|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-376 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 605.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIA 80
Cdd:COG3839 1 MASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANK 240
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND----------GRIQQVGTPEELYDRPANL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 241 FVAGFIGSPAMNFFEVVVKDGQIISeDGLDIAIPEGqakmleAAGYKDKKVIFGIRPEDISsnqiVHDTYPNAnVTAEVL 320
Cdd:COG3839 229 FVAGFIGSPPMNLLPGTVEGGGVRL-GGVRLPLPAA------LAAAAGGEVTLGIRPEHLR----LADEGDGG-LEATVE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 321 VSELLGSETMLYVKLGQTEFASRVDARDFHNPGEKVSLTFNVAKGHFFDLETEQAI 376
Cdd:COG3839 297 VVEPLGSETLVHVRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-372 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 519.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIA 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMsatknpqgNGtiGKIEQVGSPQELYNLPANK 240
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVM--------NG--GVAEQIGTPVEVYEKPAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 241 FVAGFIGSPAMNFFEVVVKDGQIISEDGLDIAIPEGQAKmleaAGYKDKKVIFGIRPEDIssnqivHDTYPNANVTAEVL 320
Cdd:PRK11650 230 FVASFIGSPAMNLLDGRVSADGAAFELAGGIALPLGGGY----RQYAGRKLTLGIRPEHI------ALSSAEGGVPLTVD 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 321 VSELLGSETMLYVKLGQTEFASRVDARDFHNPGEKVSLTFNVAKGHFFDLET 372
Cdd:PRK11650 300 TVELLGADNLAHGRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADT 351
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-368 |
1.66e-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: 441.46 E-value: 1.66e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIA 80
Cdd:COG3842 3 MPALELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANK 240
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND----------GRIEQVGTPEEIYERPATR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 241 FVAGFIGSpaMNFFEVVVKDGQ--IISEDGLDIAIPEGqakmleAAGYKDKKVIFGIRPEDISsnqiVHDTYPNANVTAE 318
Cdd:COG3842 231 FVADFIGE--ANLLPGTVLGDEggGVRTGGRTLEVPAD------AGLAAGGPVTVAIRPEDIR----LSPEGPENGLPGT 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 501958613 319 VLVSELLGSETMLYVKLGQ-TEFASRVDARDFHN--PGEKVSLTFNVAKGHFF 368
Cdd:COG3842 299 VEDVVFLGSHVRYRVRLGDgQELVVRVPNRAALPlePGDRVGLSWDPEDVVVL 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-335 |
2.21e-151 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 431.76 E-value: 2.21e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIA 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANK 240
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA----------GRVAQVGKPLELYHYPANR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 241 FVAGFIGSPAMNFFEVVVKDgqiISEDGLDIAIPEGQAKMLEAAG---YKDKKVIFGIRPEDISSNQIvhdtypnANVT- 316
Cdd:PRK11000 229 FVAGFIGSPKMNFLPVKVTA---TAIEQVQVELPNRQQVWLPVEGrgvQVGANMSLGIRPEHLLPSDI-------ADVTl 298
|
330 340
....*....|....*....|
gi 501958613 317 -AEVLVSELLGSETMLYVKL 335
Cdd:PRK11000 299 eGEVQVVEQLGNETQIHIQI 318
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-228 |
1.06e-137 |
|
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: 390.85 E-value: 1.06e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND----------GQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-364 |
7.52e-119 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 348.29 E-value: 7.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN-DKSPKDRDIAM 81
Cdd:COG1118 2 SIEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKF 241
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ----------GRIEQVGTPDEVYDRPATPF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 242 VAGFIGspAMNFFEVVVKDGQIISeDGLDIAIPEGQAkmleaagykDKKVIFGIRPEDIssnQIVHDTYPNANVTAEVLV 321
Cdd:COG1118 230 VARFLG--CVNVLRGRVIGGQLEA-DGLTLPVAEPLP---------DGPAVAGVRPHDI---EVSREPEGENTFPATVAR 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 501958613 322 SELLGSETMLYVKLGQT-------EFASRVDARDFHNPGEKVSLTFNVAK 364
Cdd:COG1118 295 VSELGPEVRVELKLEDGegqpleaEVTKEAWAELGLAPGDPVYLRPRPAR 344
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-228 |
2.78e-114 |
|
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: 331.41 E-value: 2.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE----------GRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-247 |
4.13e-111 |
|
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: 324.19 E-value: 4.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVA 243
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK----------GKIQQIGTPEEIYEEPANRFVA 228
|
....
