvSREEYAKHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTiVYVTHDQI--EAMTMADKIVVMRAGRI 212
Cdd:TIGR00956 240 LDSATALEFIRALKTSANILDTT-PLVAIYQCsqDAYELFDKVIVLYEGYQ 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
8-206 |
1.17e-11 |
|
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: 62.59 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 8 RVQKQYGAASVIHGVsADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDgRVMNDVAPKERDiamvfqsyaly 87
Cdd:cd03222 5 DCVKRYGVFFLLVEL-GVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-GITPVYKPQYID----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 phmtvrenmgfalklqgrdkatinklvseaagilalepllerlpkqLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAK 167
Cdd:cd03222 72 ----------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 644976330 168 LRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVV 206
Cdd:cd03222 106 QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-193 |
3.16e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 34 LVGPSGCGKSTLLRMLAGLEDISGGEIRidgrvmndVAPKERdIAMVFQSYALYPHMTVREN--MGFALKLQGRDK---- 107
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PAPGIK-VGYLPQEPQLDPEKTVRENveEGVAEVKAALDRfnei 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 108 --------ATINKLVSE---------AAGILALEPLLE------RLP------KQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:PRK11819 109 yaayaepdADFDALAAEqgelqeiidAADAWDLDSQLEiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLD 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 644976330 159 EPLSNPDAK----LRvtmrseiKELHQRLGtTIVYVTHD 193
Cdd:PRK11819 189 EPTNHLDAEsvawLE-------QFLHDYPG-TVVAVTHD 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-192 |
3.47e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.38 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIdgrvmndvaPKERDIAMVFQSyalyPHMTV---RE 94
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLgtlRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NM-----GFALKLQG-RDKATINKLVseaagILALEPLLER---------LPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:TIGR00954 534 QIiypdsSEDMKRRGlSDKDLEQILD-----NVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 644976330 160 PLSnpdaKLRVTMRSEIKELHQRLGTTIVYVTH 192
Cdd:TIGR00954 609 CTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-193 |
4.45e-11 |
|
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: 63.80 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerDIAMVFQSY-ALY 87
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 88 PHMTVRENMGfalklQGRDKATINKL-VSEAAGILALE---PLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:TIGR03719 399 PNKTVWEEIS-----GGLDIIKLGKReIPSRAYVGRFNfkgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
|
170 180 190
....*....|....*....|....*....|
gi 644976330 164 PDAKlrvTMRSEIKELHQRLGTTIVyVTHD 193
Cdd:TIGR03719 474 LDVE---TLRALEEALLNFAGCAVV-ISHD 499
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-234 |
9.57e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED----ISGGEIRIDGRVMNDVAPKER------DIAMVFQ- 82
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 -SYALYPhmtvRENMGFAL---------------KLQGRDKATINKLvsEAAGILALEPLLERLPKQLSGGQRQRVAMGR 146
Cdd:PRK15093 98 pQSCLDP----SERVGRQLmqnipgwtykgrwwqRFGWRKRRAIELL--HRVGIKDHKDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 147 AIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPN 226
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPH 251
|
....*...
gi 644976330 227 NTFVAAFI 234
Cdd:PRK15093 252 HPYTQALI 259
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-216 |
1.73e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLE--DISGGEIRIDGRVMNDVAPKERD---IAMVFQsyalYP-HMT 91
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQ----YPiEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENMGF----------ALKLQGRDKATINKLVSEAAGILALEP-LLER-LPKQLSGGQRQRVAMGRAIVRHPKVFLFDE 159
Cdd:CHL00131 98 GVSNADFlrlaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRnVNEGFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 160 PLSNPDAKLRVTMRSEIKELhQRLGTTIVYVTHDQ-IEAMTMADKIVVMRAGRIEQIG 216
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKL-MTSENSIILITHYQrLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-216 |
4.38e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGrvmndvapkerDIAMVFQSYALYPHMTVRENMGFALK 101
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 102 LQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQ 181
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170 180 190
....*....|....*....|....*....|....*
gi 644976330 182 RlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK13546 192 Q-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-214 |
4.78e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.48 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISgGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmT 91
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENmgfaLKLQGRDKATINKLVSEAAGilaLEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:cd03289 93 FRKN----LDPYGKWSDEEIWKVAEEVG---LKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 161 LSNPDAklrVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQ 214
Cdd:cd03289 166 SAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-193 |
5.25e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 6 IDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLR-MLAGLEDISgGEIRIDGRVmnDVApkerdiamVFQSY 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTKL--EVA--------YFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 85 --ALYPHMTVRENMGfalklQGRDKATINKLVSEAAGILA---LEPLLERLP-KQLSGGQRQRVAMGRAIVRHPKVFLFD 158
Cdd:PRK11147 391 raELDPEKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdflFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*....
