|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-332 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 572.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSPQMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 241 LIPAE-------------------KLEQGGAKTIGIRPEHITLSRE-QGTWAAKVVHVEHLGADTIIYLESDHTgLLTVR 300
Cdd:COG3839 241 LLPGTvegggvrlggvrlplpaalAAAAGGEVTLGIRPEHLRLADEgDGGLEATVEVVEPLGSETLVHVRLGGQ-ELVAR 319
|
330 340 350
....*....|....*....|....*....|...
gi 494968020 301 LFGEHQYEPDETVYATPDTGHMHRFD-ENGQAI 332
Cdd:COG3839 320 VPGDTRLRPGDTVRLAFDPERLHLFDaETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-330 |
3.36e-180 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 502.45 E-value: 3.36e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSPQM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 240 NLIPAEKLEQGGA----------------------KTIGIRPEHITLSREQGTWAAKVVHVEHLGADTIIYLE-SDHTgl 296
Cdd:PRK11650 241 NLLDGRVSADGAAfelaggialplgggyrqyagrkLTLGIRPEHIALSSAEGGVPLTVDTVELLGADNLAHGRwGGQP-- 318
|
330 340 350
....*....|....*....|....*....|....
gi 494968020 297 LTVRLFGEHQYEPDETVYATPDTGHMHRFDENGQ 330
Cdd:PRK11650 319 LVVRLPHQERPAAGSTLWLHLPANQLHLFDADTG 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-327 |
1.18e-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: 439.92 E-value: 1.18e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGspQMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 241 LIPAE----------------------KLEQGGAKTIGIRPEHITLSRE--QGTWAAKVVHVEHLGADTIIYLESDHTGL 296
Cdd:COG3842 241 LLPGTvlgdegggvrtggrtlevpadaGLAAGGPVTVAIRPEDIRLSPEgpENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
|
330 340 350
....*....|....*....|....*....|...
gi 494968020 297 LTVRLFGEH--QYEPDETVYATPDTGHMHRFDE 327
Cdd:COG3842 321 LVVRVPNRAalPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-290 |
6.26e-154 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 436.38 E-value: 6.26e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSPQMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 241 LIP-----AEK---------------------LEQGGAKTIGIRPEHItLSREQG--TWAAKVVHVEHLGADTIIYLE 290
Cdd:PRK11000 241 FLPvkvtaTAIeqvqvelpnrqqvwlpvegrgVQVGANMSLGIRPEHL-LPSDIAdvTLEGEVQVVEQLGNETQIHIQ 317
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
4.47e-125 |
|
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: 356.95 E-value: 4.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-318 |
2.05e-116 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 340.20 E-value: 2.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV-TPPAKRGISMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGspQMNL 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 242 IPAEKLE----------------QGGAKTIGIRPEHITLSRE---QGTWAAKVVHVEHLGADTIIYLESDHTG--LLTVR 300
Cdd:COG1118 240 LRGRVIGgqleadgltlpvaeplPDGPAVAGVRPHDIEVSREpegENTFPATVARVSELGPEVRVELKLEDGEgqPLEAE 319
|
330 340
....*....|....*....|..
gi 494968020 301 L----FGEHQYEPDETVYATPD 318
Cdd:COG1118 320 VtkeaWAELGLAPGDPVYLRPR 341
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
3.15e-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: 333.05 E-value: 3.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-293 |
7.70e-112 |
|
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: 328.92 E-value: 7.70e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGspQMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 241 LIPAEK-------------------LEQGGAKTIGIRPEHITLSR---EQGTWAAKVVHVEHLGADTIIYLESDH 293
Cdd:TIGR03265 240 WLPGTRgggsrarvggltlacapglAQPGASVRLAVRPEDIRVSPagnAANLLLARVEDMEFLGAFYRLRLRLEG 314
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
1.08e-111 |
|
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: 323.32 E-value: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-255 |
2.74e-111 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 328.06 E-value: 2.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGspQMNLIP 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
250
....*....|..
gi 494968020 244 AEKLEQGGAKTI 255
Cdd:PRK09452 253 ATVIERLDEQRV 264
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-282 |
1.14e-97 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 292.78 E-value: 1.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGspQMNLIP 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMG--DANIFP 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 244 AeKLEQG---------------------GAKTIGIRPEHITLSrEQGTWAAK--VVHVEHLG 282
Cdd:PRK11432 245 A-TLSGDyvdiygyrlprpaafafnlpdGECTVGVRPEAITLS-EQGEESQRctIKHVAYMG 304
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
7-318 |
5.82e-93 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 280.73 E-value: 5.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 7 KSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-----VTPPAKRGISMVF 81
Cdd:NF040933 10 KIFKKGKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVAspgkiIVPPEDRNIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:NF040933 90 QNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVLLLDEPF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGspQMNL 241
Cdd:NF040933 170 SNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLIG--DINL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 242 IPAeKLEQGGAKT-------------------IGIRPEHITLSREQGTWA--------AKVVHVEHLGADTIIYLESDHT 294
Cdd:NF040933 248 LEG-KVEEEGLVDgndlkiplpnpkleageviIGIRPEDIDISESDMRLPpgfvevgkGRVKVSSYAGGVFRVVVSPIDD 326
|
330 340
....*....|....*....|....*.
gi 494968020 295 GLLTVRLFGEHQYEPDETV--YATPD 318
Cdd:NF040933 327 DSIEIIVNSDRPIEEGEEVnlYVRPD 352
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
1.68e-90 |
|
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: 270.36 E-value: 1.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQ 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLK----QAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 159 EPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGS 236
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-255 |
6.41e-89 |
|
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: 269.36 E-value: 6.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 35 VGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 115 AKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 195 VEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSpqMNLIPAEKLEQGGAKTI 255
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERKSEQVV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-210 |
3.63e-88 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 265.03 E-value: 3.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY----GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTvTPPAKRGisM 79
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-GPGPDRG--V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
5.89e-88 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 263.97 E-value: 5.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-325 |
4.46e-84 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 257.70 E-value: 4.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQSYALYPHLTVKDNMGL 98
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 99 GLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIAR 178
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 179 LHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSPqmNLIP--AEKLEQG------ 250
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEgvAEKGGEGtildtg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 251 -----------GAKTIGIRPEHITLSREQ-GTWA-----AKVVHVEHLGadTIIYLESD----HTGLLTVRLFGEHQYEP 309
Cdd:NF040840 254 nikielpeekkGKVRIGIRPEDITISTEKvKTSArnefkGKVEEIEDLG--PLVKLTLDvgiiLVAFITRSSFLDLEINE 331
|
330
....*....|....*.
gi 494968020 310 DETVYATPDTGHMHRF 325
Cdd:NF040840 332 GKEVYASFKASAVHVF 347
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-255 |
1.62e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 255.02 E-value: 1.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGISMVF 81
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEP--YLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGS--- 236
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAdrg 242
|
250 260
....*....|....*....|
gi 494968020 237 -PQMNLIPAEKLEQGGAKTI 255
Cdd:COG1125 243 lRRLSLLRVEDLMLPEPPTV 262
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
9.90e-83 |
|
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: 250.33 E-value: 9.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHdVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIG 235
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
1.17e-82 |
|
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: 249.70 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT----HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAkrgISM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNA 209
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
4.67e-81 |
|
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: 246.44 E-value: 4.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGISMV 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEP--YLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 159 EPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSPQ 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-307 |
3.78e-78 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 243.59 E-value: 3.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSPQM---- 239
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVfegv 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 240 -------NLI-------------PAEKLEQGGAKTIGIRPEHITLSRE---QGTWAA--KVVHVEHLGaDTIIYLESDHT 294
Cdd:PRK11607 260 lkerqedGLVidspglvhplkvdADASVVDNVPVHVALRPEKIMLCEEppaDGCNFAvgEVIHIAYLG-DLSIYHVRLKS 338
|
330
....*....|....
gi 494968020 295 G-LLTVRLFGEHQY 307
Cdd:PRK11607 339 GqMISAQLQNAHRY 352
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-305 |
9.62e-76 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 236.52 E-value: 9.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLK----QAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 159 EPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGSP- 237
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 238 ------------------QMNLIPAEKleqgGAKTIGIRPEHITLSREQGTWA---AKVVHVEHLGADTIIYLESD--HT 294
Cdd:PRK10851 242 rlqgtirggqfhvgahrwPLGYTPAYQ----GPVDLFLRPWEVDISRRTSLDSplpVQVLEVSPKGHYWQLVVQPLgwYN 317
|
330
....*....|.
gi 494968020 295 GLLTVRLFGEH 305
Cdd:PRK10851 318 EPLTVVMHGDI 328
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
1.58e-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: 222.45 E-value: 1.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT----VTPPAKRGISM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGlkqagtakeeiesrvakasgmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
1.84e-70 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 218.76 E-value: 1.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD----VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--- 76
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ---ISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 154 LFLFDEPLSNLDAAlrvqTRLEI----ARLHRSLKATMIYVTHDQvEAMTLADKIVVMNAGAIE 213
Cdd:COG1136 165 LILADEPTGNLDSK----TGEEVlellRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-227 |
5.91e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 217.70 E-value: 5.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGthDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
1.60e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 216.78 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA----KRGISM 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKQA-GTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 159 EPLSNLDAALrVQtrlEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:COG1126 162 EPTSALDPEL-VG---EVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-234 |
3.45e-69 |
|
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: 217.13 E-value: 3.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA------KRGISMVFQSYALYPHLTVKDN 95
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLE 175
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 176 IARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFI 234
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-223 |
9.54e-69 |
|
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: 214.84 E-value: 9.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGIS 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLGLKQAGT-AKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 158 DEPLSNLD-AALRVQTRLeIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:COG1127 166 DEPTAGLDpITSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
9.12e-68 |
|
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: 211.58 E-value: 9.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYG----THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--- 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ---ISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 154 LFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMtLADKIVVMNAGAI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
4.55e-66 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 207.74 E-value: 4.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGIS 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLGLKQAGT-AKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 158 DEPLSNLD-AALRVQTRLeIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03261 161 DEPTAGLDpIASGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-216 |
7.58e-66 |
|
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: 206.38 E-value: 7.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 9 IRKAYGTHDvLKgIDLEVkDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGkdvTV---------TPPAKRGISM 79
Cdd:cd03297 6 IEKRLPDFT-LK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVlfdsrkkinLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKqaGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
8.70e-64 |
|
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: 202.34 E-value: 8.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT----HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGI 77
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSY--ALYPHLTVKDNMGLGLKQAGTAkeEIESRVAKASGMLSLEP-YLARRPAELSGGQRQRVAIGRAIVREPEL 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 155 FLFDEPLSNLDAALRVQT-RLeIARLHRSLKATMIYVTHDqVEAMT-LADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:COG1124 160 LLLDEPTSALDVSVQAEIlNL-LKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
1.39e-63 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 200.83 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA----KRGISM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKQA-GTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 159 EPLSNLDAALrVQTRLE-IARLHRSlKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03262 161 EPTSALDPEL-VGEVLDvMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-226 |
1.70e-62 |
|
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: 202.64 E-value: 1.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLING-------KDVTVtPPAKRGISMVFQSYALYPHLTVKD 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIFL-PPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLGLKQAGTAKEEIesRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAlrvqTRL 174
Cdd:COG4148 97 NLLYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA----RKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 175 EI----ARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:COG4148 171 EIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
3.53e-62 |
|
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: 197.55 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGISMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQsyalYP-----HLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELF 155
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 156 LFDEPLSNLDAALRVQTRLEIARLHRSLKaTMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-210 |
3.51e-61 |
|
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: 194.22 E-value: 3.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGTHD--VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--ISMV 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQsyalYP-----HLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELF 155
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 156 LFDEPLSNLDAALRVQTRLEIARLHRSLKaTMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
4.66e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 194.90 E-value: 4.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP-AKRGISMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 163 NLDAALRVQTRLEIARLHRSlKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
7.14e-60 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 200.13 E-value: 7.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY-----GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 -RGISMVFQ--SYALYPHLTVKDNMGLGLKQAGTA-KEEIESRVAKASGMLSLEP-YLARRPAELSGGQRQRVAIGRAIV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHD--QVEAMtlADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-216 |
1.15e-58 |
|
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: 188.48 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD----VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--- 76
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 --ISMVFQSY--ALYPHLTVKDNMGLGLK--QAGTAKEEIESRVAKASGMLSLEPYLARR-PAELSGGQRQRVAIGRAIV 149
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
9.22e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 186.84 E-value: 9.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGI----SM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLG-LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 159 EPLSNLDAALrvqtRLEIARLHRSLK---ATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:PRK09493 162 EPTSALDPEL----RHEVLKVMQDLAeegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-212 |
1.40e-57 |
|
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: 185.39 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVlkGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
2.96e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 184.87 E-value: 2.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT-HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGI 77
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 158 DEPLSNLDAAlrvqTRLEIARLHRSLKA---TMIYVTHDQ--VEAMtlADKIVVMNAGAI 212
Cdd:COG2884 162 DEPTGNLDPE----TSWEIMELLEEINRrgtTVLIATHDLelVDRM--PKRVLELEDGRL 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-249 |
3.67e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 188.36 E-value: 3.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY----GTHDVLKGIDLEVKDGEfvIF--VGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP----- 72
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 73 AKRGISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKasgMLS---LEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAE---LLElvgLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 150 REPELFLFDEPLSNLDAalrvQTRLEI----ARLHRSLKATMIYVTHDqveaM----TLADKIVVMNAGAIEQIGSPMEL 221
Cdd:COG1135 157 NNPKVLLCDEATSALDP----ETTRSIldllKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDV 228
|
250 260
....*....|....*....|....*...
gi 494968020 222 YNRPANVFVGGFIGSPQMNLIPAEKLEQ 249
Cdd:COG1135 229 FANPQSELTRRFLPTVLNDELPEELLAR 256
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-238 |
5.93e-57 |
|
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: 184.86 E-value: 5.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRgISMV 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLG----LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 157 FDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPME---------LYNRPAN 227
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelleeVYGVEAR 240
|
250
....*....|.