gi 501958613 244 GFIG 247
Cdd:cd03300 229 DFIG 232
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-368 |
2.50e-109 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 324.26 E-value: 2.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 2 VELNLKHIYKKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS-----P 74
Cdd:NF040933 1 VTVRVENVTKIFKkgKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGkiivpP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 75 KDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 155 KVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRI-VIMSatknpqgngtiGKIEQVGSPQEL 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAgVINN-----------GKFQQVGKPEEI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 234 YNLPANKFVAGFIGSpaMNFFEVVVKDGQIIseDGLDIAIPegqakmLEAAGYKDKKVIFGIRPEDIS---SNQIVHDTY 310
Cdd:NF040933 230 YDNPANIFVARLIGD--INLLEGKVEEEGLV--DGNDLKIP------LPNPKLEAGEVIIGIRPEDIDiseSDMRLPPGF 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 311 PNANVtAEVLVSELLGSETMLYVK---LGQTEFasRVDARDFHNPGEKVSLTFNVAKGHFF 368
Cdd:NF040933 300 VEVGK-GRVKVSSYAGGVFRVVVSpidDDSIEI--IVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-359 |
5.64e-108 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 321.51 E-value: 5.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVA 243
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD----------GRIEQDGTPREIYEEPKNLFVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 244 GFIGSpaMNFFEVVVKdgQIISEDGLDIAIpEGQAKML--EAAGYKDKKVIFGIRPEDISSNQIVHDTYPNAnVTAEVLV 321
Cdd:PRK09452 243 RFIGE--INIFDATVI--ERLDEQRVRANV-EGRECNIyvNFAVEPGQKLHVLLRPEDLRVEEINDDEHAEG-LIGYVRE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 501958613 322 SELLGSETMLYVKL--GQTEFAS---RVDARDF-HNPGEKVSLT 359
Cdd:PRK09452 317 RNYKGMTLDSVVELenGKMVMVSeffNEDDPDFdHSLGQKVAVT 360
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-335 |
1.07e-106 |
|
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: 317.36 E-value: 1.07e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIA 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT--ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANK 240
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH----------GVIEQVGTPQEIYRHPATP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 241 FVAGFIGSpaMNFFEVVVKDGQIISEDGLDIAIPEGQAKMLEAagykdkkVIFGIRPEDIssnqIVHDTYPNANV-TAEV 319
Cdd:TIGR03265 230 FVADFVGE--VNWLPGTRGGGSRARVGGLTLACAPGLAQPGAS-------VRLAVRPEDI----RVSPAGNAANLlLARV 296
|
330
....*....|....*.
gi 501958613 320 LVSELLGSETMLYVKL 335
Cdd:TIGR03265 297 EDMEFLGAFYRLRLRL 312
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-363 |
3.40e-98 |
|
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: 294.79 E-value: 3.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRV 116
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 117 KEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQ 196
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 197 TEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGFIGSpaMNFFEVVVKDGQiisEDGLDIAIPEG 276
Cdd:TIGR01187 162 EEAMTMSDRIAIMRK----------GKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERK---SEQVVLAGVEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 277 QAKML--EAAGYKDKKVIFGIRPEDISSNQIVHDTYPNAnVTAEVLVSELLGSETMLYVKL--GQTEFAS---RVDARDF 349
Cdd:TIGR01187 227 RRCDIytDVPVEKDQPLHVVLRPEKIVIEEEDEANSSNA-IIGHVIDITYLGMTLEVHVRLetGQKVLVSeffNEDDPHM 305
|
330
....*....|....*
gi 501958613 350 -HNPGEKVSLTFNVA 363
Cdd:TIGR01187 306 sPSIGDRVGLTWHPG 320
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-304 |
1.07e-94 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 286.62 E-value: 1.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVA 243
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK----------GKIMQIGSPQELYRQPASRFMA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 244 GFIGSPamNFFEVVVKDGQiISEDGLDIAIPEGQakmleAAGYKDKKVIFGIRPEDISSNQ 304
Cdd:PRK11432 235 SFMGDA--NIFPATLSGDY-VDIYGYRLPRPAAF-----AFNLPDGECTVGVRPEAITLSE 287
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-248 |
1.76e-94 |
|
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: 281.92 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMV 82
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYK----KDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPA 238
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK----------GRIEQVGTPDEVYDHPA 229
|
250
....*....|
gi 501958613 239 NKFVAGFIGS 248
Cdd:cd03296 230 SPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
4.28e-94 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 281.98 E-value: 4.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPkdrD 78
Cdd:COG1116 5 APALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtkNPqgnGTIGKIEQVGSP 230
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA--RP---GRIVEEIDVDLP 228
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-368 |
4.50e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 272.33 E-value: 4.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYpntTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:NF040840 2 IRIENLSKDW---KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:NF040840 79 QNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMsatKNpqgngtiGKIEQVGSPQELYNLPANKFVA 243
Cdd:NF040840 159 SALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIM---LN-------GRLSQVGDVREVFRRPKNEFVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 244 GFIGspAMNFFEVVVK---DGQIISEDGLDIAIPEgqakmlEAAGykdkKVIFGIRPEDIS-SNQIVHDTYPNAnVTAEV 319
Cdd:NF040840 229 RFVG--FENIIEGVAEkggEGTILDTGNIKIELPE------EKKG----KVRIGIRPEDITiSTEKVKTSARNE-FKGKV 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 320 LVSELLGSETMLYVKLGQT--EFASRVDARDFH-NPGEKVSLTFNVAKGHFF 368
Cdd:NF040840 296 EEIEDLGPLVKLTLDVGIIlvAFITRSSFLDLEiNEGKEVYASFKASAVHVF 347
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-228 |
4.56e-89 |
|
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: 267.42 E-value: 4.56e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPN--TTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPkdrDIAM 81
Cdd:cd03293 1 LEVRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSATknpqgNGTIGKIEQVG 228
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSAR-----PGRIVAEVEVD 219
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-248 |
2.01e-88 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 268.88 E-value: 2.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RD 78
Cdd:COG1125 1 MIEF--ENVTKRYPDGTV-AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGL--TEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNL 236
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMRE----------GRIVQYDTPEEILAN 227
|
250
....*....|..
gi 501958613 237 PANKFVAGFIGS 248