gi 644976330 159 EPLSNPDAklrvtmrsEIKELHQRLGT----TIVYVTHD 193
Cdd:PRK11147 466 EPTNDLDV--------ETLELLEELLDsyqgTVLLVSHD 496
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-221 |
5.94e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGleDISG----------GEIRIDGR-----------VMNDVAPKERD 76
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEplaaidaprlaRLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 IAMVFQSYAL-----YPHMtvreNMGFALKLQGRDkatinkLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAI--- 148
Cdd:PRK13547 94 PAFAFSAREIvllgrYPHA----RRAGALTHRDGE------IAWQALALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 149 ------VRHPKVFLFDEPLSNPDA----KLRVTMRSEIKELHqrLGttIVYVTHDQIEAMTMADKIVVMRAGRIEQIGKP 218
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWN--LG--VLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
...
gi 644976330 219 LDL 221
Cdd:PRK13547 240 ADV 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-207 |
9.74e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 26 IEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRI-DGRVMNDVAPK--ERDIAMVFQSYALYPHmTVRENMGFAL-- 100
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKNNIKYSLys 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 101 --KLQG-------------RDKATINKLVSEAAGILAL------------------------------------------ 123
Cdd:PTZ00265 487 lkDLEAlsnyynedgndsqENKNKRNSCRAKCAGDLNDmsnttdsneliemrknyqtikdsevvdvskkvlihdfvsalp 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 124 ---EPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHdQIEAMTM 200
Cdd:PTZ00265 567 dkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-RLSTIRY 645
|
....*..
gi 644976330 201 ADKIVVM 207
Cdd:PTZ00265 646 ANTIFVL 652
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-210 |
1.26e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 21 GVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED---ISGGEIRIDGRVMNdvAPKERDIAMVFQSYALYPHMTVRENMG 97
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 98 FALKLQGRDKATI---NKLVSEAAGILALEPLLERL---PKQ-LSGGQRQRVAMGRAIVRHPKVFLF-DEPLSNPDAKLR 169
Cdd:TIGR00956 859 FSAYLRQPKSVSKsekMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 644976330 170 VTMRSEIKELHQRlGTTIVYVTHdQIEAMTMA--DKIVVMRAG 210
Cdd:TIGR00956 939 WSICKLMRKLADH-GQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-214 |
1.29e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDiSGGEIRIDGRVMNDVAPKERDiamvfQSYALYPHMTVR 93
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-----KAFGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFALKLQGRDKATINKL--VSEAAGilaLEPLLERLPKQ-----------LSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQWSDEEIwkVAEEVG---LKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 161 LSNPDAklrVTMRSEIKELHQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQ 214
Cdd:TIGR01271 1381 SAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
34-211 |
1.41e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 34 LVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE---RDIAMVFQSYALYPHMTVRENM---GFALKLQGRDK 107
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 108 atiNKLVSEAAGILAlEPLLERLPKQ----LSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRl 183
Cdd:PRK10982 109 ---DKMYRDTKAIFD-ELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER- 183
|
170 180
....*....|....*....|....*...