gi 494968020 228 VFVGGFIGSPQ 238
Cdd:COG1120 241 VIEDPVTGRPL 251
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-226 |
2.53e-56 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 190.50 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVT---SGTVLINGKDVTVTPPAKRG--ISMVFQ 82
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 S--YALYPhLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:COG1123 91 DpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
3.71e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 182.95 E-value: 3.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD-VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGI 77
Cdd:COG3638 3 LELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDN--MGLgLKQAGT--------AKEEIEsRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRA 147
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlAGR-LGRTSTwrsllglfPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 148 IVREPELFLFDEPLSNLD--AALRVqtrLE-IARLHRSLKATMIYVTHdQVE-AMTLADKIVVMNAGAI 212
Cdd:COG3638 161 LVQEPKLILADEPVASLDpkTARQV---MDlLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
6.95e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 182.37 E-value: 6.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYG----THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTvTPPAKRG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 IsmVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494968020 157 FDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
2.08e-55 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 180.82 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP-AKRGISMVFQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 163 NLDAALRVQTRLEIARLhRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
6.27e-55 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 178.91 E-value: 6.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV-----TSGTVLINGKDV---TVTPPA-K 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydlDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 RGISMVFQSYALYPhLTVKDNMGLGLKQAGTA-KEEIESRVAKASGMLSLEPYLARR--PAELSGGQRQRVAIGRAIVRE 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 152 PELFLFDEPLSNLDAAlrvqTRLEIARLHRSLKA--TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03260 160 PEVLLLDEPTSALDPI----STAKIEELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-225 |
1.08e-54 |
|
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: 178.54 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHD----VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RG 76
Cdd:cd03258 4 LKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 157 FDEPLSNLDAalrvQTRLEIARL----HRSLKATMIYVTHdQVEAM-TLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:cd03258 164 CDEATSALDP----ETTQSILALlrdiNRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-226 |
5.91e-54 |
|
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: 180.31 E-value: 5.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHDVlkGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL------EDVTSGTVLINGKDVTVTPPAKRGISMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLtrpdegEIVLNGRTLFDSRKGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGLKQAGTAKEEIesRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
6.62e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.77 E-value: 6.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGISMVF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHlTVKDNMGLGLKQAGtaKEEIESRVAKASGMLSLEP-YLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494968020 161 LSNLDAALRvqTRLE--IARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:COG4619 158 TSALDPENT--RRVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
6.67e-54 |
|
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: 175.82 E-value: 6.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 23 DLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQSYALYPHLTVKDNMGLGLKQ 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 103 AGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRS 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 494968020 183 LKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-223 |
2.76e-53 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 174.77 E-value: 2.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 23 DLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQSYALYPHLTVKDNMGLGLKQ 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 103 AGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRS 182
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494968020 183 LKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-225 |
6.81e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 166.90 E-value: 6.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-------PAKR- 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 76 -------GISMVFQSYALYPHLTVKDNMG------LGLKQAgTAKEEIESRVAKASgmlslepyLARR----PAELSGGQ 138
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPKA-EAIERAEALLAKVG--------LADKrdayPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 139 RQRVAIGRAIVREPELFLFDEPLSNLDAALrVQtrlEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQI 215
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235
|
250
....*....|
gi 494968020 216 GSPMELYNRP 225
Cdd:COG4598 236 GPPAEVFGNP 245
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-225 |
9.35e-50 |
|
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: 167.24 E-value: 9.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 16 HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-----PAKRGISMVFQsyalYPH- 89
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkklkDLRKKVGLVFQ----FPEh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 ----LTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:TIGR04521 94 qlfeETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 165 DAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-210 |
1.37e-49 |
|
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: 163.34 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP-AKRGISMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMglglkqagtakeeiesrvakasgmlslepylarrpaELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 163 NLDaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:cd03230 125 GLD----PESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-225 |
1.60e-49 |
|
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: 164.95 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRgisMVFQSYALYPHLTVKDNMGL 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 99 GLKQA--GTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEI 176
Cdd:TIGR01184 78 AVDRVlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494968020 177 ARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL-YNRP 225
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-221 |
4.54e-49 |
|
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: 164.28 E-value: 4.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT-HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGI 77
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDNMGLG-LKQAGT--------AKEEIEsRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAI 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrLGRRSTwrslfglfPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 149 VREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHdQVE-AMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-212 |
5.80e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.03 E-value: 5.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGK--DVTVTPPAKRGIS-- 78
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 ----MVFQSYALYPHLTVKDNM-GLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:COG4161 82 qkvgMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 154 LFLFDEPLSNLDAALRVQtrleIARLHRSLKATMI---YVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:COG4161 162 VLLFDEPTAALDPEITAQ----VVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
6.16e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.47 E-value: 6.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGkdvtvTP--PAKRGISMVF 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT-----APlaEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGLKqaGTAKEEIEsRVAKASGmlsLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLK--GQWRDAAL-QALAAVG---LADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-216 |
8.61e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 8.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGK--DVTVTPPAK------ 74
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 RGISMVFQSYALYPHLTVKDNM-GLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 154 LFLFDEPLSNLDAALRVQtrleIARLHRSLKATMI---YVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQ----IVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-224 |
2.29e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 163.37 E-value: 2.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDvTVTP----PAKRGISMVFQSyalyPH---- 89
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEenlwEIRKKVGMVFQN----PDnqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 -LTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAL 168
Cdd:TIGR04520 92 gATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 169 RVQTRLEIARLHRSLKATMIYVTHDQVEAmTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:TIGR04520 172 RKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-209 |
3.02e-48 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 161.11 E-value: 3.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAG-LEDV--TSGTVLINGKDVTVTPPAKRGISM 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYPHLTVKDNMGLGLKqAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 160 PLSNLDAALRVQTR---LEIARlHRSLKATMiyVTHDqVEAMTLADKIVVMNA 209
Cdd:COG4136 160 PFSKLDAALRAQFRefvFEQIR-QRGIPALL--VTHD-EEDAPAAGRVLDLGN 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
1.70e-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: 159.91 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTH----DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV---TPPAK-- 74
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 -RGISMVFQSYALYPHLTVKDNMGLGLKQAGTAkeeiESRvAKASGMLS---LEPYLARRPAELSGGQRQRVAIGRAIVR 150
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRR----DAR-ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 151 EPELFLFDEPLSNLDAAlrvqTRLEIA----RLHRSLKATMIYVTHDQveamTLA---DKIVVMNAGAIEQ 214
Cdd:COG4181 164 EPAILFADEPTGNLDAA----TGEQIIdllfELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
2.69e-47 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 157.02 E-value: 2.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP--AKRGISMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 syalyphltvkdnmglglkqagtakeeiesrvakasgmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494968020 163 NLDAALRVQTRLEIARLHRSlKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-221 |
3.72e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 167.26 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKRG-IS 78
Cdd:COG1132 338 GEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrDLTLESLRRqIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYpHLTVKDNMGLGLKQAgtAKEEIEsRVAKASGMLS--------LEPYLARRPAELSGGQRQRVAIGRAIVR 150
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGRPDA--TDEEVE-EAAKAAQAHEfiealpdgYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 151 EPELFLFDEPLSNLDAA--LRVQTRLEIARLHRslkaTMIYVTH--DQVEAmtlADKIVVMNAGAIEQIGSPMEL 221
Cdd:COG1132 494 DPPILILDEATSALDTEteALIQEALERLMKGR----TTIVIAHrlSTIRN---ADRILVLDDGRIVEQGTHEEL 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
4.44e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 168.86 E-value: 4.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGTHD--VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGI 77
Cdd:COG2274 472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSyalyPHL---TVKDNMGLGLKQAGtaKEEIEsRVAKASGmlsLEPYLARRP-----------AELSGGQRQRVA 143
Cdd:COG2274 552 GVVLQD----VFLfsgTIRENITLGDPDAT--DEEII-EAARLAG---LHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 144 IGRAIVREPELFLFDEPLSNLDAAL--RVQTRLEiarlHRSLKATMIYVTHDqVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETeaIILENLR----RLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
...
gi 494968020 222 YNR 224
Cdd:COG2274 697 LAR 699
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
2.22e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.56 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVtppAKRGISMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPH--LTVKD--NMGL----GLKQAGTAKEeiESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREP 152
Cdd:COG1121 81 PQRAEVDWDfpITVRDvvLMGRygrrGLFRRPSRAD--REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 153 ELFLFDEPLSNLDAAlrvqTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:COG1121 159 DLLLLDEPFAGVDAA----TEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
2.37e-46 |
|
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: 156.44 E-value: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMV 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDN--MGLGLKQAGTAKEEIESrvakasgMLSLEPYLARR---PA-ELSGGQRQRVAIGRAIVREPEL 154
Cdd:cd03224 81 PEGRRIFPELTVEENllLGAYARRRAKRKARLER-------VYELFPRLKERrkqLAgTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 155 FLFDEPLSNLdAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03224 154 LLLDEPSEGL-APKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
2.81e-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: 159.45 E-value: 2.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD----VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED---VTSGTVLINGKDVTVTPPAK-- 74
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 ----RGISMVFQ-SY-ALYPHLTVKDNMGLGLKQAGTA-KEEIESRVAKASGMLSLEP---YLARRPAELSGGQRQRVAI 144
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIHGGLsKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 145 GRAIVREPELFLFDEPLSNLDAALRVQTrLE-IARLHRSLKATMIYVTHD--QVEAMtlADKIVVMNAGAIEQIGSPMEL 221
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQI-LNlLKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 494968020 222 YNRPA 226
Cdd:COG0444 239 FENPR 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-233 |
5.71e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 160.97 E-value: 5.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA------KRGISMVFQSYALYPHLTV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQT 172
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 173 RLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGF 233
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-226 |
1.02e-45 |
|
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: 155.29 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMV 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNM--------GLGLKQAGTAKEEIESRvAKASGMLS---LEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartGSGLLLARARREEREAR-ERAEELLErvgLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 150 REPELFLFDEPLSNLDAALRVqtrlEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETE----ELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-205 |
1.03e-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: 154.31 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDvtvTPPAKRG--------- 76
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE---TPPLNSKkaskfrrek 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494968020 157 FDEPLSNLDAalrvQTRLEIARLHRSLK---ATMIYVTHDQvEAMTLADKIV 205
Cdd:TIGR03608 158 ADEPTGSLDP----KNRDEVLDLLLELNdegKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-223 |
1.29e-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: 155.53 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT-HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGI 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDN--MG-LGLKQA-----GTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENvlHGrLGYKPTwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-193 |
2.15e-45 |
|
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: 153.94 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT-HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-----VTPPAKRGI 77
Cdd:TIGR02673 2 IEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 494968020 158 DEPLSNLDAALRVQTRLEIARLHRSlKATMIYVTHD 193
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHD 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
2.52e-45 |
|
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: 151.65 E-value: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVT--PPAKRGISMVFQSYALYPHLTVKDNM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 97 GLGLKQAGTAKEEIESRVAKASGMLSLEPYLARR----PAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-223 |
3.00e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.98 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVT----PPAKRGISMVFQ--SYALYPHLTV 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDnMGLGLKQAGTAKEEIESRVAKASGM--LSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRV 170
Cdd:PRK13637 103 KD-IAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 171 QTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-226 |
4.13e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 156.43 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 21 GIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGISMVFQ-SYA-LYPHLTVK 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 94 DNMGLGLKQAGTA-KEEIESRVAKASGMLSLEPYLARR-PAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQ 171
Cdd:COG4608 116 DIIAEPLRIHGLAsKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 172 --TRLEiaRLHRSLKATMIYVTHD--QVEAMtlADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:COG4608 196 vlNLLE--DLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-226 |
1.49e-44 |
|
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: 152.44 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMV 80
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLkQAGTAKEEIESRVAKasgMLSLEPYLARR---PA-ELSGGQRQRVAIGRAIVREPELFL 156
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGA-YARRDRAEVRADLER---VYELFPRLKERrrqRAgTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 157 FDEPLSNLdAALRVQtrlEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:COG0410 160 LDEPSLGL-APLIVE---EIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-224 |
1.71e-44 |
|
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: 159.92 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISM 79
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSyalyPHL---TVKDNMGLGLKQAGtaKEEIEsRVAKASGMLSLepyLARRP-----------AELSGGQRQRVAIG 145
Cdd:COG4988 416 VPQN----PYLfagTIRENLRLGRPDAS--DEELE-AALEAAGLDEF---VAALPdgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 146 RAIVREPELFLFDEPLSNLDAalrvQTRLEIARLHRSLKA--TMIYVTHDQvEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDA----ETEAEILQALRRLAKgrTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
.
gi 494968020 224 R 224
Cdd:COG4988 561 K 561
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
2.02e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.55 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTvTPPAKRGIsmVFQS 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERGV--VFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEiesRVAKASGMLS---LEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQ---RLEIAHQMLKkvgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-210 |
4.13e-44 |
|
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: 149.07 E-value: 4.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGT--HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKRG-ISM 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrDLDLESLRKnIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSYALYpHLTVKDNMglglkqagtakeeiesrvakasgmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 160 PLSNLDAALRVQTRLEIARLHRslKATMIYVTHDqVEAMTLADKIVVMNAG 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.65e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.29 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA------- 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 ---KRGISMVFQSYALYPHLTVKDNMGLG-LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:PRK11264 81 rqlRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 150 REPELFLFDEPLSNLDAALrVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPEL-VGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.79e-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: 147.58 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--ISMVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SyalyphltvkdnmglgLKQAGTAkeeiesrvakasgmlslepYLARRP-AELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:cd03214 81 A----------------LELLGLA-------------------HLADRPfNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
3.08e-43 |
|
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: 148.42 E-value: 3.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD--VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP-AKRGISMV 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGL--GLKqaGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 159 EPLSNLDAAlrvqTRLEIARLHRSLKA--TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03263 159 EPTSGLDPA----SRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-249 |
3.86e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.88 E-value: 3.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGTHD----VLKGIDLEVKDGEfvIF--VGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP-----A 73
Cdd:PRK11153 3 ELKNISKVFPQGGrtihALNNVSLHIPAGE--IFgvIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 KRGISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 154 LFLFDEPLSNLDAAlrvQTR--LE-IARLHRSLKATMIYVTH--DQVEAmtLADKIVVMNAGAIEQIGSPMELYNRPANV 228
Cdd:PRK11153 161 VLLCDEATSALDPA---TTRsiLElLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
250 260
....*....|....*....|.
gi 494968020 229 FVGGFIGSPQMNLIPAEKLEQ 249
Cdd:PRK11153 236 LTREFIQSTLHLDLPEDYLAR 256
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-193 |
8.07e-43 |
|
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: 147.17 E-value: 8.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGtHDV--LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-----VTPPAKRG 76
Cdd:cd03292 1 IEFINVTKTYP-NGTaaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494968020 157 FDEPLSNLDAAlrvqTRLEIARLHRSLK---ATMIYVTHD 193
Cdd:cd03292 160 ADEPTGNLDPD----TTWEIMNLLKKINkagTTVVVATHA 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-212 |
8.44e-42 |
|
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: 144.82 E-value: 8.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 7 KSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-PAKRGISMVFQSYA 85
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:cd03266 89 LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494968020 166 aALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03266 169 -VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-212 |
1.23e-41 |
|
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: 144.21 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 12 AYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPpakRGISMVFQSYAL---YP 88
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 89 hLTVKDNMGLGLKQA----GTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:cd03235 85 -ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 165 DaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03235 164 D----PKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
7.02e-41 |
|
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: 141.85 E-value: 7.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG-ISMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGL--GLKQAGTAKEEIESRVAKasgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:COG4133 83 ADGLKPELTVRENLRFwaALYGLRADREAIDEALEA----VGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 494968020 161 LSNLDAAlRVQTRLEIARLHRSLKATMIYVTHDQVEA 197
Cdd:COG4133 159 FTALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-212 |
1.49e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 141.72 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYG----THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--- 76
Cdd:TIGR02211 2 LKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ---ISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 154 LFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDqveaMTLA---DKIVVMNAGAI 212
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAkklDRVLEMKDGQL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-225 |
1.50e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.80 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---------- 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 -----KRGISMVFQSYALYPHLTVKDN-MGLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGR 146
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 147 AIVREPELFLFDEPLSNLDAALrVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
4.27e-40 |
|
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: 147.99 E-value: 4.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKRG-I 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrDLDEDDLRRrI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSyalyPHL---TVKDNMGLGLKQAGTakEEIEsRVAKASGmlsLEPYLARRP-----------AELSGGQRQRVA 143
Cdd:COG4987 412 AVVPQR----PHLfdtTLRENLRLARPDATD--EELW-AALERVG---LGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 144 IGRAIVREPELFLFDEPLSNLDAAlrvqTRLEI-ARLHRSLK-ATMIYVTHDQVeAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAA----TEQALlADLLEALAgRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
....*
gi 494968020 222 YNRPA 226
Cdd:COG4987 557 LAQNG 561
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-207 |
6.56e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 143.62 E-value: 6.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGISMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLG--LKQAGTA-KEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGrePRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 158 DEPLSNLDAAlrvqtrlEIARLH---RSLKA---TMIYVTHDQVEAMTLADKIVVM 207
Cdd:COG1129 165 DEPTASLTER-------EVERLFriiRRLKAqgvAIIYISHRLDEVFEIADRVTVL 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-225 |
1.50e-38 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 143.29 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 10 RKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDvTSGTVLINGKDVTVTP-----PAKRGISMVFQS- 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YA-LYPHLTVKDNM--GLGLKQAGTAKEEIESRVAKASGMLSLEP-YLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:COG4172 372 FGsLSPRMTVGQIIaeGLRVHGPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 160 PLSNLDAALRVQTrLEI-ARLHRSLKATMIYVTHDQ--VEAMtlADKIVVMNAGAI-EQiGSPMELYNRP 225
Cdd:COG4172 452 PTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGKVvEQ-GPTEQVFDAP 517
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-212 |
3.04e-38 |
|
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: 135.73 E-value: 3.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMV 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPherARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVakasgmLSLEPYL----ARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI------YELFPVLkemlGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 157 FDEPLSNLDAALrVQtrlEIARLHRSLKA----TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:TIGR03410 155 LDEPTEGIQPSI-IK---DIGRVIRRLRAeggmAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-226 |
3.40e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 138.85 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 33 IFvGPSGCGKSTLLRSIAGLEDVTSGTVLING-------KDVTVtPPAKRGISMVFQSYALYPHLTVKDNMGLGLKQagT 105
Cdd:PRK11144 29 IF-GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICL-PPEKRRIGYVFQDARLFPHYKVRGNLRYGMAK--S 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 106 AKEEIESRVakasGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALR--VQTRLEiaRLHRSL 183
Cdd:PRK11144 105 MVAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKreLLPYLE--RLAREI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494968020 184 KATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-224 |
3.73e-38 |
|
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: 135.82 E-value: 3.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTH-DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-VTPPA-KRGISMV 80
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIReVTLDSlRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYpHLTVKDNMGLGLKQAGtaKEEIEsRVAKASGM----LSL-EPY---LARRPAELSGGQRQRVAIGRAIVREP 152
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRPDAT--DEEVI-EAAKAAQIhdkiMRFpDGYdtiVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 153 ELFLFDEPLSNLDaalrVQTRLEIARLHRSLKA--TMIYVTHDQVEAMTlADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:cd03253 157 PILLLDEATSALD----THTEREIQAALRDVSKgrTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-221 |
6.69e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.60 E-value: 6.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRgISMVF 81
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelAKR-LAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGL----KqaGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 158 DEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-222 |
9.17e-38 |
|
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: 134.59 E-value: 9.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGT---HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKRG-ISMV 80
Cdd:cd03249 3 FKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSqIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPhLTVKDNMGLGLKQAgTAKEEIE-SRVAKASGMLSLEPY-----LARRPAELSGGQRQRVAIGRAIVREPEL 154
Cdd:cd03249 83 SQEPVLFD-GTIAENIRYGKPDA-TDEEVEEaAKKANIHDFIMSLPDgydtlVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 155 FLFDEPLSNLDAA--LRVQTRLEIARLHRslkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELY 222
Cdd:cd03249 161 LLLDEATSALDAEseKLVQEALDRAMKGR----TTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
1.02e-37 |
|
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: 133.88 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRGISMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGLKQAGTAKEEIEsrvaKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494968020 164 LDAalrvQTRLEIARLHRSLKATMIYV---THDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03268 157 LDP----DGIKELRELILSLRDQGITVlisSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.29e-37 |
|
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: 134.03 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-PAKRGISMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 163 NLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
1.88e-37 |
|
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: 131.40 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGISMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQsyalyphltvkdnmglglkqagtakeeiesrvakasgmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 161 LSNLDAAlrvqtrlEIARLH---RSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03216 110 TAALTPA-------EVERLFkviRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-224 |
2.10e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 134.86 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 15 THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP--PAKRGISMVFQSyalyPH--- 89
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRHKIGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 --LTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAa 167
Cdd:PRK13650 95 vgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 168 lrvQTRLEIARLHRSLKA----TMIYVTHDqVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:PRK13650 174 ---EGRLELIKTIKGIRDdyqmTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-222 |
2.37e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP--PAKRGISMVFQSyalyPH-----LT 91
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwDVRRQVGMVFQN----PDnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQ 171
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 172 TRLEIARLHRSLKATMIYVTHDQVEAMTlADKIVVMNAGAIEQIGSPMELY 222
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-227 |
6.57e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 132.85 E-value: 6.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 13 YGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV-----TSGTVLINGKDV---TVTPPA-KRGISMVFQS 83
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIydpDVDVVElRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHlTVKDNMGLGLKQAG-TAKEEIESRVAKAsgmlslepyLAR------------RPA-ELSGGQRQRVAIGRAIV 149
Cdd:COG1117 101 PNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVEES---------LRKaalwdevkdrlkKSAlGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 150 REPELFLFDEPLSNLD--AALRvqtrleIARLHRSLKA--TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:COG1117 171 VEPEVLLMDEPTSALDpiSTAK------IEELILELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
..