Cdd:COG1125 228 PANDFVADFVGA 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-247 |
1.45e-85 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 259.35 E-value: 1.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 9 IYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYAL 88
Cdd:TIGR00968 6 ISKRFGSFQ--ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 YPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:TIGR00968 84 FKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 169 KLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGFIG 247
Cdd:TIGR00968 164 KVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN----------GKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-249 |
6.43e-82 |
|
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: 250.30 E-value: 6.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTtHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGL--TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPAN 239
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN----------GEIVQVGTPDEILRSPAN 229
|
250
....*....|
gi 501958613 240 KFVAGFIGSP 249
Cdd:cd03295 230 DFVAEFVGAD 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-342 |
7.96e-82 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 254.76 E-value: 7.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 19 YAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNM 98
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 179 AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGFIGSpaMNFFEVVV 258
Cdd:PRK11607 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR----------GKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEGVL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 259 K----DGQIISEDGLDIAIpegqaKMLEAAGYKDK-KVIFGIRPEDIS-SNQIVHDTYPNAnvTAEVLVSELLGSETMLY 332
Cdd:PRK11607 261 KerqeDGLVIDSPGLVHPL-----KVDADASVVDNvPVHVALRPEKIMlCEEPPADGCNFA--VGEVIHIAYLGDLSIYH 333
|
330
....*....|
gi 501958613 333 VKLGQTEFAS 342
Cdd:PRK11607 334 VRLKSGQMIS 343
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-247 |
9.25e-82 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 249.56 E-value: 9.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMAF 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 GLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAK 180
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 181 IHRRIGSTTIYVTHDQTEAMTLADRIVIMsatKNpqgngtiGKIEQVGSPQELYNLPANKFVAGFIG 247
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIM---LN-------GKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-263 |
1.51e-75 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 237.67 E-value: 1.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMAFGL 102
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 103 KL----RKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:PRK10851 100 TVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 179 AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSatknpQGNgtigkIEQVGSPQELYNLPANKFVAGFIGSpaMNFFEVVV 258
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMS-----QGN-----IEQAGTPDQVWREPATRFVLEFMGE--VNRLQGTI 247
|
....*
gi 501958613 259 KDGQI 263
Cdd:PRK10851 248 RGGQF 252
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
3.08e-71 |
|
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: 220.52 E-value: 3.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS----PKDRDI 79
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYPHMTVYDNMAFGlklrkykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-246 |
5.68e-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: 217.90 E-value: 5.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD------RDIAMVFQNYALYPHMT 93
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 VYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 174 MRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGFI 246
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD----------GRLVQVGTPEEILTNPANDYVREFF 261
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-247 |
1.87e-68 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 219.72 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSP------KDRDIAMVFQNYALYPHMT 93
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 VYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 174 MRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGFIG 247
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKA----------GEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
7.58e-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: 213.12 E-value: 7.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPN--TTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD--- 78
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 ---IAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMtLADRIVIMS 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELR 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-209 |
1.35e-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: 209.84 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIK---DKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDK------SPKDRDIAMVFQNYAL 88
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlPPQQRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 YPHMTVYDNMAFGLKLRKYKKDDIdrRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:cd03297 87 FPHLNVRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501958613 169 KLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-234 |
1.10e-65 |
|
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: 207.96 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNyalyP-----HMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1122 80 VFQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD----------GRIVADGTPREVF 222
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-246 |
2.44e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 212.27 E-value: 2.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD------RDIAMVFQNYALYPHMT 93
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 VYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:COG4175 122 VLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 174 MRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMsatKNpqgngtiGKIEQVGSPQELYNLPANKFVAGFI 246
Cdd:COG4175 202 MQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM---KD-------GRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-247 |
6.23e-65 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 206.14 E-value: 6.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyaveDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFG----LKLRKYKKddidRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGlrpgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPAN 239
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD----------GRIAADGPTAALLDGEPP 223
|
....*...