gi 644976330 184 GTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:PRK10982 184 GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-229 |
1.50e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGrvmNDVAP-----KERDIAMVFQSYALYPHmTV 92
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG---CDISKfglmdLRKVLGIIPQAPVLFSG-TV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMG-F-----ALKLQGRDKATINKLVSEAAgiLALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLS---- 162
Cdd:PLN03130 1330 RFNLDpFnehndADLWESLERAHLKDVIRRNS--LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAavdv 1407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 163 NPDAKLRVTMRSEIKE-----LHQRLGTTIvyvthDqieamtmADKIVVMRAGRIEQIGKPLDLYDRPNNTF 229
Cdd:PLN03130 1408 RTDALIQKTIREEFKSctmliIAHRLNTII-----D-------CDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-221 |
3.63e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKE--RDIAMVFQSYALYPHmTVREN 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 96 MG-----------FALKLqgrdkATINKLVSEAAGILALEplLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNP 164
Cdd:TIGR00957 1380 LDpfsqysdeevwWALEL-----AHLKTFVSALPDKLDHE--CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 644976330 165 DAKLRVTMRSEIKElhQRLGTTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDL 221
Cdd:TIGR00957 1453 DLETDNLIQSTIRT--QFEDCTVLTIAH-RLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-213 |
1.02e-08 |
|
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: 56.37 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGL-EDISGGEIRIDGRVMNDVAPK---ERDIAMVFQS---YALYPHMTVRE 94
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 95 NMGFAL-----KLQGRDKATINKLVSEAAGILALEPLLERLP-KQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKL 168
Cdd:TIGR02633 359 NITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 644976330 169 RVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIE 213
Cdd:TIGR02633 439 KYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-169 |
1.17e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 36 GPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKErdIAMVFQSYALYPHMTVRENMGFALKLQgrDKATinkLVS 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFENLKFWSEIY--NSAE---TLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 116 EAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLR 169
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-212 |
1.47e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGL-EDISGGEIRIDGRVMNDVAPKE---RDIAMVFQS---YALYPHM 90
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 91 TVRENMgfalKLQGRDKATINKLVSEAAGILALEPLLERLP----------KQLSGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:PRK13549 357 GVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 644976330 161 LSNPDaklrVTMRSEIKELHQRL---GTTIVYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK13549 433 TRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-280 |
1.51e-08 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 50.27 E-value: 1.51e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 235 GSPSMNLFEGGVSDGGFRIE-GGVSLPLPPQLSHSAAR------TYGIRPEDL 280
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLgGGVTLPLPEGQVLALKLyvgkevILGIRPEHI 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-219 |
1.62e-08 |
|
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: 53.15 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 29 GEFVTLVGPSGCGKSTLLRMLAG-LEDISGGEIRIDGRVMNDVAPKERdiamvfqsyalyphmtvrenmgfalklqgrdk 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 108 atinklvseaagilaLEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEI-----KELHQR 182
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSE 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 644976330 183 LGTTIVYVTHDQIEAMTMADKIvvmRAGRIEQIGKPL 219
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR---RFDRRIVLLLIL 148
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-215 |
3.51e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVMNDVAPKErdiAMvfqsyalyphmtvreNMGF 98
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE---AI---------------NHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKLQGRDKATI--------NKLVS------EAAGILA-----------LEPLLERLPKQ------LSGGQRQRVAMGRA 147
Cdd:PRK10982 326 ALVTEERRSTGIyayldigfNSLISnirnykNKVGLLDnsrmksdtqwvIDSMRVKTPGHrtqigsLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 148 IVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQI 215
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-210 |
4.32e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQkqygaasVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEdiSGG----EIRIDGrvmndvAPKERDIAM 79
Cdd:PLN03140 888 VTEDRLQ-------LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGGyiegDIRISG------FPKKQETFA 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 80 VFQSYALY-----PHMTVRENMGFALKLqgRDKATINK-----LVSEAAGILALEPLLER---LP--KQLSGGQRQRVAM 144
Cdd:PLN03140 953 RISGYCEQndihsPQVTVRESLIYSAFL--RLPKEVSKeekmmFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTI 1030
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644976330 145 GRAIVRHPKVFLFDEPLSNPDAK-LRVTMRSEIKELHQrlGTTIVYVTHD-QIEAMTMADKIVVMRAG 210
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARaAAIVMRTVRNTVDT--GRTVVCTIHQpSIDIFEAFDELLLMKRG 1096
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-197 |
7.00e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 12 QYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGleD---------ISGGEIRIDGRVMNDVapkERDIAMVfq 82
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DhpqgysndlTLFGRRRGSGETIWDI---KKHIGYV-- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 83 SYALypHMTVRENM--------GFAlklqgrDKATINKLVSEAAGILALEpLLERL---------P-KQLSGGQRQRVAM 144
Cdd:PRK10938 342 SSSL--HLDYRVSTsvrnvilsGFF------DSIGIYQAVSDRQQKLAQQ-WLDILgidkrtadaPfHSLSWGQQRLALI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 644976330 145 GRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRLGTTIVYVTHDQIEA 197
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-217 |
9.23e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 3 SVAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCG--KSTLLRMLAGlEDISGGEIRIDGRVMNDVAPKERDIAMV 80
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*TWCANRRALRRTIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 81 FQSYALYPHMTVRENM---GFALKLQGRD-KATINKLV-----SEAAGilaleplleRLPKQLSGGQRQRVAMGRAIVRH 151
Cdd:NF000106 92 PVR*GRRESFSGRENLymiGR*LDLSRKDaRARADELLerfslTEAAG---------RAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 152 PKVFLFDEPLSNPDAKLRVTMRSEIKELhQRLGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-174 |
1.20e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerDIAMVFQSyalyp 88
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVDQS----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 89 hmtvRENMGfalklqgrDKATINKLVSEAAGILALE-----------------PLLERLPKQLSGGQRQRVAMGRAIVRH 151
Cdd:PRK11819 396 ----RDALD--------PNKTVWEEISGGLDIIKVGnreipsrayvgrfnfkgGDQQKKVGVLSGGERNRLHLAKTLKQG 463
|
170 180
....*....|....*....|....