gi 494968020 226 AN 227
Cdd:COG1117 245 KD 246
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
7.80e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 132.66 E-value: 7.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVT-----SGTVLINGKDV---TVTP- 71
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspDVDPi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 72 PAKRGISMVFQSYALYPHLTVKDNMGLGLKQAGTA--KEEIESRV----AKASGMLSLEPYLARRPAELSGGQRQRVAIG 145
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVksKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 146 RAIVREPELFLFDEPLSNLDAalrVQTRlEIARLHRSLKA--TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDP---VGTA-KIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
....
gi 494968020 224 RPAN 227
Cdd:PRK14267 238 NPEH 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-212 |
7.80e-37 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 131.23 E-value: 7.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRgISMVFQS--YALYPHlTVKD 94
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS-IGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLGLKQAGTAKEEIESRVAKasgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVqtrl 174
Cdd:cd03226 92 ELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME---- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494968020 175 EIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03226 164 RVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-268 |
9.06e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 9.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLI------NGKDVTVTPPAKRGISMVFQ--SYALYPHl 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 TVKDNMGLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAalr 169
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 170 vQTRLEI----ARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANvfvggfIGSPQMNLIPAE 245
Cdd:PRK13634 179 -KGRKEMmemfYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE------LEAIGLDLPETV 251
|
250 260
....*....|....*....|...
gi 494968020 246 KLEQGGAKTIGIRPEHITLSREQ 268
Cdd:PRK13634 252 KFKRALEEKFGISFPKPCLTLEE 274
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
7.40e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVT--PPAKRGISMVFQSyalyPH-----L 90
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlKEIRKKIGIIFQN----PDnqfigA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 TVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRV 170
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 171 QTRLEIARLHRSLKATMIYVTHDQVEAmTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-210 |
7.61e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 135.54 E-value: 7.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGISMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAG-------TAKEEIEsRVAKASGmLSLEPYlaRRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKggrldrkAARARIR-ELSERYG-LDVDPD--AKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 154 LFLFDEPLSNLdaalrvqTRLEIARLHRSLKA------TMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:COG3845 162 ILILDEPTAVL-------TPQEADELFEILRRlaaegkSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
8.78e-36 |
|
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: 128.85 E-value: 8.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIfVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG-ISMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVK---DNMGLgLKqaGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:cd03264 80 EFGVYPNFTVReflDYIAW-LK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 160 PLSNLDAALRVQTRLEIARLhrSLKATMIYVTH--DQVEAMtlADKIVVMNAGAIEQIG 216
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL--GEDRIVILSTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-212 |
1.09e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHD---------VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 72 PA-----KRGISMVFQSY--ALYPHLTVKDNMGLGLKQAGTAKEEieSRVAKASGML---SLEPYLA-RRPAELSGGQRQ 140
Cdd:PRK10419 81 RAqrkafRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDKA--ERLARASEMLravDLDDSVLdKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 141 RVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
1.26e-35 |
|
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: 128.48 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGI 77
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSyalyPHL---TVKDNMGLGlkqAGTAKEEiesRVAKASGMLSLEPYLARRP-----------AELSGGQRQRVA 143
Cdd:cd03245 81 GYVPQD----VTLfygTLRDNITLG---APLADDE---RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 144 IGRAIVREPELFLFDEPLSNLDaaLRVQTRLeIARLHRSLKA-TMIYVTHDQVeAMTLADKIVVMNAGAI 212
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMD--MNSEERL-KERLRQLLGDkTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-226 |
3.32e-35 |
|
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: 127.66 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR---GISMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 161 LSNLDaALRVQtrlEIARLHRSLKATMIYV---THDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:cd03218 161 FAGVD-PIAVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-215 |
4.23e-35 |
|
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: 128.77 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAygthdVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA-----KRG 76
Cdd:TIGR02769 15 GGLFGAKQRAP-----VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafRRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQ-SY-ALYPHLTVKDNMGLGLKQAGTAKE-EIESRVAKASGMLSLEPYLARR-PAELSGGQRQRVAIGRAIVREP 152
Cdd:TIGR02769 90 VQLVFQdSPsAVNPRMTVRQIIGEPLRHLTSLDEsEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 153 ELFLFDEPLSNLDAALRVQtrleIARLHRSLKA----TMIYVTHDQVEAMTLADKIVVMNAGAI-EQI 215
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAV----ILELLRKLQQafgtAYLFITHDLRLVQSFCQRVAVMDKGQIvEEC 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
8.64e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 127.34 E-value: 8.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL-----EDVTSGTVLINGKDVTVTPPA-- 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 KRGISMVFQSYALYPHLTVKDNMGLGLK--QAGTAKEEIESRVAKASGMLSLEPYLARR---PA-ELSGGQRQRVAIGRA 147
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 148 IVREPELFLFDEPLSNLDAalrvQTRLEIARLHRSLKATM--IYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDP----ENTAKIESLFLELKKDMtiVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-255 |
1.53e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 128.67 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 20 KGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR-----GISMVFQS--YALYPHLTV 92
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLGLK--QAGTAKEEIESRVAKASGMLSLEPYLARR-PAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALR 169
Cdd:PRK15079 118 GEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 170 VQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGFIGS-PqmnlIPAEKLE 248
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAvP----IPDPDLE 273
|
....*..
gi 494968020 249 QGgaKTI 255
Cdd:PRK15079 274 RN--KTI 278
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-210 |
3.27e-34 |
|
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: 124.70 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-------PAKRG 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ismvfqsyaLYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:cd03269 81 ---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 157 FDEPLSNLDAALRVQTRLEIARLHRSLKaTMIYVTH--DQVEAMtlADKIVVMNAG 210
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHqmELVEEL--CDRVLLLNKG 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
3.47e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.53 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGI 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEpYLARRPA-ELSGGQRQRVAIGRAIVREPELFL 156
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGIT-HLRKSKAySLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 157 FDEPLSNLD--AAlrvqtrLEIARLHRSLKATMIYV--T-HDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:COG1137 160 LDEPFAGVDpiAV------ADIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-222 |
3.99e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 125.04 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPA-KRGISMVFQSYALYpHLTVKDN 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASlRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGLKQAGtaKEEIEsRVAKASGMLS--------LEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD-- 165
Cdd:cd03251 96 IAYGRPGAT--REEVE-EAARAANAHEfimelpegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDte 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 166 AALRVQTRLEIARLHRslkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELY 222
Cdd:cd03251 173 SERLVQAALERLMKNR----TTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
6.74e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.20 E-value: 6.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY--GTHD---VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG-- 76
Cdd:COG1101 2 LELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYAL--YPHLTVKDNMGL--------GLKQAGTAK--EEIESRVAKASgmLSLEPYLARRPAELSGGQRQRVAI 144
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLALayrrgkrrGLRRGLTKKrrELFRELLATLG--LGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 145 GRAIVREPELFLFDEPLSNLD--AALRVqtrLEI-ARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDpkTAALV---LELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-221 |
7.67e-34 |
|
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: 124.26 E-value: 7.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 14 GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKR-GISMVFQSYALYPHlT 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRsMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMGLGlkqAGTAKEEIESRVAKASGMLS--------LEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03254 93 IMENIRLG---RPNATDEEVIEAAKEAGAHDfimklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 164 LD--AALRVQTRLEIARLHRslkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:cd03254 170 IDteTEKLIQEALEKLMKGR----TSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
1.19e-33 |
|
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: 129.71 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 14 GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISMVFQSYALYPHlT 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMGLGLKQAgtAKEEIEsRVAKASGMLSLEPYL--------ARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:TIGR02857 412 IAENIRLARPDA--SDAEIR-EALERAGLDEFVAALpqgldtpiGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494968020 164 LDAALRVQTRLEIARLHRSlkATMIYVTHDqVEAMTLADKIVVM 207
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-212 |
4.53e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.07 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-------R 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 76 GismvfqsyaLYPHLTVKDNM-------GLGLKQagtAKEEIESRVAKasgmLSLEPYLARRPAELSGGQRQRVAIGRAI 148
Cdd:COG4152 81 G---------LYPKMKVGEQLvylarlkGLSKAE---AKRRADEWLER----LGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 149 VREPELFLFDEPLSNLDAalrVQTRLeIARLHRSLKA---TMIYVTH--DQVEAmtLADKIVVMNAGAI 212
Cdd:COG4152 145 LHDPELLILDEPFSGLDP---VNVEL-LKDVIRELAAkgtTVIFSSHqmELVEE--LCDRIVIINKGRK 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-212 |
6.98e-33 |
|
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: 128.83 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGI 77
Cdd:TIGR03375 462 GEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYpHLTVKDNMGLGlkqAGTAKEEIESRVAKASGMLS--------LEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:TIGR03375 542 GYVPQDPRLF-YGTLRDNIALG---APYADDEEILRAAELAGVTEfvrrhpdgLDMQIGERGRSLSGGQRQAVALARALL 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 150 REPELFLFDEPLSNLDAalRVQTRLeIARLHRSLKA-TMIYVTHdQVEAMTLADKIVVMNAGAI 212
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDN--RSEERF-KDRLKRWLAGkTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
6.13e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 6.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 12 AYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVlingkdvtvTPPAKRGISMVFQSYAL---YP 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 89 hLTVKDNMGLGLKQ----AGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:NF040873 72 -LTVRDLVAMGRWArrglWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494968020 165 DAALRVQTRLEIARLHRSlKATMIYVTHDqVEAMTLADKIVVM 207
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-193 |
1.35e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.05 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-----VTPPAKRGI 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 494968020 158 DEPLSNLDAALRVqtrlEIARLHRSLK---ATMIYVTHD 193
Cdd:PRK10908 162 DEPTGNLDDALSE----GILRLFEEFNrvgVTVLMATHD 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-225 |
1.44e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.84 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA-----KRGISMVFQS-YA-LYPHLT 91
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMG--LGLKQAGTAKEeiesRVAKASGMLS---LEP-YLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:PRK11308 111 VGQILEepLLINTSLSAAE----RREKALAMMAkvgLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 166 AALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-227 |
3.77e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.57 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV-----TSGTVLINGKDV----TVTPPAK 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysprTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 RGISMVFQSYALYPhLTVKDNMGLGLKQAGTAKEEI-----ESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVldeavEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 150 REPELFLFDEPLSNLD--AALRVQTRLeiarLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:PRK14239 165 TSPKIILLDEPTSALDpiSAGKIEETL----LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-212 |
6.05e-31 |
|
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: 115.01 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--ISMVFQSYA 85
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYphltvkdnmglglkqAGTAKEEIesrvakasgmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:cd03246 87 LF---------------SGSIAENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 166 ----AALRVQtrleIARLhRSLKATMIYVTHdQVEAMTLADKIVVMNAGAI 212
Cdd:cd03246 129 vegeRALNQA----IAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-222 |
9.42e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.50 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP--PAKRGISMVFQSY-ALYPHLTVKDN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494968020 176 IARLHRSLKATMIYVTHDQVEAMTlADKIVVMNAGAIEQIGSPMELY 222
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
1.06e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.75 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA----KRGism 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VF-QSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAI--VREPE--- 153
Cdd:COG4559 79 VLpQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdgg 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 154 ---LFLfDEPLSNLDAALRVQTrLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSP 218
Cdd:COG4559 159 prwLFL-DEPTSALDLAHQHAV-LRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-212 |
1.65e-30 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 114.07 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 15 THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGISMV---FQSYALYP 88
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 89 HLTVKDNMGLglkqagtakeeiesrvakasgmlslepylarrPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDaal 168
Cdd:cd03215 92 DLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD--- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494968020 169 rVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03215 137 -VGAKAEIYRLIRELADagkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-193 |
2.29e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 115.30 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAK-----RGISMVFQSYALYPHL 90
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKaelrnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 TVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRV 170
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|...
gi 494968020 171 QTRLEIARLHRSLKATMIYVTHD 193
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHD 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-221 |
4.41e-30 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 114.78 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED--VTSGTVLINGKDVTVTPP---AKRGISMVFQSYALYPHLT 91
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPderARAGIFLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNmglgLKQAGTAKEEIES-------RVAKASGMLSLEPYLARRP--AELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:COG0396 94 VSNF----LRTALNARRGEELsareflkLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 163 NLDA-ALRVQTRLeIARLHRSlKATMIYVTH-----DQVEamtlADKIVVMNAGAIEQIGSPmEL 221
Cdd:COG0396 170 GLDIdALRIVAEG-VNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-231 |
4.74e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.47 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV---TVTPPAKRGISMVFQS-YALYPHLTVKD 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRL 174
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 175 EIARLHRSLKaTMIYVTHDqVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVG 231
Cdd:PRK13644 178 RIKKLHEKGK-TIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
5.03e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.17 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY--GThDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP----AKRGI 77
Cdd:PRK13639 2 LETRDLKYSYpdGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKslleVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQS-----YAlyPhlTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREP 152
Cdd:PRK13639 81 GIVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 153 ELFLFDEPLSNLDAalrvQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK13639 157 EIIVLDEPTSGLDP----MGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-210 |
8.62e-30 |
|
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: 112.26 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV--TSGTVLINGKDVTVTPPAKRgISMVFQSYALYPHLTVKD 94
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLglkqagtakeeiesrVAKASGmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSNLD---AALRVQ 171
Cdd:cd03213 102 TLMF---------------AAKLRG--------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494968020 172 TRLEIARLHRslkaTMIYVTHD-QVEAMTLADKIVVMNAG 210
Cdd:cd03213 153 LLRRLADTGR----TIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
1.01e-29 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 118.75 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD--VLK---GIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKD--VTVTPP---- 72
Cdd:TIGR03269 280 IKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 73 ---AKRGISMVFQSYALYPHLTVKDNM----GLGL-KQAGTAKEEIesrVAKASGMLS--LEPYLARRPAELSGGQRQRV 142
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVLDNLteaiGLELpDELARMKAVI---TLKMVGFDEekAEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 143 AIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-225 |
1.06e-29 |
|
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: 119.29 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV--TPPAKRGISMVFQSYALYPHlTVKDN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQAVRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 M----GLGLKQAGTAkeeiesrvAKASGM--------LSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:TIGR03797 547 IaggaPLTLDEAWEA--------ARMAGLaedirampMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 164 LDAalRVQtRLEIARLHRsLKATMIYVTHDQVEAMTlADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:TIGR03797 619 LDN--RTQ-AIVSESLER-LKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-215 |
1.11e-29 |
|
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: 113.64 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSG-TVLINGKD---VTVTPPAKR-GI- 77
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWELRKRiGLv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYaLYPHLTVKD--------NMGLGLKqagtAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:COG1119 84 SPALQLR-FPRDETVLDvvlsgffdSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHdQVE--------AMTLAD-KIVVmnAGAIEQI 215
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH-HVEeippgithVLLLKDgRVVA--AGPKEEV 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-233 |
1.51e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.06 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY----GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPA----- 73
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVaTLDADAlaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 KRGISMVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 154 LFLFDEPLSNLDAALRVQTrleIARLH--RSLKATMIYVTHD-QVEAMtlADKIVVMNAGAI----------EQIGSPME 220
Cdd:PRK10535 165 VILADEPTGALDSHSGEEV---MAILHqlRDRGHTVIIVTHDpQVAAQ--AERVIEIRDGEIvrnppaqekvNVAGGTEP 239
|
250
....*....|....*
gi 494968020 221 LYNRPANV--FVGGF 233
Cdd:PRK10535 240 VVNTASGWrqFVSGF 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-226 |
1.83e-29 |
|
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: 117.86 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL----EDVTSGTVLINGKDVTVTPPAK----RG--I 77
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERElrriRGnrI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQ--SYALYPHLTVKDNMGLGLK-QAGTAKEEIESRVAKasgMLSL----EPylARR----PAELSGGQRQRVAIGR 146
Cdd:COG4172 95 AMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALE---LLERvgipDP--ERRldayPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 147 AIVREPELFLFDEPLSNLDAALRVQTrLE-IARLHRSLKATMIYVTHDQ--VEAMtlADKIVVMNAGAIEQIGSPMELYN 223
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQI-LDlLKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGEIVEQGPTAELFA 246
|
...