gi 501958613 240 KFVAGFIG 247
Cdd:COG3840 224 PALAAYLG 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-210 |
3.29e-64 |
|
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: 203.47 E-value: 3.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVF 83
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNyalyP-HM----TVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03225 82 QN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-210 |
3.37e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 204.12 E-value: 3.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVEL-NLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD- 78
Cdd:COG1136 4 LLELrNLTKSYGTGEGEVT-ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 -----IAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:COG1136 83 lrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQtEAMTLADRIVIMS 210
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLR 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
2.18e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.90 E-value: 2.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD-IAMV 82
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 163 LSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDK----------GRIVADGTPDEL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-260 |
8.69e-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: 202.25 E-value: 8.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHiykKYPntthyaveDFDLDIK----DKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS--- 73
Cdd:COG4148 2 MLEVDFRL---RRG--------GFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSArgi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 74 ---PKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDrrVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAI 150
Cdd:COG4148 71 flpPHRRRIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 151 VRDAKVFLMDEPLSNLDAKLrvsmRAEI----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQ 226
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLAR----KAEIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQ----------GRVVA 214
|
250 260 270
....*....|....*....|....*....|....
gi 501958613 227 VGSPQELYNLPANKFVAGfiGSPAMNFFEVVVKD 260
Cdd:COG4148 215 SGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAA 246
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-235 |
1.76e-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: 203.21 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RDI 79
Cdd:COG1123 265 NLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrRRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQN--YALYPHMTVYDNMAFGLKLRK-YKKDDIDRRVKEAAEILGL-TEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:COG1123 345 QMVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 156 VFLMDEPLSNLDaklrVSMRAEI----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:COG1123 425 LLILDEPTSALD----VSVQAQIlnllRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD----------GRIVEDGPTE 490
|
....
gi 501958613 232 ELYN 235
Cdd:COG1123 491 EVFA 494
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-244 |
8.78e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 193.93 E-value: 8.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPkDRd 78
Cdd:COG4525 1 MSMLTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 iAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtkNPqgngtiGKIEQVgspqelYNLPA 238
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSP--GP------GRIVER------LELDF 223
|
....*..
gi 501958613 239 NK-FVAG 244
Cdd:COG4525 224 SRrFLAG 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-246 |
1.95e-59 |
|
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: 192.50 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTTHYavEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD-- 78
Cdd:COG1127 5 MIEV--RNLTKSFGDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 ---IAMVFQNYALYPHMTVYDNMAFGLK-LRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG1127 81 rrrIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 155 KVFLMDEPLSNLDAklrVSMRA---EIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:COG1127 161 EILLYDEPTAGLDP---ITSAVideLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD----------GKIIAEGTPE 227
|
250
....*....|....*
gi 501958613 232 ELYNLPaNKFVAGFI 246
Cdd:COG1127 228 ELLASD-DPWVRQFL 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-239 |
7.21e-58 |
|
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: 188.47 E-value: 7.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDI 79
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNY--ALYPHMTVYDNMAFGLKLrkYKKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRI--HGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLDaklrVSMRAEI----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:COG1124 160 LLLDEPTSALD----VSVQAEIlnllKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN----------GRIVEELTVAD 225
|
....*..
gi 501958613 233 LYNLPAN 239
Cdd:COG1124 226 LLAGPKH 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-211 |
1.26e-55 |
|
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: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RD 78
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFG-------LK--LRKYKKDDIDRrVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRA 149
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 150 IVRDAKVFLMDEPLSNLDAKL-RVSMRAeIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-237 |
1.05e-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: 180.08 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNT--THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-- 76
Cdd:cd03258 1 MIEL--KNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 ---RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:cd03258 79 karRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK----------GEVVEEGTVEEV 228
|
....