gi 644976330 152 PKVFLFDEPlSNpDakLRV-TMRS 174
Cdd:PRK11819 464 GNVLLLDEP-TN-D--LDVeTLRA 483
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
240-282 |
1.36e-07 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 47.44 E-value: 1.36e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 644976330 240 NLFEGGVSDGGFRIeGGVSLPLP-PQLSHSAARTYGIRPEDLDI 282
Cdd:pfam17850 1 NLFHGRVEDGRVRI-GGLALPLPeLAGAEGSEVVAYVRPHDLEI 43
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-216 |
1.39e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLED--ISGGEIRIDGRVMNDVAPKER---DIAMVFQSYALYPHMTV 92
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMGFALKL--QGRDKATINK-----LVSEAAGILALEP-LLER-LPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSN 163
Cdd:PRK09580 96 QFFLQTALNAvrSYRGQEPLDRfdfqdLMEEKIALLKMPEdLLTRsVNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 164 PDAKLRVTMRSEIKELHQRLGTTIVyVTHDQ-IEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFII-VTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
274-340 |
1.84e-07 |
|
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: 48.00 E-value: 1.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644976330 274 GIRPEDLDI--AETGIPATVLTVEPTGAETHLSVRVGTQTATIVL---HRRVDLKPDQQIDLAPKSEKIHLF 340
Cdd:pfam08402 2 AIRPEKIRLaaAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRvpnAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-229 |
2.41e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.45 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 18 VIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRvmnDVAP------KERdIAMVFQSYALYPHmT 91
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKlplhtlRSR-LSIILQDPILFSG-S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 92 VRENmgfalkLQGRDKATINKLvSEAAGILALEPLLERLPKQL-----------SGGQRQRVAMGRAIVRHPKVFLFDEP 160
Cdd:cd03288 111 IRFN------LDPECKCTDDRL-WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 161 LSNPD-AKLRVTMRSEIKELHQRlgtTIVYVTHdQIEAMTMADKIVVMRAGRIEQIGKPLDLYDRPNNTF 229
Cdd:cd03288 184 TASIDmATENILQKVVMTAFADR---TVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-212 |
4.96e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 17 SVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDIS---GGEIRIDGRVMNDVAPKERDiAMVFQSYALYPHMTVR 93
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTS-AYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 94 ENMGFALKLQGrdKATINKLVSEA------AGIL------------ALEPLLERL-----------------------PK 132
Cdd:PLN03140 258 ETLDFSARCQG--VGTRYDLLSELarrekdAGIFpeaevdlfmkatAMEGVKSSLitdytlkilgldickdtivgdemIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 133 QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKlrvTMRSEIKELHQRL----GTTIVYVTHDQIEAMTMADKIVVMR 208
Cdd:PLN03140 336 GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSS---TTYQIVKCLQQIVhlteATVLMSLLQPAPETFDLFDDIILLS 412
|
....