gi 494968020 224 RPA 226
Cdd:COG4172 247 APQ 249
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-224 |
2.23e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 112.58 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISMVFQSYALYpHLTVKD 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLGlkQAGTAKEEIE--SRVAKASGMLSLEP-----YLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAA 167
Cdd:cd03252 95 NIALA--DPGMSMERVIeaAKLAGAHDFISELPegydtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 168 lrvQTRLEIARLHRSLKA-TMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:cd03252 173 ---SEHAIMRNMHDICAGrTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-211 |
3.75e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.73 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISMVF 81
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHlTVKDNMGLGLKQAGTAKEeiESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 161 LSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEaMTLADKIVVMNAGA 211
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHA 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-264 |
4.87e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLING---KDVTVTPPAKRGISMVFQSyalyPH----- 89
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALR 169
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 170 VQTRLEIARLHRSLKATMIYVTHDQVEAMTlADKIVVMNAGAIEQIGSPMELYnrpANVFVGGFIG--SPQMNLIpAEKL 247
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF---KEVEMMKKIGldVPQVTEL-AYEL 255
|
250
....*....|....*..
gi 494968020 248 EQGGaktIGIRPEHITL 264
Cdd:PRK13633 256 KKEG---VDIPSDILTI 269
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
8-221 |
6.50e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.68 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--ISMVFQSYA 85
Cdd:TIGR01842 323 TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHlTVKDNMGLgLKQAGTAKEEIESrvAKASG----MLSL----EPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:TIGR01842 403 LFPG-TVAENIAR-FGENADPEKIIEA--AKLAGvhelILRLpdgyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 158 DEPLSNLDAALRVQTRLEIARLhRSLKATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-225 |
7.62e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 112.17 E-value: 7.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 14 GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-----PAKRGISMVFQSYALYP 88
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlyTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 89 HLTVKDNMGLGLKQAGTAKEEIesrvAKASGMLSLEPYLAR-----RPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPL----LHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 164 LDA-ALRVQTRLeIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK11831 174 QDPiTMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-259 |
7.74e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP------PAKRGISMVFQ--SYALYPHLTVK 93
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQfpESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 94 DnMGLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQT 172
Cdd:PRK13643 105 D-VAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 173 RLEIARLHRSlKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRpANVFVGGFIGSPQMNLIpAEKLEQGGA 252
Cdd:PRK13643 184 MQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-VDFLKAHELGVPKATHF-ADQLQKTGA 260
|
....*..
gi 494968020 253 KTIGIRP 259
Cdd:PRK13643 261 VTFEKLP 267
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-193 |
1.29e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 110.25 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG------ISMVFQSYALYPHLT 91
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAalrvQ 171
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR----Q 180
|
170 180
....*....|....*....|....*.
gi 494968020 172 TRLEIA----RLHRSLKATMIYVTHD 193
Cdd:PRK10584 181 TGDKIAdllfSLNREHGTTLILVTHD 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-210 |
1.48e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 109.48 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 15 THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGkdvtvtppakrGISMVFQSyalyPHL---T 91
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE----PWIqngT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMGLGlkqagtaKEEIESR---VAKASgmlSLEPYLARRPA-------E----LSGGQRQRVAIGRAIVREPELFLF 157
Cdd:cd03250 82 IRENILFG-------KPFDEERyekVIKAC---ALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 158 DEPLSNLDAalrvQTRLEIARL----HRSLKATMIYVTHdQVEAMTLADKIVVMNAG 210
Cdd:cd03250 152 DDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-220 |
1.59e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGISMV 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYAL-YPhLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVR------EPE 153
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 154 LFLFDEPLSNLDaaLRVQ-TRLEIAR-LHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPME 220
Cdd:PRK13548 161 WLLLDEPTSALD--LAHQhHVLRLARqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
2.44e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 14 GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVT--PPAKRGISMVFQS---YALYP 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEniREVRKFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 89 hlTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAL 168
Cdd:PRK13652 95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 169 RVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-216 |
2.60e-28 |
|
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: 114.85 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--ISMVFQSYALYPHlTVKDN 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 ---MGlglkqAGTAKEEIEsrVAKASGM----LSL----EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:COG4618 426 iarFG-----DADPEKVVA--AAKLAGVhemiLRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 165 D----AALrVQTrleIARLhRSLKATMIYVTHDQvEAMTLADKIVVMNAGAIEQIG 216
Cdd:COG4618 499 DdegeAAL-AAA---IRAL-KARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-229 |
3.43e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.26 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 13 YGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV-----TSGTVLINGKDV---TVTPPA-KRGISMVFQS 83
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyapDVDPVEvRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHlTVKDNMGLGLK---QAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARingYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 161 LSNLDAAlrvqTRLEIARLHRSLKA--TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL--YNRPANVF 229
Cdd:PRK14243 179 CSALDPI----STLRIEELMHELKEqyTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLveFDRTEKIF 247
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-221 |
4.83e-28 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 114.45 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYG--THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGI 77
Cdd:TIGR01846 454 GAITFENIRFRYApdSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHlTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPY-----LARRPAELSGGQRQRVAIGRAIVREP 152
Cdd:TIGR01846 534 GVVLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQgynteVGEKGANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 153 ELFLFDEPLSNLDAalrvQTRLEIARLHRSLKA--TMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:TIGR01846 613 RILIFDEATSALDY----ESEALIMRNMREICRgrTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
6.85e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP--AKRGIS 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLG----LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPEL 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 155 FLFDEPLSNLDAALRVQTrLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK09536 161 LLLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-227 |
1.48e-27 |
|
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: 107.45 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 21 GIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED----VTSGTVLINGKDVTVTPPAKRGISMVFQS--YALYPHLTVKD 94
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLGLKQAGTAKEEIESRVA---KASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQ 171
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILealEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 172 TrLEIARLHRSLKAT-MIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:TIGR02770 164 V-LKLLRELRQLFGTgILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
2.00e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINgKDVTvtppakrgISMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR--------IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHLTVKDN--MGLG-LKQAGTAKEEIESRV--------------------------AKASGMLS----LEPYLARRPA 132
Cdd:COG0488 72 LDDDLTVLDTvlDGDAeLRALEAELEELEAKLaepdedlerlaelqeefealggweaeARAEEILSglgfPEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 133 ELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDaalrvqtrLE-IARLHRSLKA---TMIYVTHD 193
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsIEWLEEFLKNypgTVLVVSHD 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-223 |
3.93e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.79 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLI-------NGKDVTVTPPAKRGISMVFQ--SYALYPH 89
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipaNLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 lTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAL 168
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 169 RVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
6.36e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.86 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKD----------------VTVTPPAKRGIS--- 78
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvlekLVIQKTRFKKIKkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 -------MVFQ--SYALYPHLTVKDNMgLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAI 148
Cdd:PRK13651 102 eirrrvgVVFQfaEYQLFEQTIEKDII-FGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 149 VREPELFLFDEPLSNLDAAlRVQTRLEI-ARLHRSLKaTMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQ-GVKEILEIfDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-227 |
1.11e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.89 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVtSGTVLINGK-----------DVTVTP 71
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRveffnqniyerRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 72 pAKRGISMVFQSYALYPhLTVKDNMGLGLKQAG-TAKEEI----ESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGR 146
Cdd:PRK14258 86 -LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIddivESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 147 AIVREPELFLFDEPLSNLD--AALRVQTRLEIARLHRSLkaTMIYVTHDQVEAMTLADKIVVMNA-----GAIEQIGSPM 219
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
....*...
gi 494968020 220 ELYNRPAN 227
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-220 |
2.02e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGISMV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLG----LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 157 FDEPLSNLDAALRVqtrlEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPME 220
Cdd:PRK11231 162 LDEPTTYLDINHQV----ELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
2.47e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL----------EDVTSGTVLINGKDVTVTPPAK--------RGISM 79
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQ--SYALYPHLTVKDNMgLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIM-FGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 157 FDEPLSNLDAAlrvqTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:PRK13631 200 FDEPTAGLDPK----GEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-224 |
2.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP------PAKRGISMVFQsyalYPHL-- 90
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 ---TVKDNMGLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDA 166
Cdd:PRK13649 99 feeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 167 ALRVQTRLEIARLHRSlKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:PRK13649 179 KGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-221 |
3.98e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 108.75 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-VTPPAKRG-ISMVFQSYALYpHLTVKDN 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdVTQASLRAaIGIVPQDTVLF-NDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGlkQAGTAKEEIEsRVAKASgmlSLEPYLARRPA-----------ELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:COG5265 452 IAYG--RPDASEEEVE-AAARAA---QIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 165 D--------AALRV----QTRLEIArlHR-SlkaTmiyVTHdqveamtlADKIVVMNAGAI-EQiGSPMEL 221
Cdd:COG5265 526 DsrteraiqAALREvargRTTLVIA--HRlS---T---IVD--------ADEILVLEAGRIvER-GTHAEL 579
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-227 |
4.85e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 4.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 9 IRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKST----LLRSIAgledvTSGTVLINGKDV-TVTP----PAKRGISM 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhNLNRrqllPVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQ--SYALYPHLTVKDNMGLGLK--QAGTAKEEIESRVAKASGMLSLEPYLARR-PAELSGGQRQRVAIGRAIVREPEL 154
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 155 FLFDEPLSNLDAALRVQtrleIARLHRSLKAT----MIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQ----ILALLKSLQQKhqlaYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-212 |
5.05e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.21 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR---GISMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEpylaRRPAELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLD----SSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 161 LSNLdaalrvqTRLEIARLHRSLKAT------MIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK15439 168 TASL-------TPAETERLFSRIRELlaqgvgIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-211 |
5.43e-26 |
|
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: 103.28 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGK----DVTVTPPA------KRGISMVFQSYALY 87
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilalrRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 88 PHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLAR-RPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDA 166
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494968020 167 AlrvqTRLEIARLHRSLKA---TMIYVTHDQvEAM-TLADKIVVMNAGA 211
Cdd:COG4778 186 A----NRAVVVELIEEAKArgtAIIGIFHDE-EVReAVADRVVDVTPFS 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-212 |
5.73e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 103.57 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSI-RKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDvtvtpPAKRG------IS 78
Cdd:cd03267 23 LKSLfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRkkflrrIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVF-QSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:cd03267 98 VVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 158 DEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-225 |
8.43e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL---EDVTSGTVLINGKDVTVTP--PAKRGISMVFQSyalyPH--- 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTvwDIREKVGIVFQN----PDnqf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 --LTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAA 167
Cdd:PRK13640 98 vgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 168 LRVQTRLEIARLHRSLKATMIYVTHDQVEAmTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-223 |
8.86e-26 |
|
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: 102.62 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 24 LEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDvtvTPPAKRGISMVFQSYAL---YP----HLTVKDNM 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHEFawdFPisvaHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 97 GL--GLKQAGTAKEEIESRVAKASGMlslePYLARRP-AELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDaalrVQTR 173
Cdd:TIGR03771 78 GHigWLRRPCVADFAAVRDALRRVGL----TELADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD----MPTQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 174 LEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNaGAIEQIGSPMELYN 223
Cdd:TIGR03771 150 ELLTELFIELAGagtAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-224 |
1.12e-25 |
|
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: 101.83 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED--VTSGTVLINGKDVTVTPP---AKRGISMVFQSYALYPHLTV 92
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KD-----NMGlglkqagtakeeiesrvakasgmlslepylarrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSNLDA- 166
Cdd:cd03217 95 ADflryvNEG------------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDId 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 167 ALRVQTRlEIARLhRSLKATMIYVTH-----DQVEamtlADKIVVMNAGAIEQIGsPMELYNR 224
Cdd:cd03217 139 ALRLVAE-VINKL-REEGKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-221 |
1.15e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.12 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKRGISMVFQ 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 163 NLDAalrvQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK13537 168 GLDP----QARHLMWERLRSLLArgkTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-224 |
1.78e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 14 GTHdVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV-TPPAKRG-ISMVFQSyalyPH-- 89
Cdd:PRK13647 17 GTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAeNEKWVRSkVGLVFQD----PDdq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 ---LTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDA 166
Cdd:PRK13647 92 vfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 167 ALRVQTRLEIARLHRSLKaTMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:PRK13647 172 RGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-193 |
2.03e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 106.29 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISM 79
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQSyalyPHL---TVKDNMGLGlkqAGTAKEEIESRVAKASGmlsLEPYLARRP-----------AELSGGQRQRVAIG 145
Cdd:TIGR02868 414 CAQD----AHLfdtTVRENLRLA---RPDATDEELWAALERVG---LADWLRALPdgldtvlgeggARLSGGERQRLALA 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494968020 146 RAIVREPELFLFDEPLSNLDAAlrvqTRLEIarLHRSLKA----TMIYVTHD 193
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAE----TADEL--LEDLLAAlsgrTVVLITHH 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
2.24e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.52 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVT--PPAKRGISMVFQSyalyPH-----LT 91
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfEKLRKHIGIVFQN----PDnqfvgSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAalrvQ 171
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP----D 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 172 TRLEIARLHRSLKA----TMIYVTHDQVEAMTlADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK13648 177 ARQNLLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-232 |
2.25e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.88 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK---RGISMV 80
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGLKQAgtAKEEIESRVAKASGML-SLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 160 PLSNLDAALRVQTRLEIARLhRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI--EQIGSPMELYNRPANVFVGG 232
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDALLANEAVRSAYLGG 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
3.09e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.06 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGI 77
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHlTVKDNMGLGLKQAGTAK-EEIESRV---AKASGMLSLEPYLAR--RPaeLSGGQRQRVAIGRAIVRE 151
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPNASDEAlIEVLQQVgleKLLEDDKGLNAWLGEggRQ--LSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 152 PELFLFDEPLSNLDAalrvQTRLEIARLHRSLKA--TMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK11160 494 APLLLLDEPTEGLDA----ETERQILELLAEHAQnkTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-225 |
4.83e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 105.80 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGTHD--VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGI 77
Cdd:TIGR03796 476 GYVELRNITFGYSPLEppLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlANSV 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHlTVKDNMGL--------GLKQAgtAKE-EIESRVAKASGmlSLEPYLARRPAELSGGQRQRVAIGRAI 148
Cdd:TIGR03796 556 AMVDQDIFLFEG-TVRDNLTLwdptipdaDLVRA--CKDaAIHDVITSRPG--GYDAELAEGGANLSGGQRQRLEIARAL 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 149 VREPELFLFDEPLSNLDAAlrvqTRLEIARLHRSLKATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:TIGR03796 631 VRNPSILILDEATSALDPE----TEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-220 |
6.49e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtVTPPAkrGISMVFQsya 85
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSALL--ELGAGFH--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 lyPHLTVKDNMGLGLKQAGTAKEEIESRVAKA---SGmlsLEPYLaRRPAE-LSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:COG1134 101 --PELTGRENIYLNGRLLGLSRKEIDEKFDEIvefAE---LGDFI-DQPVKtYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 162 SNLDAALR--VQTRLEiARLHRSlkATMIYVTHD--QVEamTLADKIVVMNAGAIEQIGSPME 220
Cdd:COG1134 175 AVGDAAFQkkCLARIR-ELRESG--RTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-227 |
9.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV------TSGTVLINGKDVTVTPPAK--RGISMVFQSYALYPH 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGLGLKQAGTA-KEEIESRVAKASGMLSLEPYLARR---PA-ELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 165 DaalrVQTRLEIARLHRSLKA--TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:PRK14246 185 D----IVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-223 |
9.88e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.39 E-value: 9.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 16 HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINgkDVTVTP--------PAKRGISMVFQsyalY 87
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD--DITITHktkdkyirPVRKRIGMVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 88 PHL-----TVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLE-PYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:PRK13646 94 PESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-253 |
1.27e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAY--GTHDVLKGID---LEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--- 74
Cdd:PRK13641 2 SIKFENVDYIYspGTPMEKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 ---RGISMVFQ--SYALYPHLTVKDNMgLGLKQAGTAKEEIESRVAKASGMLSL-EPYLARRPAELSGGQRQRVAIGRAI 148
Cdd:PRK13641 82 klrKKVSLVFQfpEAQLFENTVLKDVE-FGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 149 VREPELFLFDEPLSNLDAALRVQTrLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPaNV 228
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EW 238
|
250 260
....*....|....*....|....*
gi 494968020 229 FVGGFIGSPQMNLIpAEKLEQGGAK 253
Cdd:PRK13641 239 LKKHYLDEPATSRF-ASKLEKGGFK 262
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-212 |
1.47e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGISMV---FQSYALYPHL 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaiRAGIAYVpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 TVKDNMGLG-LKQAGTA----KEEIESRVAKASGMLSLE-PYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:COG1129 346 SIRENITLAsLDRLSRGglldRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 165 DaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:COG1129 426 D----VGAKAEIYRLIRELAAegkAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-225 |
1.55e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.42 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISMVFQSYALYPHlTVKDN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGLKQagTAKEEIESrVAKASGMLSL--------EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAa 167
Cdd:TIGR00958 575 IAYGLTD--TPDEEIMA-AAKAANAHDFimefpngyDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA- 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 168 lRVQTRLEIARLHRSLkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:TIGR00958 651 -ECEQLLQESRSRASR--TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-222 |
1.89e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP-PAKRGISMVF 81
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 QSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 162 SNLDAALRvqtRLEIARLhRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI-----------EQIGSP-MELY 222
Cdd:PRK13536 201 TGLDPHAR---HLIWERL-RSLLArgkTILLTTHFMEEAERLCDRLCVLEAGRKiaegrphalidEHIGCQvIEIY 272
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-212 |
4.04e-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: 98.31 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGT---HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRG 76
Cdd:cd03248 10 GIVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYALYPHlTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPY-----LARRPAELSGGQRQRVAIGRAIVRE 151
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydteVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 152 PELFLFDEPLSNLDAALRVQTRLEIARLHRSlkATMIYVTHdQVEAMTLADKIVVMNAGAI 212
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
7.61e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 7.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTsGTVLINGKDVTVTPPA--KRGISMVFQSYALyPHLTVKDNMGLG 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPEswRKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 100 LKQAGtaKEEIESRVAKA-------SGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDA--ALRV 170
Cdd:PRK11174 447 NPDAS--DEQLQQALENAwvseflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhsEQLV 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 171 QTRLEIArlhrSLKATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK11174 525 MQALNAA----SRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-212 |
9.51e-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: 97.34 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 10 RKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED---VTSGTVLINGKDVTvtpPA--KRGISMVFQSY 84
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRK---PDqfQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 85 ALYPHLTVKD------NMGLGLKQAGTAKEEIESRVAkaSGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:cd03234 91 ILLPGLTVREtltytaILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494968020 159 EPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-225 |
1.21e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 29 GEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK-----RGISMVFQS-YA-LYPHLTVKDNMGLGLK 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 102 QAGTAK-EEIESRVAKASGMLSLEPYLA-RRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARL 179
Cdd:PRK10261 430 VHGLLPgKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494968020 180 HRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-218 |
1.41e-23 |
|
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: 96.41 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLK--SIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAK--RGI 77
Cdd:cd03244 1 GDIEFKnvSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSyalyPHL---TVKDNMG-LG----------LKQAGtakeeIESRVAKASGMLSLEpyLARRPAELSGGQRQRVA 143
Cdd:cd03244 81 SIIPQD----PVLfsgTIRSNLDpFGeysdeelwqaLERVG-----LKEFVESLPGGLDTV--VEEGGENLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 144 IGRAIVREPELFLFDEPLSNLDaalrVQTRLEIARLHRSL--KATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSP 218
Cdd:cd03244 150 LARALLRKSKILVLDEATASVD----PETDALIQKTIREAfkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.90e-23 |
|
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: 100.65 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDV--TSGTVLIN------------------ 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 64 -----------------GKDVTVTPPAKRGISMVFQ-SYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEP 125
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 126 YLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAalrvqtrlEIARL-HRSLKA-------TMIYVTHDQVEA 197
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP--------QTAKLvHNALEEavkasgiSMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*..