gi 501958613 234 YNLP 237
Cdd:cd03258 229 FANP 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
2.00e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.42 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDkSPKD---- 76
Cdd:COG1126 1 MIEI--ENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 -RDIAMVFQNYALYPHMTVYDNMAFGL-KLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG1126 76 rRKVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 155 KVFLMDEPLSNLDAKlrvsMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:COG1126 156 KVMLFDEPTSALDPE----LVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDG----------GRIVEEGPPE 221
|
....*...
gi 501958613 232 ELYNLPAN 239
Cdd:COG1126 222 EFFENPQH 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-196 |
6.24e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 177.55 E-value: 6.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTtHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---- 76
Cdd:COG2884 1 MIRF--ENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 -RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:COG2884 78 rRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501958613 156 VFLMDEPLSNLDAKLRVS-MRAeIAKIHRRiGSTTIYVTHDQ 196
Cdd:COG2884 158 LLLADEPTGNLDPETSWEiMEL-LEEINRR-GTTVLIATHDL 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-246 |
1.80e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 176.82 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDI- 79
Cdd:PRK09493 1 MIEF--KNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 ---AMVFQNYALYPHMTVYDNMAFG-LKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK09493 77 qeaGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 156 VFLMDEPLSNLDAKLrvsmRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:PRK09493 157 LMLFDEPTSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDK----------GRIAEDGDPQV 222
|
250
....*....|....
gi 501958613 233 LYNLPANKFVAGFI 246
Cdd:PRK09493 223 LIKNPPSQRLQEFL 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-209 |
2.04e-53 |
|
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: 176.54 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---- 77
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 -DIAMVFQNY--ALYPHMTVYDNMAFGLKLRK--YKKDDIDRRVKEAAEILGLTE-FLERKPADLSGGQRQRVAMGRAIV 151
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
9.66e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.85 E-value: 9.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyaVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPhMTVYDNMAFGLKLRKYKKDdiDRRVKEAAEILGLTE-FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-209 |
1.03e-52 |
|
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: 173.87 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK----DRDI 79
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYPHMTVYDNMAFGL-KLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501958613 159 MDEPLSNLDAKlrvsMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03262 159 FDEPTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-213 |
1.13e-51 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 172.62 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNT--THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVnDKSPKDRdiAM 81
Cdd:NF040729 2 LKIQNISKTFINNkkENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEV-TKPGPDR--GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDK 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-250 |
1.18e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.27 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYP--NTTHYAVEDFDLDIKDKEfiVF--VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD 76
Cdd:COG1135 1 MIEL--ENLSKTFPtkGGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 -----RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIV 151
Cdd:COG1135 77 lraarRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 152 RDAKVFLMDEPLSNLDAK-----LRVsmraeIAKIHRRIGSTTIYVTHDqteaM----TLADRIVIMSAtknpqgngtiG 222
Cdd:COG1135 157 NNPKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLEN----------G 217
|
250 260
....*....|....*....|....*...
gi 501958613 223 KIEQVGSPQELYNLPANKFVAGFIGSPA 250
Cdd:COG1135 218 RIVEQGPVLDVFANPQSELTRRFLPTVL 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
1.24e-51 |
|
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: 171.92 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYavEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RDIA 80
Cdd:cd03261 3 LRGLTKSFGGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLK-LRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYD----------GKIVAEGTPEEL 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-249 |
5.28e-51 |
|
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: 170.99 E-value: 5.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLK-----LRKYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYphlglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE---- 232
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD----------GRIVAQGPPEEvltp 228
|
250 260
....*....|....*....|..
gi 501958613 233 -----LYNLPANKFVAGFIGSP 249
Cdd:COG1120 229 elleeVYGVEARVIEDPVTGRP 250
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-233 |
9.02e-51 |
|
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: 170.04 E-value: 9.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-DIAMV 82
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 163 LSNLDAKLRVSMRAEIAKiHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:COG4555 160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK----------GKVVAQGSLDEL 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-235 |
3.50e-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: 169.55 E-value: 3.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKkyPNTT--HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----R 77
Cdd:TIGR04521 5 NVSYIYQ--PGTPfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 DIAMVFQnyalYPHM-----TVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTE-FLERKPADLSGGQRQRVAMGRAIV 151
Cdd:TIGR04521 83 KVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK----------GKIVLDGTPR 228
|
....