gi 644976330 209 AGRI 212
Cdd:PLN03140 413 EGQI 416
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
8.83e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 4 VAIDRVQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEI------RIdGRVMNDVAPK-ERD 76
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNI-GYYAQDHAYDfEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 77 iamvfqsyalyphMTVRENMGfalklQGRdkatinklvSEAAGILALEPLLERL----------PKQLSGGQRQRVAMGR 146
Cdd:PRK15064 399 -------------LTLFDWMS-----QWR---------QEGDDEQAVRGTLGRLlfsqddikksVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 147 AIVRHPKVFLFDEPLSNPDaklrvtMRSeIKELHQRL----GTTIvYVTHDQIEAMTMADKIVVMRAGRI 212
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMD------MES-IESLNMALekyeGTLI-FVSHDREFVSSLATRIIEITPDGV 513
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-216 |
1.31e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRIDGRVmndvapkerdiAMVFQSYALYPHMTVRENMGF 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKLQGRDKATINKLVSEAAGILALEPLLERLPKQLSGGQRQRvaMGRAIVRH--PKVFLFDEPLSNPDAKLRVTMRSEI 176
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSR--LGFAISVHinPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 644976330 177 KELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGRIEQIG 216
Cdd:PRK13545 187 NEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-211 |
2.62e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 22 VSADIEDGEFVTLVGPSGCGKSTLLRMLAGL------EdisgGEIRIDGRVMN--DVAPKERD-IAMVFQSYALYPHMTV 92
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRfkDIRDSEALgIVIIHQELALIPYLSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 93 RENMgFALKLQGRdKATI--NKLVSEAAGILA---LEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEP---LSNP 164
Cdd:NF040905 96 AENI-FLGNERAK-RGVIdwNETNRRARELLAkvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPtaaLNEE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 644976330 165 DaklrvtmrSE-----IKELHQRlGTTIVYVTHDQIEAMTMADKIVVMRAGR 211
Cdd:NF040905 174 D--------SAalldlLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-217 |
3.25e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 19 IHGVSADIEDGEFVTLVGPSGCGKSTLLrmLAGLEdisggeiridgrvmndvAPKERDIAMVFQSYalYPHMTVrenmgF 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLY-----------------ASGKARLISFLPKF--SRNKLI-----F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 99 ALKLQgrdkatinKLVSEAAGILALEplleRLPKQLSGGQRQRVAMGRAIVRHPK--VFLFDEPLSNPDAKLRVTMRSEI 176
Cdd:cd03238 65 IDQLQ--------FLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 644976330 177 KELHQrLGTTIVYVTHDqIEAMTMADKIVVMRAGRIEQIGK 217
Cdd:cd03238 133 KGLID-LGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-165 |
3.28e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 32 VTLVGPSGCGKSTLLRMLAG-LEDISGGEIRidgrvmndvAPKERdIAMVFQSYA----------LY--------PHMTV 92
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGeLQPSSGTVFR---------SAKVR-MAVFSQHHVdgldlssnplLYmmrcfpgvPEQKL 607
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 93 RENMG-FALklqgrdkatinklvseaAGILALEPLLerlpkQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:PLN03073 608 RAHLGsFGV-----------------TGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-214 |
5.79e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 9 VQKQYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAgledisgGEIRIDGRVMNdvAPKERDIAMVFQS----- 83
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYT--FPGNWQLAWVNQEtpalp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 84 -----YALYPHMTVRE-----------NMGFAL-----KLQGRDKATINklvSEAAGILA----LEPLLERLPKQLSGGQ 138
Cdd:PRK10636 78 qpaleYVIDGDREYRQleaqlhdanerNDGHAIatihgKLDAIDAWTIR---SRAASLLHglgfSNEQLERPVSDFSGGW 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644976330 139 RQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRseiKELHQRLGTTIVyVTHDQIEAMTMADKIVvmragRIEQ 214
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLE---KWLKSYQGTLIL-ISHDRDFLDPIVDKII-----HIEQ 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-193 |
1.57e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 12 QYGAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLAG-LEDISG----------GEIR-----------IDGRVMND 69
Cdd:PRK15064 10 QFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSAGnvsldpnerlGKLRqdqfafeeftvLDTVIMGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 70 V----APKERDiamvfQSYALyPHMTVRENMGFAlKLQGRdKATINKLVSEA-AGILALE---PLLER--LPKQLSGGQR 139
Cdd:PRK15064 90 TelweVKQERD-----RIYAL-PEMSEEDGMKVA-DLEVK-FAEMDGYTAEArAGELLLGvgiPEEQHygLMSEVAPGWK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 140 QRVAMGRAIVRHPKVFLFDEPLSNPDAKlrvTMRSEIKELHQRLGTTIVyVTHD 193
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDIN---TIRWLEDVLNERNSTMII-ISHD 211
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
32-110 |
1.86e-04 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 41.32 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 32 VTLVGPSGCGKSTLLRMLA---GLEDISGGEIRIDgrvmndvapkerDIAMVFQSYALYPHmtVRENMgfaLKLQ----- 103
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAkklGLPYLDTGGIRTE------------EVGKLASEVAAIPE--VRKAL---DERQrelak 64
|
90
....*....|....