gi 494968020 198 MTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
2.29e-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: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLInGKDVTVtppakrgismvfqS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI-------------G 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 Y------ALYPHLTVKDNMglglKQAGTAKEEIESRvakasGMLS---LEPYLARRPAE-LSGGQRQRVAIGRAIVREPE 153
Cdd:COG0488 382 YfdqhqeELDPDKTVLDEL----RDGAPGGTEQEVR-----GYLGrflFSGDDAFKPVGvLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 154 LFLFDEPLSNLDaalrVQTR--LEIArlhrsLKA---TMIYVTHDQ--VEamTLADKIVVMNAGAIE 213
Cdd:COG0488 453 VLLLDEPTNHLD----IETLeaLEEA-----LDDfpgTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-225 |
2.86e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.60 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 21 GIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMVFQSYALYPHLTVKDNM- 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVRLFREMTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 97 -------------GLgLKQAGTAKEEIES--RVA---KASGMLSlepyLARRPA-ELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:PRK11300 103 vaqhqqlktglfsGL-LKTPAFRRAESEAldRAAtwlERVGLLE----HANRQAgNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 158 DEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
2.92e-23 |
|
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: 94.69 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD--VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG-ISMV 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSyalyPHL---TVKDNMGlglkqagtakeeiesrvakasgmlslepylarrpAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:cd03247 81 NQR----PYLfdtTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 158 DEPLSNLDAalrvQTRLEIARLHRS-LK-ATMIYVTHdQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03247 123 DEPTVGLDP----ITERQLLSLIFEvLKdKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
4.00e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDvtvtpPAK------RGISMVF-QSYALYPHLT 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKrrkefaRRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 92 VKDNmgLGLKQA--GTAKEEIESRVAKASGMLSLEPYLaRRPA-ELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAL 168
Cdd:COG4586 113 AIDS--FRLLKAiyRIPDAEYKKRLDELVELLDLGELL-DTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494968020 169 RVQTRLEIARLHRSLKATMIYVTHD--QVEAmtLADKIVVMNAGAI 212
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-224 |
1.23e-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: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISMVFQSYALYPHlTVKD 94
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLGlKQAGTAKEEIESRVAKASGM-------LSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD-- 165
Cdd:TIGR02203 425 NIAYG-RTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDne 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 166 AALRVQTRLEiaRLHRSlkATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:TIGR02203 504 SERLVQAALE--RLMQG--RTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-221 |
1.33e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.05 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 12 AYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT--VTPPAKRGISMVFQSYALYPH 89
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGLG-------LKQAGTAKEEIESRVAKASGMLSlepyLARRPAE-LSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:PRK10253 96 ITVQELVARGryphqplFTRWRKEDEEAVTKAMQATGITH----LADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-216 |
1.96e-22 |
|
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: 93.37 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtVTPPAkrGISMV 80
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSLL--GLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQsyalyPHLTVKDN-------MGLGLKQAGTAKEEIEsrvakasgMLS-LEPYLARRPAELSGGQRQRVAIGRAIVREP 152
Cdd:cd03220 95 FN-----PELTGRENiylngrlLGLSRKEIDEKIDEII--------EFSeLGDFIDLPVKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 153 ELFLFDEPLSNLDAALRVQTRLEIARLHRSLKaTMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-224 |
2.23e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.89 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGTHD-VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-VTPPAKRG-IS 78
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdIDRHTLRQfIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHlTVKDNMGLGLKQAGTAKE--------EIESRVAKASgmLSLEPYLARRPAELSGGQRQRVAIGRAIVR 150
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLGAKENVSQDEiwaaceiaEIKDDIENMP--LGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 151 EPELFLFDEPLSNLDAALRvqtRLEIARLHRSLKATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.39e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAY--GTHdVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA----KRGI 77
Cdd:PRK13636 6 LKVEELNYNYsdGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQS--YALYPhLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPyLARRPAE-LSGGQRQRVAIGRAIVREPEL 154
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 155 FLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELY 222
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-206 |
3.97e-22 |
|
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: 93.24 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 25 EVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPpakRGISMVFQSyalyphlTVKDNMGLGLKQAG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP---QYIKADYEG-------TVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 105 TaKEEIESRVAKAsgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLK 184
Cdd:cd03237 91 T-HPYFKTEIAKP---LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|..
gi 494968020 185 ATMIYVTHDQVEAMTLADKIVV 206
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIV 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-224 |
5.53e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.53 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 13 YGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTppaKRG-------ISMVFQSYA 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS---KRGllalrqqVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHLT-VKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:PRK13638 88 QQIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 165 DAALRVQTRLEIARLHRSLKATMIyVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-215 |
7.70e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 20 KGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMVFQSY---ALYPHLTVK 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITESRrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 94 DNMGL-------GLKQA-GTAKEEIESRVA-KASGMLSLEPY-LARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK09700 360 QNMAIsrslkdgGYKGAmGLFHEVDEQRTAeNQRELLALKCHsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 164 LDaalrVQTRLEIARLHRSLK---ATMIYVTHDQVEAMTLADKIVVMNAGAIEQI 215
Cdd:PRK09700 440 ID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-167 |
8.73e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.47 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRgISMVFQSYALYPHLTVKDNMG 97
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 98 LGLKQAGTAkeeiESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAA 167
Cdd:PRK13539 96 FWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-257 |
1.02e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.64 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHD----VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL---EDVTSGTVLINGKDVTVTPPAK-- 74
Cdd:PRK09473 13 LDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKEln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 75 ----RGISMVFQS--YALYPHLTVKDN-MGLGLKQAGTAKEEI--ES-RVAKASGMLSLEPYLARRPAELSGGQRQRVAI 144
Cdd:PRK09473 93 klraEQISMIFQDpmTSLNPYMRVGEQlMEVLMLHKGMSKAEAfeESvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 145 GRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
250 260 270
....*....|....*....|....*....|...
gi 494968020 225 PANVFVGGFigspqMNLIPaeKLEQGGAKTIGI 257
Cdd:PRK09473 253 PSHPYSIGL-----LNAVP--RLDAEGESLLTI 278
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-223 |
1.41e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP---PAKRGI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDN-MGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 157 FDEPLSNLDAALRVQTRLEIARLHRSLKATMIyVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLI-TDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-218 |
2.31e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.16 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGTH--DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP--PAKRGI 77
Cdd:cd03369 5 GEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHlTVKDNMGLGLKQagtAKEEIESRVAKASGMLSlepylarrpaeLSGGQRQRVAIGRAIVREPELFLF 157
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLDPFDEY---SDEEIYGALRVSEGGLN-----------LSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 158 DEPLSNLDaalrVQTRLEIARLHRSL--KATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSP 218
Cdd:cd03369 150 DEATASID----YATDALIQKTIREEftNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-167 |
2.95e-21 |
|
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: 89.73 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPAKRGISMVFQSYALYPHLTVKDNM 96
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 97 GLGLKQAGTAKEEIESRVAKAsGMLSLEPYLArrpAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAA 167
Cdd:TIGR01189 95 HFWAAIHGGAQRTIEDALAAV-GLTGFEDLPA---AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-223 |
5.15e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.46 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL--EDVTSG--------TVLINGKDVTVTPPA 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGshiellgrTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 KRGISMVFQSYALYPHLTVKDNMGLGlkQAGTA----------KEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVA 143
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIG--ALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 144 IGRAIVREPELFLFDEPLSNLDAAlRVQTRLEIARLHRSLKATMIYVTHDQVE-AMTLADKIVVMNAGAIEQIGSPMELY 222
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFD 241
|
.
gi 494968020 223 N 223
Cdd:PRK09984 242 N 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-192 |
6.84e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLIngkdvtvtPPAKRgisMVF---QSYalyphltvkd 94
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR---VLFlpqRPY---------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 nMGLG-LKQA----GTAKEEIESRVAKASGMLSLePYLARRPAE-------LSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:COG4178 437 -LPLGtLREAllypATAEAFSDAELREALEAVGL-GHLAERLDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|.
gi 494968020 163 NLDAALrvQTRLeIARLHRSL-KATMIYVTH 192
Cdd:COG4178 515 ALDEEN--EAAL-YQLLREELpGTTVISVGH 542
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-220 |
7.87e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.07 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL--EDVTSGTVLINGKDV---TVTPPAKRGIS 78
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqasNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLG--LKQAG-TAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELF 155
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGneITPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 156 LFDEPLSNLDAAlRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGaiEQIGS-PME 220
Cdd:PRK13549 166 ILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGTrPAA 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
9.85e-21 |
|
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: 86.73 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLInGKDVTVtppakrgismvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVKI-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 yalyphltvkdnmglglkqagtakeeiesrvakasgmlslePYLARrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:cd03221 66 -----------------------------------------GYFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494968020 164 LDaalrVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:cd03221 101 LD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-212 |
1.52e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVT-----PPAKRGIS 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 M------VFQSYA--LYPHLTVKDN-----MGLGLKQAGTAKEEiesrvakASGMLS-LEPYLAR---RPAELSGGQRQR 141
Cdd:PRK11701 87 LrtewgfVHQHPRdgLRMQVSAGGNigerlMAVGARHYGDIRAT-------AGDWLErVEIDAARiddLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 142 VAIGRAIVREPELFLFDEPLSNLDAAlrVQTRL--EIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVS--VQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-226 |
1.61e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.99 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAygTHDVL-KGIDLEVKDGEFVIFVGPSGCGKSTllrSIAGLEDV-------TSGTVLINGKdvTVTPPAKR 75
Cdd:PRK10418 5 IELRNIALQ--AAQPLvHGVSLTLQRGRVLALVGGSGSGKSL---TCAAALGIlpagvrqTAGRVLLDGK--PVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 76 G--ISMVFQS--YALYPHLTVKDNMGLGLKQAG-TAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVR 150
Cdd:PRK10418 78 GrkIATIMQNprSAFNPLHTMHTHARETCLALGkPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 151 EPELFLFDEPLSNLDAAlrVQTRLE--IARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPA 226
Cdd:PRK10418 158 EAPFIIADEPTTDLDVV--AQARILdlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-263 |
2.63e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 91.42 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL--EDVTSGTVLINGKDV---TVTPPAKRGIS 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkasNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLG----LKQAGTAKEEIESRVAKASGMLSLEPYLARRP-AELSGGQRQRVAIGRAIVREPE 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 154 LFLFDEPLSNLDAAlRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGaiEQIGS-PMELYNRPAnvFVGG 232
Cdd:TIGR02633 162 LLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVATkDMSTMSEDD--IITM 236
|
250 260 270
....*....|....*....|....*....|.
gi 494968020 233 FIGSPQMNLIPAEKLEQGgakTIGIRPEHIT 263
Cdd:TIGR02633 237 MVGREITSLYPHEPHEIG---DVILEARNLT 264
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-224 |
3.11e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.56 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV-TVTPPA-KRGISMVFQSYALYpHLTVKDNM 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrTVTRASlRRNIAVVFQDAGLF-NRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 97 GLGLKQAGTAKEEIESRVAKASGML-----SLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAL--R 169
Cdd:PRK13657 430 RVGRPDATDEEMRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETeaK 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 170 VQTRLEIARLHRslkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:PRK13657 510 VKAALDELMKGR----TTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
4.95e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGlkQAGTAK---------EEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVRE 151
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG--RHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 152 PELFLFDEPLSNLDAAlRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGA 211
Cdd:PRK09700 164 AKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-225 |
1.14e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.87 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED----VTSGTVLINGKDVTVTPPAKR------GISMVFQS--YALYPH 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGLGLK--QAGTAKEeiesRVAKASGMLSL------EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:PRK11022 106 YTVGFQIMEAIKvhQGGNKKT----RRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 162 SNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-210 |
1.97e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDvTSGTVLINGKDVT-----------------VTPPAkrgiSM-V 80
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSdwsaaelarhraylsqqQSPPF----AMpV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHltvkdnmglglkqAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVR-------EPE 153
Cdd:COG4138 87 FQYLALHQP-------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 154 LFLFDEPLSNLDAALrvQTRLEiaRLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:COG4138 154 LLLLDEPMNSLDVAQ--QAALD--RLLRELCQqgiTVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-221 |
3.50e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.18 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLL-----RSIAGLEdvTSGTVLINGKdvTVTPPAKRGIS-MVFQSYALYPHLTV 92
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGM--PIDAKEMRAISaYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNM----GLGLKQAGTAKEEIEsRVAKASGMLSLEPY------LARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:TIGR00955 117 REHLmfqaHLRMPRRVTKKEKRE-RVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 163 NLD---AALRVQTRLEIARlhrslKATMIYVTHDQ--VEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:TIGR00955 196 GLDsfmAYSVVQVLKGLAQ-----KGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-210 |
5.99e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV---TVTPPAKRGI 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHLTVKDNMGLGlkQAGTAKEEIESRVAKASGMLSLE-------PylARRPAELSGGQRQRVAIGRAIVR 150
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLG--QLPHKGGIVNRRLLNYEAREQLEhlgvdidP--DTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 151 EPELFLFDEPLSNLDAalRVQTRLeiARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:PRK11288 158 NARVIAFDEPTSSLSA--REIEQL--FRVIRELRAegrVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-226 |
1.13e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 10 RKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL-----EDVTSGTVLINGKDVTVTPPAK----RG--IS 78
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTlrgvRGnkIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQS------------YALYPHLTVKDNMGlglKQAgtAKEEIES---RVakasGMLSLEPYLARRPAELSGGQRQRVA 143
Cdd:PRK15134 96 MIFQEpmvslnplhtleKQLYEVLSLHRGMR---REA--ARGEILNcldRV----GIRQAAKRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 144 IGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG-AIEQiGSPMELY 222
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGrCVEQ-NRAATLF 245
|
....