gi 501958613 232 ELYN 235
Cdd:TIGR04521 229 EVFS 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-233 |
3.77e-50 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 167.74 E-value: 3.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYpnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDI-----SEGELKIDGEVVNDKSPKD-- 76
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 --RDIAMVFQNYALYPhMTVYDNMAFGLKLRKYK-KDDIDRRVKEAAEILGLTEFLERK--PADLSGGQRQRVAMGRAIV 151
Cdd:cd03260 79 lrRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIgsTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLN----------GRLVEFGPTE 225
|
..
gi 501958613 232 EL 233
Cdd:cd03260 226 QI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-238 |
4.14e-50 |
|
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: 175.48 E-value: 4.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIS---EGELKIDGEVVNDKSPKDR--D 78
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQN--YALYPhMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNL 236
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD----------GRIVEDGPPEEILAA 233
|
..
gi 501958613 237 PA 238
Cdd:COG1123 234 PQ 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-235 |
4.55e-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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 169.15 E-value: 4.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG-EVVNDKSPKD--RDIAMV 82
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEirKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNyalyPH-----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:TIGR04520 83 FQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAmTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNK----------GKIVAEGTPREIFS 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-233 |
6.68e-50 |
|
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: 166.91 E-value: 6.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG-EVVNDKSPKDRDIAMV 82
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 163 LSNLDAKLRVSMRAEIAKIhrRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSD----------GKLRCIGSPQEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-231 |
6.92e-50 |
|
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: 167.26 E-value: 6.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPkdrDIAMVFQNYALYPHMTVYDNMAF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 GLK--LRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501958613 179 AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMsaTKNPQGNgtIGKIEQVGSPQ 231
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVML--TNGPAAN--IGQILEVPFPR 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-209 |
1.30e-49 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 166.13 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMAFG- 101
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 ---LKLRKYKKddidRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:cd03298 96 spgLKLTAEDR----QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|.
gi 501958613 179 AKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-233 |
1.47e-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: 166.97 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RD 78
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFGL---------KLRKYKKDDIdRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRA 149
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 150 IVRDAKVFLMDEPLSNLDAKL-RVSMRAeIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKD----------GRIVFDG 227
|
....*
gi 501958613 229 SPQEL 233
Cdd:cd03256 228 PPAEL 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-211 |
1.78e-49 |
|
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: 165.88 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---- 76
Cdd:TIGR02673 1 MIEF--HNVSKAYPGGVA-ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 -RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:TIGR02673 78 rRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
2.11e-49 |
|
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: 176.95 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIA 80
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYpHMTVYDNMAFGlklrkykKDDIDR-RVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGR 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLRvsmraeiAKIHRRI-----GSTTIYVTHDqTEAMTLADRIVIMSAtknpqgngtiGK 223
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETE-------AIILENLrrllkGRTVIIIAHR-LSTIRLADRIIVLDK----------GR 686
|
250
....*....|
gi 501958613 224 IEQVGSPQEL 233
Cdd:COG2274 687 IVEDGTHEEL 696
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-238 |
7.56e-49 |
|
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: 168.37 E-value: 7.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDK------SPKDRDIAMVFQNYALYPHMTVYD 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFGLKlrkyKKDDIDRRVKEAA--EILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:TIGR02142 95 NLRYGMK----RARPSERRISFERviELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 175 RAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPA 238
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED----------GRVAAAGPIAEVWASPD 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-228 |
4.27e-48 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 162.34 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 24 FDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMAFG-- 101
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 --LKLRKYKKDdidrRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIA 179
Cdd:TIGR01277 97 pgLKLNAEQQE----KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501958613 180 KIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQ----------GKIKVVS 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-209 |
4.61e-47 |
|
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: 157.94 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-DIAMV 82
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMafglklrkykkddidrrvkeaaeilglteflerkpaDLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501958613 163 LSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAIL 168
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-238 |
2.45e-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: 160.60 E-value: 2.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED---ISEGELKIDGEVVNDKSPKD-- 76
Cdd:COG0444 2 LEVRNLKVYFPtrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 ----RDIAMVFQN-Y-ALYPHMTVYDNMAFGLKL-RKYKKDDIDRRVKEAAEILGLT---EFLERKPADLSGGQRQRVAM 146
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 147 GRAIVRDAKVFLMDEPLSNLDaklrVSMRAEI----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiG 222
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVAVMYA----------G 227
|
250
....*....|....*.