gi 644976330 104 -------GRDKATI 110
Cdd:cd02020 65 kpgivleGRDIGTV 78
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
31-60 |
2.29e-04 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 41.33 E-value: 2.29e-04
10 20 30
....*....|....*....|....*....|...
gi 644976330 31 FVTLVGPSGCGKSTLLRMLA---GLEDISGGEI 60
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEI 34
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-61 |
7.73e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 7.73e-04
10 20 30
....*....|....*....|....*....|...
gi 644976330 29 GEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIR 61
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
111-190 |
1.44e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 111 NKLVSEAAGILALEPLLERLPKQLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPDAKLRVTMRSEIKELHQRlGTTIVYV 190
Cdd:PRK10938 113 PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-211 |
2.33e-03 |
|
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: 40.00 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 90 MTVRENMGF--ALKLQGRDKATINKLVSEAA---GIL---ALEPL-LERLPKQLSGGQRQRVAMGRAI------VrhpkV 154
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKIAEEVLKEIRerlGFLidvGLDYLsLSRAAGTLSGGEAQRIRLATQIgsgltgV----L 511
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644976330 155 FLFDEP---LSNPD-AKLRVTMRseikelHQR-LGTTIVYVTHDQiEAMTMADKIVVM--RAGR 211
Cdd:TIGR00630 512 YVLDEPsigLHQRDnRRLINTLK------RLRdLGNTLIVVEHDE-DTIRAADYVIDIgpGAGE 568
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-165 |
2.69e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 14 GAASVIHGVSADIEDGEFVTLVGPSGCGKSTLLRMLA-----GL----------EDISGGEIRIDGRVMN-DVapkERDI 77
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqilhveQEVVGDDTTALQCVLNtDI---ERTQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644976330 78 AMVFQSYALYPHMTVRENMGFAlKLQGRDKATINK-LVSE--------------------AAGILA---LEPLLE-RLPK 132
Cdd:PLN03073 265 LLEEEAQLVAQQRELEFETETG-KGKGANKDGVDKdAVSQrleeiykrlelidaytaearAASILAglsFTPEMQvKATK 343
|
170 180 190
....*....|....*....|....*....|...
gi 644976330 133 QLSGGQRQRVAMGRAIVRHPKVFLFDEPLSNPD 165
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
28-65 |
2.98e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 2.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 644976330 28 DGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRID---GR 65
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDdskGR 234
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-65 |
4.06e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 4.06e-03
10 20 30
....*....|....*....|....*....|....*....
gi 644976330 28 DGEFVTLVGPSGCGKSTLLRMLAGLEDISGGEIRI-DGR 65
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEkLGR 143
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-50 |
4.57e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.23 E-value: 4.57e-03
10 20
....*....|....*....|....*.
gi 644976330 26 IEDGE-FVTLVGPSGCGKSTLLRMLA 50
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| PEPCK_HprK |
cd00820 |
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ... |
20-61 |
8.82e-03 |
|
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of HPr and its dephosphorylation by phosphorolysis. PEPCK and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting that these two phosphotransferases have related functions.
Pssm-ID: 238418 [Multi-domain] Cd Length: 107 Bit Score: 35.73 E-value: 8.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 644976330 20 HGVSADIEDGEFVTLVGPSGCGKSTLLRML------------AGLEDISGGEIR 61
Cdd:cd00820 6 HGVLVDVYGKVGVLITGDSGIGKTELALELikrkhrlvgddnVEIREDSKDELI 59
|
|
| |