gi 494968020 223 NRPA 226
Cdd:PRK15134 246 SAPT 249
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-217 |
1.30e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 83.54 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLE--DVTSGTVLINGKDVTVTPP---AKRGIS 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPeerAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLGL--KQAGTAKEEIE-----SRVAKASGMLSLEP-YLARRPAE-LSGGQRQRVAIGRAIV 149
Cdd:CHL00131 88 LAFQYPIEIPGVSNADFLRLAYnsKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 150 REPELFLFDEPLSNLDA-ALRVQTRlEIARLHRSLKAtMIYVTHDQveamTLADKIV-----VMNAGAIEQIGS 217
Cdd:CHL00131 168 LDSELAILDETDSGLDIdALKIIAE-GINKLMTSENS-IILITHYQ----RLLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-212 |
2.36e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 16 HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR---GISMV---FQSYALYPH 89
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGL-----------GLKQAGTAKEEIESRVA----KASGmlslepylARRPAE-LSGGQRQRVAIGRAIVREPE 153
Cdd:COG3845 351 MSVAENLILgryrrppfsrgGFLDRKAIRAFAEELIEefdvRTPG--------PDTPARsLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 154 LFLFDEPLSNLD--AALRVQTRLeIARlhRSLKATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:COG3845 423 LLIAAQPTRGLDvgAIEFIHQRL-LEL--RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-206 |
2.53e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.63 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTH--DVLKGidlEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLingKDVTVtppakrgismvfqSY- 84
Cdd:PRK13409 345 DLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELKI-------------SYk 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 85 -----ALYPhLTVKDNmglgLKQAGTA------KEEIESRvakasgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPE 153
Cdd:PRK13409 406 pqyikPDYD-GTVEDL----LRSITDDlgssyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 154 LFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVV 206
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-223 |
3.19e-18 |
|
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: 85.84 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR-GISMVFQSYALYPHLTVKDNMGLGL 100
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 101 KQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRvQTRLEIARLH 180
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR-RSIWDLLLKY 1107
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494968020 181 RSLKaTMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:TIGR01257 1108 RSGR-TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-225 |
3.54e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.15 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 15 THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-VTPPAKRG-ISMVFQSYALYPHlTV 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTkLQLDSWRSrLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLGLKQAgtAKEEIEsRVAKASG----MLSL----EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:PRK10789 406 ANNIALGRPDA--TQQEIE-HVARLASvhddILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 165 DAalrvQTRLEIARLHRSL--KATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK10789 483 DG----RTEHQILHNLRQWgeGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-225 |
5.09e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKRG--ISMVFQ--SYALYPHLTV 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQdpSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLGLK-QAGTAKEEIESRVAKASGMLSLEP-YLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRV 170
Cdd:PRK15112 107 SQILDFPLRlNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 171 QTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-216 |
6.07e-18 |
|
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: 81.80 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKD-----VTVTPPAKRGIS 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MvfQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGML---------SLEPYLAR---RPAELSGGQRQRVAIGR 146
Cdd:TIGR02323 84 M--RTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIrataqdwleEVEIDPTRiddLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 147 AIVREPELFLFDEPLSNLDAAlrVQTRL--EIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVS--VQARLldLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-217 |
6.36e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.83 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLingkdvtvtppAKRGISMVFQSyALYPHLTVKDNMG 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 98 LglkqagtAKEEIESRVAKASGMLSLEPYLARRPA-----------ELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDA 166
Cdd:PTZ00243 743 F-------FDEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 167 AL--RVQTRLEIARLHrslKATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGS 217
Cdd:PTZ00243 816 HVgeRVVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-224 |
6.59e-18 |
|
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: 85.00 E-value: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtvtppakrgISMVFQSyALYPHLTVKDNMGL 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 99 GLKqagtAKEEIESRVAKASGMLS-LE-------PYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRV 170
Cdd:TIGR00957 722 GKA----LNEKYYQQVLEACALLPdLEilpsgdrTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 171 QTRLEIARLHRSLK-ATMIYVTHDqVEAMTLADKIVVMNAGAIEQIGSPMELYNR 224
Cdd:TIGR00957 798 HIFEHVIGPEGVLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-215 |
9.38e-18 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 80.38 E-value: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 9 IRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVT---SGTVLINGKDVTVTP-PAKRGISMVFQSY 84
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAeKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 85 ALYPHLTVKDNMGLGLKqagtakeeiesrvAKASGMLSlepylarrpaELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:cd03233 93 VHFPTLTVRETLDFALR-------------CKGNEFVR----------GISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 165 DAAlrvqTRLEIARLHRSL-----KATMIYVTHDQVEAMTLADKIVVMNAGaiEQI 215
Cdd:cd03233 150 DSS----TALEILKCIRTMadvlkTTTFVSLYQASDEIYDLFDKVLVLYEG--RQI 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-167 |
1.59e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 25 EVKDGEFVIFVGPSGCGKSTLLRSIAGLEDvTSGTVLINGKDVTVTPPAK----RG---------ISM-VFQSYALYPHl 90
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 tvkdnmglglkqAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRV-------AIGRAIVREPELFLFDEPLSN 163
Cdd:PRK03695 96 ------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNS 163
|
....
gi 494968020 164 LDAA 167
Cdd:PRK03695 164 LDVA 167
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-235 |
2.07e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 34 FVGPSGCGKSTLLRSIAGLEDVTSG-----TVLINGKDVTVTPPA---KRGISMVFQSYALYPhLTVKDNMGLGLKQAGT 105
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlefRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 106 AKEE-----IESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAlrvqTRLEIARLH 180
Cdd:PRK14271 131 VPRKefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPT----TTEKIEEFI 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 181 RSL--KATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANV----FVGGFIG 235
Cdd:PRK14271 207 RSLadRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-221 |
2.71e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR---G-ISmvfQSYALYPHLTVKDNMG 97
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRrrvGyMS---QAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 98 LGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQT-RLEI 176
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFwRLLI 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494968020 177 aRLHRSLKATmIYV-THDQVEAMtLADKIVVMNAGAIEQIGSPMEL 221
Cdd:NF033858 442 -ELSREDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-227 |
3.40e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 17 DVLKGIDLEVKDGEFVIFVGPSGCGKS----TLLRSI--AGLEdVTSGTVLINGKDVTVTPPAK---------RG--ISM 79
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLRRRSRQVIELSEqsaaqmrhvRGadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 80 VFQS--YALYPHLTVKDNMGLGLK-QAGTAKEEiesRVAKASGMLSL------EPYLARRPAELSGGQRQRVAIGRAIVR 150
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRlHQGASREE---AMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 151 EPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPAN 227
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-167 |
3.62e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGK-DVTVTPPAKRGISMVFQSYALYPHLTVKDNm 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSVLEN- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 97 gLGLKQAGTAKEEIESRVAKAsgmlSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAA 167
Cdd:cd03231 94 -LRFWHADHSDEQVEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-194 |
3.77e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 15 THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVtPPAKRGISmvfqsyALYPHLTVKD 94
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-GREASLID------AIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLgLKQAGtakeeiesrvakasgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRL 174
Cdd:COG2401 115 AVEL-LNAVG----------------LSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|
gi 494968020 175 EIARLHRSLKATMIYVTHDQ 194
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-187 |
4.47e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 82.23 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTS--GTVLINGKdvTVTPPAKRGISMVFQSYALYPHLTVKDN 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR--KPTKQILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MG----LGLKQAGTAKEEI---ESRVAKAsGMLSLEPYLARRP--AELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD- 165
Cdd:PLN03211 161 LVfcslLRLPKSLTKQEKIlvaESVISEL-GLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDa 239
|
170 180
....*....|....*....|....
gi 494968020 166 -AALR-VQTRLEIARLHRSLKATM 187
Cdd:PLN03211 240 tAAYRlVLTLGSLAQKGKTIVTSM 263
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-221 |
5.49e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGTHDV--LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLING---KDVTVTPpAKRG 76
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLAS-LRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYALYpHLTVKDNMGLGLKQAGTaKEEIE--SRVAKASGMLS-----LEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYARTEQYS-REQIEeaARMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 150 REPELFLFDEPLSNLD--AALRVQTRLEIARLHRslkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK11176 497 RDSPILILDEATSALDteSERAIQAALDELQKNR----TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-192 |
6.15e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLIngkdvtvtpPAKRGISMVFQSyalyPHLTvkdnmg 97
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 98 lglkqAGTAKEEIesrvakasgmlslepylaRRP--AELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDaalrVQTRLE 175
Cdd:cd03223 77 -----LGTLREQL------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129
|
170
....*....|....*..
gi 494968020 176 IARLHRSLKATMIYVTH 192
Cdd:cd03223 130 LYQLLKELGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-205 |
1.08e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 12 AYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAG---LEDvtsGTVLINgKDVTVT-----PPakRGIS-MVF- 81
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYE-QDLIVArlqqdPP--RNVEgTVYd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 82 -------------QSYALYPHLTVKDNMGLGLKQAGTAKEEI--------ESRVAKASGMLSLEPylARRPAELSGGQRQ 140
Cdd:PRK11147 86 fvaegieeqaeylKRYHDISHLVETDPSEKNLNELAKLQEQLdhhnlwqlENRINEVLAQLGLDP--DAALSSLSGGWLR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 141 RVAIGRAIVREPELFLFDEPLSNLDaalrVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIV 205
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-206 |
1.37e-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: 80.60 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYG--THDVLKGidlEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVlinGKDVTVtppakrgismvfqSY- 84
Cdd:COG1245 346 DLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKI-------------SYk 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 85 -----ALYPhLTVKDNMGlglkqaGTAKEEIES-----RVAKAsgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPEL 154
Cdd:COG1245 407 pqyisPDYD-GTVEEFLR------SANTDDFGSsyyktEIIKP---LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 155 FLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHD-QVEAMtLADKIVV 206
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDiYLIDY-ISDRLMV 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-208 |
1.54e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVlingkdvtVTPPAKRgISMVFQSYA 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPH--LTVKDNMGLglkQAGTAKEEIESRVAKASGMLSLEPYLARrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK09544 78 LDTTlpLTVNRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494968020 164 LDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMN 208
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-223 |
4.99e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.40 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHD------VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAG-LEDVTSGTVLINGKdVTVTPPakrgISMV 80
Cdd:PLN03130 616 SIKNGYFSWDskaerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-VAYVPQ----VSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSyalyphlTVKDNMGLGLkQAGTAKEEIESRVAKASGMLSLEP-----YLARRPAELSGGQRQRVAIGRAIVREPELF 155
Cdd:PLN03130 691 FNA-------TVRDNILFGS-PFDPERYERAIDVTALQHDLDLLPggdltEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 156 LFDEPLSNLDAalrvqtrlEIAR------LHRSLKA-TMIYVThDQVEAMTLADKIVVMNAGAIEQIGSPMELYN 223
Cdd:PLN03130 763 IFDDPLSALDA--------HVGRqvfdkcIKDELRGkTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-229 |
9.86e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.28 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV--TPPAKRGI 77
Cdd:PTZ00243 1307 GSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHlTVKDNMG----------------LGLKQAGTAKEE-IESRVAKASGMLSLepylarrpaelsgGQRQ 140
Cdd:PTZ00243 1387 SMIPQDPVLFDG-TVRQNVDpfleassaevwaalelVGLRERVASESEgIDSRVLEGGSNYSV-------------GQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 141 RVAIGRAIVREPELF-LFDEPLSNLDAALRVQTRleiARLHRSLKA-TMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSP 218
Cdd:PTZ00243 1453 LMCMARALLKKGSGFiLMDEATANIDPALDRQIQ---ATVMSAFSAyTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSP 1528
|
250
....*....|.
gi 494968020 219 MELYNRPANVF 229
Cdd:PTZ00243 1529 RELVMNRQSIF 1539
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-221 |
1.18e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 35 VGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV--TPPAKRGISMVFQSYALYPHLTVKDNMGLG-------LKQAGT 105
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQLPAAEGMTVRELVAIGrypwhgaLGRFGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 106 AKEEiesRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKA 185
Cdd:PRK10575 123 ADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGL 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 494968020 186 TMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMEL 221
Cdd:PRK10575 200 TVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-194 |
1.64e-15 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 74.83 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED--VTSGTVLINGKDVTVTPPAKR---GIS 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLGLKQAGTAKEE-----------IESRVAkasgMLSLEPYLARRPAEL--SGGQRQRVAIG 145
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQepldrfdfqdlMEEKIA----LLKMPEDLLTRSVNVgfSGGEKKRNDIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494968020 146 RAIVREPELFLFDEPLSNLDA-ALRVQTrlEIARLHRSLKATMIYVTHDQ 194
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIdALKIVA--DGVNSLRDGKRSFIIVTHYQ 205
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-211 |
2.05e-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: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGK-DVTVTPPAKRGISMVFQSYALY-PHL---TVK 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAAQkPWLlnaTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 94 DNMGLGL---KQagtakeeiesRVAKASGMLSLEP-----------YLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:cd03290 97 ENITFGSpfnKQ----------RYKAVTDACSLQPdidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 160 PLSNLDAALRVQTRLE-IARLHRSLKATMIYVTHdQVEAMTLADKIVVMNAGA 211
Cdd:cd03290 167 PFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDGS 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-234 |
2.75e-15 |
|
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: 74.33 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 26 VKDGEFVIFVGPSGCGKSTLLRSIAG--------------LEDVTS---GTVL-------INGK-DVTVTPpakrgismv 80
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdWDEILDefrGSELqnyftklLEGDvKVIVKP--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 fQSYALYPHlTVKDNMGLGLKQAGT--AKEEIESRvakasgmLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:cd03236 94 -QYVDLIPK-AVKGKVGELLKKKDErgKLDELVDQ-------LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 159 EPLSNLDaalrVQTRLEIARLHRSL---KATMIYVTHDQVEAMTLADKIVVM--NAGAIEQIGSPMELYNrPANVFVGGF 233
Cdd:cd03236 165 EPSSYLD----IKQRLNAARLIRELaedDNYVLVVEHDLAVLDYLSDYIHCLygEPGAYGVVTLPKSVRE-GINEFLDGY 239
|
.
gi 494968020 234 I 234
Cdd:cd03236 240 L 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-214 |
3.28e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAYGT-HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGIS 78
Cdd:PRK10790 339 GRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHlTVKDNMGLGlkqagtaKEEIESRVAKASGMLSLEPyLARRPAE------------LSGGQRQRVAIGR 146
Cdd:PRK10790 419 MVQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAE-LARSLPDglytplgeqgnnLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494968020 147 AIVREPELFLFDEPLSNLDAALR--VQTRLEIARLHrslkATMIYVTHdQVEAMTLADKIVVMNAG-AIEQ 214
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEqaIQQALAAVREH----TTLVVIAH-RLSTIVEADTILVLHRGqAVEQ 555
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-167 |
5.84e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 21 GIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAkrgismvFQSYALY--------PHLTV 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLGLKQAGTAKEE-IESRVAKASgmlslepyLARR---PAE-LSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAA 167
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEaLWEALAQVG--------LAGFedvPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-246 |
7.17e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 75.72 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 13 YGThDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtvtppakrgISMVFQSYALYPHlTV 92
Cdd:TIGR01271 437 YVT-PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLGLkqagTAKEEIESRVAKASgmlSLEPYLARRPAE-----------LSGGQRQRVAIGRAIVREPELFLFDEPL 161
Cdd:TIGR01271 504 KDNIIFGL----SYDEYRYTSVIKAC---QLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 162 SNLDaalrVQTRLEIarLHRSL-----KATMIYVThDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANvFVGGFIGS 236
Cdd:TIGR01271 577 THLD----VVTEKEI--FESCLcklmsNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD-FSSLLLGL 648
|
250
....*....|
gi 494968020 237 PQMNLIPAEK 246
Cdd:TIGR01271 649 EAFDNFSAER 658
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-246 |
8.23e-15 |
|
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: 73.35 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtvtppakrgISMVFQSYALYPHlTVKDNMG 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 98 LGLkqagTAKEEIESRVAKASgmlSLEPYLARRPAE-----------LSGGQRQRVAIGRAIVREPELFLFDEPLSNLDa 166
Cdd:cd03291 120 FGV----SYDEYRYKSVVKAC---QLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 167 alrVQTRLEI-----ARLHRSlkATMIYVThDQVEAMTLADKIVVMNAGAIEQIGSPMELYN-RPAnvFVGGFIGSPQMN 240
Cdd:cd03291 192 ---VFTEKEIfescvCKLMAN--KTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSlRPD--FSSKLMGYDTFD 263
|
....*.