gi 501958613 223 KIEQVGSPQELYNLPA 238
Cdd:COG0444 228 RIVEEGPVEELFENPR 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-235 |
8.23e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 156.67 E-value: 8.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 24 FDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMAFG-- 101
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 --LKLRKYKKddidRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIA 179
Cdd:PRK10771 98 pgLKLNAAQR----EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 180 KIHRRIGSTTIYVTHDQTEAMTLADR-IVIMSatknpqgngtiGKIEQVGSPQELYN 235
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRsLVVAD-----------GRIAWDGPTDELLS 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-233 |
2.78e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.80 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 13 YPNTtHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYp 90
Cdd:COG1132 349 YPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 91 HMTVYDNMAFGlklrkykKDDIDR-RVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:COG1132 427 SGTIRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 159 MDEPLSNLDAklrvsmRAEiAKIHRRI-----GSTTIYVTH------DqteamtlADRIVIMSAtknpqgngtiGKIEQV 227
Cdd:COG1132 500 LDEATSALDT------ETE-ALIQEALerlmkGRTTIVIAHrlstirN-------ADRILVLDD----------GRIVEQ 555
|
....*.
gi 501958613 228 GSPQEL 233
Cdd:COG1132 556 GTHEEL 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-234 |
2.85e-45 |
|
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: 163.39 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 2 VELNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDI 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALyPHMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKPAD-----------LSGGQRQRVAMGR 148
Cdd:COG4988 414 AWVPQNPYL-FAGTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDqTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDD----------GRIVEQG 553
|
....*.
gi 501958613 229 SPQELY 234
Cdd:COG4988 554 THEELL 559
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
3.34e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 156.01 E-value: 3.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpKDRdiAMVF 83
Cdd:PRK11248 2 LQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER--GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLS 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-212 |
1.75e-44 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 152.64 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL--EDIS-EGELKIDGEVVNDKSPKDRDIAMVFQNYALYPHMTVYDN 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAFGLKlRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAE 177
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 501958613 178 I-AKIHRRiGSTTIYVTHDQTEAMtLADRIVIMSAT 212
Cdd:COG4136 176 VfEQIRQR-GIPALLVTHDEEDAP-AAGRVLDLGNW 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-209 |
2.75e-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: 150.61 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYpHMTVYDNMafglklrkykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDqTEAMTLADRIVIM 209
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVL 167
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
3.11e-44 |
|
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: 150.11 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHMTVYDNM 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERK----PADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-236 |
4.45e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 153.63 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNyalyPH-----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTlADRIVIMsatknpqgNGtiGKIEQVGSPQELYNL 236
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--------NK--GEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-235 |
2.90e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 151.74 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDI----A 80
Cdd:PRK13637 7 NLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQ--NYALYPHmTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLT--EFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK13637 87 LVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK----------GKCELQGTPREVFK 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-195 |
5.06e-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: 149.10 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTThYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVND----KSPK-DRDIA 80
Cdd:cd03292 3 FINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYlRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHD 195
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-238 |
7.74e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.81 E-value: 7.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RDIAMVFQN-YA-LYPHM 92
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 TVYDNMAFGLKL-RKYKKDDIDRRVKEAAEILGL-TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDakl 170
Cdd:COG4608 113 TVGDIIAEPLRIhGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD--- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 171 rVSMRAEI----AKIHRRIGSTTIYVTHDqteamtL------ADRIVIMsatknpqgngTIGKIEQVGSPQELYNLPA 238
Cdd:COG4608 190 -VSIQAQVlnllEDLQDELGLTYLFISHD------LsvvrhiSDRVAVM----------YLGKIVEIAPRDELYARPL 250
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
1.06e-42 |
|
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: 147.76 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG-EVVNDKSPKDRD-----I 79
Cdd:TIGR03608 1 LKNISKKFGD--KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqETPPLNSKKASKfrrekL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501958613 160 DEPLSNLDAKlrvsMRAEIAKIHRRI---GSTTIYVTHDqTEAMTLADRIV 207
Cdd:TIGR03608 159 DEPTGSLDPK----NRDEVLDLLLELndeGKTIIIVTHD-PEVAKQADRVI 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-234 |
1.12e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 150.27 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVEL-NLKhiYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--R 77
Cdd:PRK13650 4 IIEVkNLT--FKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 DIAMVFQNyalyPH-----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVR 152
Cdd:PRK13650 82 KIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 153 DAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEaMTLADRIVIMsatKNpqgngtiGKIEQVGSPQE 232
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM---KN-------GQVESTSTPRE 226
|
..
gi 501958613 233 LY 234
Cdd:PRK13650 227 LF 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
1.34e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpkdRDIA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR---RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPH--MTVYDNMAFGLK-----LRKYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMsatknpqgNGTI---GKIEQVGSP 230
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL--------NRGLvahGPPEEVLTP 228
|
...