gi 494968020 241 LIPAEK 246
Cdd:cd03291 264 QFSAER 269
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-222 |
9.26e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 9.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHD------VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAG-LEDVTSGTVLINGKdVTVTPPakrgISMV 80
Cdd:PLN03232 616 SIKNGYFSWDsktskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-VAYVPQ----VSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSyalyphlTVKDNMGLGLKQAgtakeeiESRVAKASGMLSLEPYL-----------ARRPAELSGGQRQRVAIGRAIV 149
Cdd:PLN03232 691 FNA-------TVRENILFGSDFE-------SERYWRAIDVTALQHDLdllpgrdlteiGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTrLEIARLHRSLKATMIYVThDQVEAMTLADKIVVMNAGAIEQIGSPMELY 222
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQV-FDSCMKDELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-250 |
1.10e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 26 VKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTppakrgISMVFQSYALYPH-------LTVKDNMGL 98
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------ISDVHQNMGYCPQfdaiddlLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 99 GLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIAR 178
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 179 LHRSLKAtMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVGGF-IGSPQMNLI----PAEKLEQG 250
Cdd:TIGR01257 2116 IIREGRA-VVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLLpdlnPVEQFFQG 2191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
1.57e-14 |
|
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: 74.20 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAY-GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGtvlingkDVTVTPPAKRGisMVFQS 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQPGIKVG--YLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGLGL---KQAGTAKEEI---------------------------------ESRVAKASGMLSLEPYL 127
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVaeiKDALDRFNEIsakyaepdadfdklaaeqaelqeiidaadawdlDSQLEIAMDALRCPPWD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 128 ARrPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAAlrvqtrlEIARLHRSL---KATMIYVTHD 193
Cdd:TIGR03719 157 AD-VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLqeyPGTVVAVTHD 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-208 |
2.49e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTH---DVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLING----KDVTVTpPAKRG 76
Cdd:PTZ00265 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLK-WWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 ISMVFQSYALYPHlTVKDNMGLGL-------------KQAGTAKEE----IESRVAKASGMLSL---------------- 123
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyyNEDGNDSQEnknkRNSCRAKCAGDLNDmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 124 -----------------------------EPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRL 174
Cdd:PTZ00265 541 yqtikdsevvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270
....*....|....*....|....*....|....
gi 494968020 175 EIARLHRSLKATMIYVTHdQVEAMTLADKIVVMN 208
Cdd:PTZ00265 621 TINNLKGNENRITIIIAH-RLSTIRYANTIFVLS 653
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-225 |
2.53e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED----VTSGTVLINGKDVTVTPPAKR------GISMVFQ--SYA 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHLTVKDNmglgLKQA--------------GTAKEEIES---RVakasGMLSLEPYLARRPAELSGGQRQRVAIGRAI 148
Cdd:COG4170 102 LDPSAKIGDQ----LIEAipswtfkgkwwqrfKWRKKRAIEllhRV----GIKDHKDIMNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 149 VREPELFLFDEPLSNLDAALRVQT-RLeIARLHRSLKATMIYVTHDqVEAMT-LADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIfRL-LARLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-207 |
4.13e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 16 HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTvTPPAKRGISMVFQSYAL---YPHLtV 92
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNLVAYVPQSEEVdwsFPVL-V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNMGLG----LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDaal 168
Cdd:PRK15056 98 EDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD--- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494968020 169 rVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVM 207
Cdd:PRK15056 175 -VKTEARIISLLRELRDegkTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-229 |
4.16e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTV--TPPAKRGI 77
Cdd:PLN03232 1233 GSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 78 SMVFQSYALYPHlTVKDNM-------GLGLKQAgTAKEEIESRVAKASgmLSLEPYLARRPAELSGGQRQRVAIGRAIVR 150
Cdd:PLN03232 1313 SIIPQSPVLFSG-TVRFNIdpfsehnDADLWEA-LERAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 151 EPELFLFDEPLSNLDAALRVQTRLEIARLHRSlkATMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVF 229
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-210 |
4.48e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPP---AKRGISMV 80
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDNMGLGlkqagtakEEIESRV---------AKASGMLS-LE-PYLARRP-AELSGGQRQRVAIGRAI 148
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLG--------REFVNRFgridwkkmyAEADKLLArLNlRFSSDKLvGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 149 VREPELFLFDEPLSNLdaalrvqTRLEIARLH---RSLKAT---MIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:PRK10762 157 SFESKVIIMDEPTDAL-------TDTETESLFrviRELKSQgrgIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-165 |
6.41e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVtppAKRGISMVFQSY--ALYPHLTVKDN 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHlpGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARrpaELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
1.64e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGISMV---FQSYALYPHLTVKDN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaiRAGIMLCpedRKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGL--------------GLKQAGTAKEEIESRVAKASGmlslepylARRP-AELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:PRK11288 352 INIsarrhhlragclinNRWEAENADRFIRSLNIKTPS--------REQLiMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 161 LSNLDaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK11288 424 TRGID----VGAKHEIYNVIYELAAqgvAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-226 |
3.29e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDV-LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA--KRGISMV 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLtvkdnmglgLKQAGTAKE-----------EIESRVAKASGMLSLepylarrpAELSGGQRQRVAIGRAIV 149
Cdd:PRK10522 403 FTDFHLFDQL---------LGPEGKPANpalvekwlerlKMAHKLELEDGRISN--------LKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQvEAMTLADKIVVMNAGAI-EQIGSPMELYNRPA 226
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLsELTGEERDAASRDA 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-207 |
3.76e-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: 70.20 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 27 KDGEFVIFVGPSGCGKSTLLRSIAGledvtsgtVLI-NGKDVTvTPPAKRGISMVFQSYALYPHLT-VKDNmglGLKQA- 103
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSG--------ELKpNLGDYD-EEPSWDEVLKRFRGTELQDYFKkLANG---EIKVAh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 104 -------------GTAKEEIES-----RVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:COG1245 165 kpqyvdlipkvfkGTVRELLEKvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494968020 166 aalrVQTRLEIARLHRSL----KATMIyVTHDQveAM--TLADKIVVM 207
Cdd:COG1245 245 ----IYQRLNVARLIRELaeegKYVLV-VEHDL--AIldYLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-207 |
7.29e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 26 VKDGEFVIFVGPSGCGKSTLLRSIAGL---------EDVT--------SGTVL-------INGK-DVTVTPPAKRGISMV 80
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSwdevlkrfRGTELqnyfkklYNGEiKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSyalyphlTVKDnmgLgLKQA---GTAKEEIEsrvakasgMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLF 157
Cdd:PRK13409 176 FKG-------KVRE---L-LKKVderGKLDEVVE--------RLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494968020 158 DEPLSNLDaalrVQTRLEIARLHRSL--KATMIYVTHDQVEAMTLADKIVVM 207
Cdd:PRK13409 237 DEPTSYLD----IRQRLNVARLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-186 |
2.62e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.57 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED--VTSGTVLINGKDVTVTPPakRGISMVFQSYALYPHLTVKDNM 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 97 GLGLKQAGtakeeiesrvakasgmLSLEpylarrpaelsggQRQRVAIGRAIVREPELFLFDEPLSNLDAalrvQTRLEI 176
Cdd:cd03232 101 RFSALLRG----------------LSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNI 147
|
170
....*....|
gi 494968020 177 ARLHRSLKAT 186
Cdd:cd03232 148 VRFLKKLADS 157
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-195 |
2.95e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHD--VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA-KRGISMVFQ 82
Cdd:PRK13540 2 LDVIELDFDYHDqpLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLGLKQAGTAKEeiesrVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|....*
gi 494968020 163 NLD--AALRVQTRLEiarLHRSLKATMIYVTHDQV 195
Cdd:PRK13540 157 ALDelSLLTIITKIQ---EHRAKGGAVLLTSHQDL 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-224 |
3.09e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTvtppAKRGISMVFQSY 84
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 85 A---------LYPHLTVKDNM-------GLGlkqagtaKEEIESRVA---KASGmlsLEPYLARRPAELSGGQRQRVAIG 145
Cdd:NF033858 79 AympqglgknLYPTLSVFENLdffgrlfGQD-------AAERRRRIDellRATG---LAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 146 RAIVREPELFLFDEPLSNLDAALRVQTRLEIARLhRSLKATM--IYVTHDQVEAMTLaDKIVVMNAGAIEQIGSPMELYN 223
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRI-RAERPGMsvLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
.
gi 494968020 224 R 224
Cdd:NF033858 227 R 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-183 |
3.26e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED---VTSGTVLINGKDVTVTPPakRGISMVFQSYALYPHLTVKD 94
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQ--RSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGLG--LKQ-AGTAKEEIESRVAKASGMLSLEPY---LARRPAE-LSGGQRQRVAIGRAIVREPELFLF-DEPLSNLDA 166
Cdd:TIGR00956 856 SLRFSayLRQpKSVSKSEKMEYVEEVIKLLEMESYadaVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS 935
|
170
....*....|....*..
gi 494968020 167 alrvQTRLEIARLHRSL 183
Cdd:TIGR00956 936 ----QTAWSICKLMRKL 948
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-206 |
3.54e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 64.13 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 25 EVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPpakrgismvfqsyalyphltvkdnmglglkqag 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP--------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 105 takeeiesrvakasgmlslepylarRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLK 184
Cdd:cd03222 68 -------------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 494968020 185 ATMIYVTHDQVEAMTLADKIVV 206
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-228 |
6.64e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 16 HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGleDVT----------SGTVLINGKDVTVTPP---AKRGISMVFQ 82
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAprlARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPhLTVKDNMGLG----LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAI---------V 149
Cdd:PRK13547 92 AQPAFA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYnRPANV 228
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAHI 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-212 |
7.29e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 14 GTHDVlkgiDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPA---KRGIsmVFQSY-----A 85
Cdd:PRK10762 267 GVNDV----SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglANGI--VYISEdrkrdG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHLTVKDNMGLGL-----KQAGTAKEEIESR-VAKASGMLSLE-PYLARRPAELSGGQRQRVAIGRAIVREPELFLFD 158
Cdd:PRK10762 341 LVLGMSVKENMSLTAlryfsRAGGSLKHADEQQaVSDFIRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 159 EPLSNLDaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK10762 421 EPTRGVD----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-193 |
8.60e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 5 QLKSIRKAYGT-HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGtvlingkDVTVTPPAKRGISMvfQS 83
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIKVGYLP--QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDN--MGLGLKQA--------------------GTAKE--------------EIESRVAKASGMLSLEPYL 127
Cdd:PRK11819 79 PQLDPEKTVRENveEGVAEVKAaldrfneiyaayaepdadfdALAAEqgelqeiidaadawDLDSQLEIAMDALRCPPWD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 128 ARrPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAalrvqtrlE-IARLHRSLKA---TMIYVTHD 193
Cdd:PRK11819 159 AK-VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsVAWLEQFLHDypgTVVAVTHD 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-225 |
1.04e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.82 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED----VTSGTVLINGKDV-TVTPPAKR-----GISMVFQSyalyPH-- 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLlRLSPRERRklvghNVSMIFQE----PQsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGLGLKQA-------GTAKEEIESRVAKA------SGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:PRK15093 102 LDPSERVGRQLMQNipgwtykGRWWQRFGWRKRRAiellhrVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 157 FDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRP 225
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-165 |
1.98e-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: 64.57 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLInGKDVTvtppakrgISMVFQS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 Y-ALYPHLTVKDNMGLGLKQAGTAKEEIESRVakasgmlslepYLAR----------RPAELSGGQRQRVAIGRAIVREP 152
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----------YVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|...
gi 494968020 153 ELFLFDEPLSNLD 165
Cdd:TIGR03719 463 NVLLLDEPTNDLD 475
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-215 |
3.86e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.66 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHD-----VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVT-VTPPAKRG 76
Cdd:COG4615 327 TLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 77 -ISMVFQSYALYPHLtvkdnmgLGLKQAGTAKE--------EIESRVAKASGMLSlepylarrPAELSGGQRQRVAIGRA 147
Cdd:COG4615 407 lFSAVFSDFHLFDRL-------LGLDGEADPARarellerlELDHKVSVEDGRFS--------TTDLSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494968020 148 IVREPELFLFDEPLSNLDAALRvqtRL---EIarLHRsLKA---TMIYVTHDQvEAMTLADKIVVMNAGAIEQI 215
Cdd:COG4615 472 LLEDRPILVFDEWAADQDPEFR---RVfytEL--LPE-LKArgkTVIAISHDD-RYFDLADRVLKMDYGKLVEL 538
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
255-325 |
4.39e-11 |
|
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: 58.02 E-value: 4.39e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 255 IGIRPEHITLSREQGTWAAKVVHVEHLGADTIIYLESDHTGLLTVRLFGEHQ--YEPDETVYATPDTGHMHRF 325
Cdd:pfam08402 1 LAIRPEKIRLAAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHArpPAPGDRVGLGWDPEDAHVL 73
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-208 |
4.54e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 57 SGTVLINGKDVT--VTPPAKRGISMVFQSYALYpHLTVKDNMGLGLKQAgtAKEEiesrVAKASGMLSLEPYLARRPAE- 133
Cdd:PTZ00265 1276 SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDA--TRED----VKRACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 134 ----------LSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHdQVEAMTLADK 203
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
....*
gi 494968020 204 IVVMN 208
Cdd:PTZ00265 1428 IVVFN 1432
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-210 |
5.56e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 15 THDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLED----VTSGTVLINGKDVTVTPPAKRGISM-VFQSYALYPH 89
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGDVVyNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNM-------GLGLKQAGTAKEEIESRVAKasgmLSLEPY-------------LARrpaELSGGQRQRVAIGRAIV 149
Cdd:TIGR00956 153 LTVGETLdfaarckTPQNRPDGVSREEYAKHIAD----VYMATYglshtrntkvgndFVR---GVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 150 REPELFLFDEPLSNLDAAlrvqTRLEIArlhRSLKaTMIYVTHDQV---------EAMTLADKIVVMNAG 210
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSA----TALEFI---RALK-TSANILDTTPlvaiyqcsqDAYELFDKVIVLYEG 287
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-210 |
2.67e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 6 LKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV---TVTPPAKRGISMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 83 SYALYPHLTVKDNMGLG---LKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDE 159
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 160 PLSNLDAAlRVQTRLEIARLHRSLKATMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:PRK10982 161 PTSSLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-165 |
5.12e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 21 GIDLEVKdgefVIFVGPSGCGKSTLLRSIAGLEDVTSGTVL--------------INGKDVTVTPpakrgISMVFQSYAL 86
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNP-----LLYMMRCFPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 87 YPHLTVKDNMG-LGLkqagtakeeiesrvakaSGMLSLEPYLArrpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:PLN03073 602 VPEQKLRAHLGsFGV-----------------TGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-212 |
1.14e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTPPAKR-GISMVF-----QSYALY-------- 87
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 88 -PHLTVkDNMGLGLKqagTAKEE-IESRVAKASGM-LSLEPYLARRpaeLSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:PRK15439 362 vCALTH-NRRGFWIK---PARENaVLERYRRALNIkFNHAEQAART---LSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 165 DaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK15439 435 D----VSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-193 |
1.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGK-DVTvtppakrgismVFQSY--ALYPHLTVKDN 95
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA-----------YFDQHraELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGlkqagtaKEEIE--SRVAKASGMLS---LEPYLARRPAE-LSGGQRQRVAIGRAIVREPELFLFDEPLSNLDaalr 169
Cdd:PRK11147 404 LAEG-------KQEVMvnGRPRHVLGYLQdflFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD---- 472
|
170 180
....*....|....*....|....*
gi 494968020 170 VQTrLE-IARLHRSLKATMIYVTHD 193
Cdd:PRK11147 473 VET-LElLEELLDSYQGTVLLVSHD 496
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-221 |
2.76e-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: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVtvtppAKRGISMVFQSYALY 87
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-----AKIGLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 88 PHLTV--KDNMGLGLKQAGTAKEEiesRVAKASGMLSLEPYLARRPAE-----------LSGGQRQRVAIGRAIVREPEL 154
Cdd:TIGR00957 1366 PQDPVlfSGSLRMNLDPFSQYSDE---EVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 155 FLFDEPLSNLD--------AALRVQ----TRLEIArlHRsLKATMIYVthdqveamtladKIVVMNAGAIEQIGSPMEL 221
Cdd:TIGR00957 1443 LVLDEATAAVDletdnliqSTIRTQfedcTVLTIA--HR-LNTIMDYT------------RVIVLDKGEVAEFGAPSNL 1506
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-306 |
2.76e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCG--KSTLLRSI----AGLEDVTSGTVLINGKDVTVT----PP 72
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*gpdAGRRPWRF*TWCANRRALRRTig*hRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 73 AKRGISMVFQSyalyphltvKDNMGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREP 152
Cdd:NF000106 93 VR*GRRESFSG---------RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 153 ELFLFDEPLSNLDAALRVQTRLEIARLHRSlKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIGSPMELYNRpanvfVGG 232
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK-----VGG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 233 figspqmnlipaekleqggaKTIGIRPEHIT-LSREQGTwaakvvhVEHLGADTIIYLESDHT-GLLTVRLFGEHQ 306
Cdd:NF000106 238 --------------------RTLQIRPAHAAeLDRMVGA-------IAQAGLDGIAGATADHEdGVVNVPIVSDEQ 286
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-210 |
2.87e-09 |
|
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: 57.91 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 22 IDLEVKDGEFVIFVGPSGCGKSTLLRSIAGL-EDVTSGTVLINGKDVTVTPPAK---RGISMVFQS---YALYPHLTVKD 94
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 95 NMGL-------GLKQAGTAKEE--IESRVAKASgMLSLEPYLArrPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:TIGR02633 359 NITLsvlksfcFKMRIDAAAELqiIGSAIQRLK-VKTASPFLP--IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494968020 166 aalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAG 210
Cdd:TIGR02633 436 ----VGAKYEIYKLINQLAQegvAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-212 |
5.40e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 26 VKDGEFVIFVGPSGCGKSTLLRSIAGL-EDVTSGTVLINGKDVTVTPPA---KRGISMVFQS---YALYPHLTVKDNMGL 98
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVGKNITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 99 G-LKQ------------AGTAKEEIES-RVAKASGMLSLepylarrpAELSGGQRQRVAIGRAIVREPELFLFDEPLSNL 164
Cdd:PRK13549 365 AaLDRftggsriddaaeLKTILESIQRlKVKTASPELAI--------ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 165 DaalrVQTRLEIARLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK13549 437 D----VGAKYEIYKLINQLVQqgvAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-229 |
6.66e-09 |
|
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: 55.69 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVTVTP--PAKRGISMVFQSYALYPHlTVKDN 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILFSG-SIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 96 MGLGLK-QAGTAKEEIEsrVAKASGMLS-----LEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALR 169
Cdd:cd03288 115 LDPECKcTDDRLWEALE--IAQLKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494968020 170 --VQTRLEIARLHRslkaTMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVF 229
Cdd:cd03288 193 niLQKVVMTAFADR----TVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-165 |
2.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 36 GPSGCGKSTLLRSIAGLEDVTSGTVLIngKDVTVTPPAKRGISMVFQSYALYPHLTVKDNMGLGLKQAGTAkeeieSRVA 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA-----ETLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 494968020 116 KASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLD 165
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-165 |
4.37e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 7 KSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLInGKDVTvtppakrgISMVFQSY-A 85
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK--------LAYVDQSRdA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 86 LYPHLTVKDNMGLGLKQAGTAKEEIESRVakasgmlslepYLAR----------RPAELSGGQRQRVAIGRAIVREPELF 155
Cdd:PRK11819 399 LDPNKTVWEEISGGLDIIKVGNREIPSRA-----------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|
gi 494968020 156 LFDEPLSNLD 165
Cdd:PRK11819 468 LLDEPTNDLD 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
7.08e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTvlingkdVTVTPPAKRGISMVFQS 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSENANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 84 YALYPHLTVKDNMGlglkQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSN 163
Cdd:PRK15064 393 YDFENDLTLFDWMS----QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 164 LDaalrvqtrLE-IARLHRSL---KATMIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:PRK15064 469 MD--------MEsIESLNMALekyEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-216 |
7.18e-08 |
|
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: 51.55 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 8 SIRKAYGTHdvLKGIDLEVKDGEFVIFVGPSGCGKSTLLRsiAGLEdvTSGTVLINGkdvTVTPPAKRGISMVFQSYALY 87
Cdd:cd03238 2 TVSGANVHN--LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLIS---FLPKFSRNKLIFIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 88 phltvkdNMGLGlkqagtakeeiesrvakasgMLSLEpylaRRPAELSGGQRQRVAIGRAIVREPE--LFLFDEPLSNLD 165
Cdd:cd03238 73 -------DVGLG--------------------YLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494968020 166 AALRVQTRLEIARLhRSLKATMIYVTHDqVEAMTLADKIVVMNAGAIEQIG 216
Cdd:cd03238 122 QQDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGG 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-231 |
1.37e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDVtvtppAKRGI-------SMVFQSYALYPHl 90
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI-----SKFGLmdlrkvlGIIPQAPVLFSG- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 91 TVKDNMG-LGLKQAGTAKEEIESRVAK---ASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPlsnlDA 166
Cdd:PLN03130 1328 TVRFNLDpFNEHNDADLWESLERAHLKdviRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEA----TA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 167 ALRVQTRLEIARLHR-SLKA-TMIYVTHdQVEAMTLADKIVVMNAGAIEQIGSPMELYNRPANVFVG 231
Cdd:PLN03130 1404 AVDVRTDALIQKTIReEFKScTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-212 |
1.77e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 18 VLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLE--DVTSGTVLINGKDV---TVTPPAKRGISMVFQ---SYALYPH 89
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVdvsTVSDAIDAGLAYVTEdrkGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 90 LTVKDNMGL----GLKQAGTAKEEIESRVA---------KASGMLSlepylarRPAELSGGQRQRVAIGRAIVREPELFL 156
Cdd:NF040905 355 DDIKRNITLanlgKVSRRGVIDENEEIKVAeeyrkkmniKTPSVFQ-------KVGNLSGGNQQKVVLSKWLFTDPDVLI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494968020 157 FDEPLSNLDaalrVQTRLEIARLHRSLKAT---MIYVTHDQVEAMTLADKIVVMNAGAI 212
Cdd:NF040905 428 LDEPTRGID----VGAKYEIYTIINELAAEgkgVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-215 |
2.34e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKDV---TVTPPAKRGISMVFQ---SYALYPHLTV 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 93 KDNM----------GLGLKQAGTAKEEIESRVakaSGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:PRK10982 344 GFNSlisnirnyknKVGLLDNSRMKSDTQWVI---DSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 163 NLDAALRVQTRLEIARLHRSLKAtMIYVTHDQVEAMTLADKIVVMNAGAIEQI 215
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKKDKG-IIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-204 |
3.14e-07 |
|
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: 49.29 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 29 GEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLIngkdvtvtppakrgISMvfqsyalyphltvkdnmglglkqagtake 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDG----------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 109 eieSRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALRVQTRLEI-----ARLHRSL 183
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180
....*....|....*....|.
gi 494968020 184 KATMIYVTHDQVEAMTLADKI 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRR 136
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-197 |
3.19e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 13 YGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAG------LEDVT-------SGTVLINGK------------DV 67
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrrgSGETIWDIKkhigyvssslhlDY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 68 TVTPPAKRGI-SMVFQSYALYPhlTVKDnmglglKQAGTAKEEIEsrvakasgMLSLEPYLARRP-AELSGGQRQRVAIG 145
Cdd:PRK10938 350 RVSTSVRNVIlSGFFDSIGIYQ--AVSD------RQQKLAQQWLD--------ILGIDKRTADAPfHSLSWGQQRLALIV 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494968020 146 RAIVREPELFLFDEPLSNLDAALRVQTRLEIARLHRSLKATMIYVTHDQVEA 197
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-192 |
5.66e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.90 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 25 EVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGtvlingkdvTVTPPAKRGISMVFQSyalyPHLTVkdnmglglkqaG 104
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---------RLTKPAKGKLFYVPQR----PYMTL-----------G 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 105 TAKEEI----ESRVAKASGM-----------LSLEPYLARRPA---------ELSGGQRQRVAIGRAIVREPELFLFDEP 160
Cdd:TIGR00954 530 TLRDQIiypdSSEDMKRRGLsdkdleqildnVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 494968020 161 LSnldaALRVQTRLEIARLHRSLKATMIYVTH 192
Cdd:TIGR00954 610 TS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-268 |
1.06e-06 |
|
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: 50.29 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 2 GSLQLKSIRKAY--GTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDvTSGTVLING------------KDV 67
Cdd:TIGR01271 1216 GQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvtlqtwrKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 68 TVTPPAKRGISMVFQSyALYPHLTVKDnmglglkqagtakEEIeSRVAKASGMLS--------LEPYLARRPAELSGGQR 139
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRK-NLDPYEQWSD-------------EEI-WKVAEEVGLKSvieqfpdkLDFVLVDGGYVLSNGHK 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 140 QRVAIGRAIVREPELFLFDEPLSNLDAalrvqTRLEIARlhRSLK-----ATMIYVTHdQVEAMTLADKIVVMNAGAIEQ 214
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDP-----VTLQIIR--KTLKqsfsnCTVILSEH-RVEALLECQQFLVIEGSSVKQ 1431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 494968020 215 IGSPMELYNRpANVFVGGFIGSPQMNLIPAEKLEQGGAKTigiRPEhITLSREQ 268
Cdd:TIGR01271 1432 YDSIQKLLNE-TSLFKQAMSAADRLKLFPLHRRNSSKRKP---QPK-ITALREE 1480
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-182 |
2.90e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 1 MGSLQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGledvtsGTVLINGKdvtVTPPAKRGISMV 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG------ELPLLSGE---RQSQFSHITRLS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 81 FQSYALYPHLTVKDN----MGLGLKQAG-TAKEEI------ESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIV 149
Cdd:PRK10938 72 FEQLQKLVSDEWQRNntdmLSPGEDDTGrTTAEIIqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALM 151
|
170 180 190
....*....|....*....|....*....|...
gi 494968020 150 REPELFLFDEPLSNLDAALRVQTRLEIARLHRS 182
Cdd:PRK10938 152 SEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-162 |
2.94e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 16 HDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtvtppakrgISMVFQSYALYPHLTVKDN 95
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 96 MGLGLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLS 162
Cdd:PRK13545 106 IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
111-192 |
3.30e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 111 ESRVAKASGMLSLEPYLARRPAE-LSGGQRQRVAIGRAIVREPELFLFDEPLSNLD--AALRVQTRLeiarlhrsLK--A 185
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDlhAVLWLETYL--------LKwpK 392
|
....*..
gi 494968020 186 TMIYVTH 192
Cdd:PLN03073 393 TFIVVSH 399
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
9-211 |
4.50e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 9 IRKAYgTHDvLKGIDLEVKDGEFVIFVGPSGCGKSTL----------LRSIAGLE-------------DVTSgtvlINGK 65
Cdd:cd03270 3 VRGAR-EHN-LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSayarqflgqmdkpDVDS----IEGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 66 DVTVTPPAKRGismvfqsyALYPHLTV------KDNMGLGLKQAGTaKEEIESRVAKASGMLSLEpylaRRPAELSGGQR 139
Cdd:cd03270 77 SPAIAIDQKTT--------SRNPRSTVgtvteiYDYLRLLFARVGI-RERLGFLVDVGLGYLTLS----RSAPTLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494968020 140 QRVAIGRAIVREPE--LFLFDEPLSNLDAalRVQTRLeIARLH--RSLKATMIYVTHDQvEAMTLADKIVVMNAGA 211
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHP--RDNDRL-IETLKrlRDLGNTVLVVEHDE-DTIRAADHVIDIGPGA 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-211 |
7.40e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKAYGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTS--GTVLINGKDV---TVTPPAKRGIS 78
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 79 MVFQSYALYPHLTVKDNMGLGLKQAGTAKEEIESRVAKASGMLS---LEPYLARRPAELSGGQRQRVAIGRAIVREPELF 155
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAkvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494968020 156 LFDEPLSNLD----AALrvqtrLEiarLHRSLKA---TMIYVTHDQVEAMTLADKIVVMNAGA 211
Cdd:NF040905 162 ILDEPTAALNeedsAAL-----LD---LLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-216 |
3.53e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVLINGKdvtvtppakrgISMVFQSYALYPHLTVKDNMGL 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 99 GLKQAGTAKEEIESRVAKASGMLSLEPYLARRPAELSGGQRQRVAIGRAIVREPELFLFDEPLSNLDAALrVQTRLEIAR 178
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF-AQKCLDKIY 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 494968020 179 LHRSLKATMIYVTHDQVEAMTLADKIVVMNAGAIEQIG 216
Cdd:PRK13546 188 EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
28-207 |
3.79e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 28 DGEFVIFVGPSGCGKSTLLRSIAgledvtsgtvlingkdvtvtppakrgismvfqsyalyphltvkdnMGLGLKQAGTAK 107
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------------------------------------------LALGGAQSATRR 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 108 EEIESRvAKASGMLSLEPYLARrpAELSGGQRQRVAI-----GRAIVREPeLFLFDEPLSNLDaALRVQTRLEIARLHRS 182
Cdd:cd03227 55 RSGVKA-GCIVAAVSAELIFTR--LQLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLD-PRDGQALAEAILEHLV 129
|
170 180
....*....|....*....|....*
gi 494968020 183 LKATMIYVTHDQvEAMTLADKIVVM 207
Cdd:cd03227 130 KGAQVIVITHLP-ELAELADKLIHI 153
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-205 |
1.60e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 4 LQLKSIRKaygTHDVLKgIDLevkDGEFVIFVGPSGCGKSTLL---------------RSIAGLEDV-TSGTV------- 60
Cdd:cd03240 4 LSIRNIRS---FHERSE-IEF---FSPLTLIVGQNGAGKTTIIealkyaltgelppnsKGGAHDPKLiREGEVraqvkla 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 61 --LINGKDVTVTppakRGISMVfqSYALYPHltvkdnmglglkqagtaKEEIESrvakasgmlslepYLARRPAELSGGQ 138
Cdd:cd03240 77 feNANGKKYTIT----RSLAIL--ENVIFCH-----------------QGESNW-------------PLLDMRGRCSGGE 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494968020 139 RQ------RVAIGRAI-VREPELFLfDEPLSNLDAALRVQTRLEIARLHRSLKA-TMIYVTHDQvEAMTLADKIV 205
Cdd:cd03240 121 KVlasliiRLALAETFgSNCGILAL-DEPTTNLDEENIEESLAEIIEERKSQKNfQLIVITHDE-ELVDAADHIY 193
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-262 |
1.66e-04 |
|
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: 38.72 E-value: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 494968020 235 GSPQMNLIPAE-------------------------KLEQGGAKTIGIRPEHI 262
Cdd:pfam17912 1 GSPPMNFLPATvvedgllvlgggvtlplpegqvlalKLYVGKEVILGIRPEHI 53
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-214 |
2.09e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 3 SLQlksIRKayGTHDVLKGIDLEVKDGEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTVL---------INGKDVTVTPPA 73
Cdd:PRK10636 6 SLQ---IRR--GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 74 krgISMVFQSYALYPHLTVK------DNMG---------LGLKQAGTakeeIESRVAKA-SGMLSLEPYLARRPAELSGG 137
Cdd:PRK10636 81 ---LEYVIDGDREYRQLEAQlhdaneRNDGhaiatihgkLDAIDAWT----IRSRAASLlHGLGFSNEQLERPVSDFSGG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 138 QRQRVAIGRAIVREPELFLFDEPLSNLDaaLRVQTRLEiaRLHRSLKATMIYVTHDQVEAMTLADKIVvmnagAIEQ 214
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIWLE--KWLKSYQGTLILISHDRDFLDPIVDKII-----HIEQ 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-211 |
2.12e-04 |
|
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: 43.08 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494968020 126 YLARRPAELSGGQRQRVA----IGRAIVrePELFLFDEP---LSNLDAALRVQTrleIARLhRSLKATMIYVTHDQvEAM 198
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRlatqIGSGLT--GVLYVLDEPsigLHQRDNRRLINT---LKRL-RDLGNTLIVVEHDE-DTI 553
|
90
....*....|...
gi 494968020 199 TLADKIVVMNAGA 211
Cdd:TIGR00630 554 RAADYVIDIGPGA 566
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-45 |
3.12e-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: 39.23 E-value: 3.12e-03
10 20
....*....|....*....|....*..
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTL 45
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
133-204 |
3.49e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 3.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494968020 133 ELSGGQRQRVAIGR--AIVR-EPELF-LFDEplsnLDAALRVQTRLEIARLHRSL-KATMIYVTHDQVEAMTLADKI 204
Cdd:cd03272 158 QLSGGQKSLVALALifAIQKcDPAPFyLFDE----IDAALDAQYRTAVANMIKELsDGAQFITTTFRPELLEVADKF 230
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-45 |
3.78e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 3.78e-03
10 20
....*....|....*....|....*..
gi 494968020 19 LKGIDLEVKDGEFVIFVGPSGCGKSTL 45
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
21-60 |
8.70e-03 |
|
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: 36.99 E-value: 8.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 494968020 21 GIDlEVKD---GEFVIFVGPSGCGKSTLLRSIAGLEDVTSGTV 60
Cdd:cd01854 75 GLD-ELREllkGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| |