gi 501958613 231 QEL 233
Cdd:COG1121 229 ENL 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-209 |
1.68e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 149.06 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpkdRDIAMVF 83
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKlrkykkDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-209 |
8.16e-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: 145.97 E-value: 8.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKY--PNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG-EVVNDKSPKDRDIA 80
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501958613 161 EPLSNLDAKLRVSMRaEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03266 162 EPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-245 |
9.87e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 150.95 E-value: 9.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD------RDIAMVFQNYALYPHMT 93
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 VYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 174 MRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGF 245
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN----------GEVVQVGTPDEILNNPANDYVRTF 264
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-213 |
1.94e-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: 144.54 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK-DRDIAMVFQNYALYPHMTVYDNMAF 100
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 GLKLRKYKKDDIDrrVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlrvsMRAEIAK 180
Cdd:COG4133 99 WAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA----GVALLAE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 501958613 181 I---HRRIGSTTIYVTHDQTEAmtLADRIVIMSATK 213
Cdd:COG4133 173 LiaaHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-213 |
3.81e-41 |
|
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: 142.00 E-value: 3.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVF 83
Cdd:cd00267 2 IENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QnyalyphmtvydnmafglklrkykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-233 |
9.22e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 151.07 E-value: 9.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 2 VELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDI 79
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYpHMTVYDNMAFGlklrkykKDDI-DRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMG 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 148 RAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDQTeAMTLADRIVIMSAtknpqgngtiGKIEQV 227
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLED----------GRIVEQ 550
|
....*.
gi 501958613 228 GSPQEL 233
Cdd:COG4987 551 GTHEEL 556
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.78e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.98 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNlkHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RD 78
Cdd:PRK13632 7 MIKVE--NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNyalyPH-----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK13632 85 IGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAmTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSE----------GKLIAQGKPKEI 229
|
..
gi 501958613 234 YN 235
Cdd:PRK13632 230 LN 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-226 |
4.96e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 142.07 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYpnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD------ 76
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 --RDIAMVFQNYALYPHMTVYDNM-AFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:COG4161 80 lrQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 154 AKVFLMDEPLSNLDAKLrvsmRAEIAKIHRRIGSTTI---YVTHDQTEAMTLADRIVIMSatknpqgNGTIgkIEQ 226
Cdd:COG4161 160 PQVLLFDEPTAALDPEI----TAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYME-------KGRI--IEQ 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-211 |
6.98e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 144.56 E-value: 6.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTT--HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-- 76
Cdd:PRK11153 1 MIEL--KNISKVFPQGGrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 ---RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK11153 79 karRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-209 |
8.42e-40 |
|
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: 141.04 E-value: 8.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIAMVFQNYALYPHMTVYD 96
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFGLKLRK----------YKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:cd03219 95 NVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501958613 167 DAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03219 175 NPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVL 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-235 |
2.73e-39 |
|
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: 140.13 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RD 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNM---AFGLK------LRKYKKDDIdRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRA 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 150 IVRDAKVFLMDEPLSNLDAKL-RVSMRAeIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTsKQVMDY-LKRINKEDGITVIINLHQVDLAKKYADRIVGLKA----------GEIVFDG 228
|
....*..
gi 501958613 229 SPQELYN 235
Cdd:TIGR02315 229 APSELDD 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-209 |
3.70e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.55 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RD--IA 80
Cdd:COG1129 5 LEMRGISKSFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRKYKKddIDRR--VKEAAEIL---GLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGL--IDWRamRRRARELLarlGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 156 VFLMDEPLSNLDAKlrvsmraEIAKIHRRI------GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1129 161 VLILDEPTASLTER-------EVERLFRIIrrlkaqGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-212 |
5.37e-39 |
|
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: 138.44 E-value: 5.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpkdRDIAMVFQNYAL---YPhMTV 94
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRSIdrdFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFGL-----KLRKYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:cd03235 88 RDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501958613 170 LRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAT 212
Cdd:cd03235 167 TQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-209 |
5.44e-39 |
|
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: 137.18 E-value: 5.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVF 83
Cdd:cd03214 2 VENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QnyalyphmtvydnmafglklrkykkddidrrvkeAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILL 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-209 |
5.96e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 139.40 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIAMVFQNYALYPHMTVYD 96
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFG-------------LKLRKYKKDD--IDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG0411 99 NVLVAaharlgrgllaalLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-233 |
9.58e-39 |
|
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: 137.89 E-value: 9.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 7 KHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG-EVVNDKSPKDRDIAMVFQN 85
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 86 YALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSN 165
Cdd:cd03265 82 LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 166 LDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH----------GRIIAEGTPEEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-226 |
8.58e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.91 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYpnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--------R 77
Cdd:PRK11124 5 LNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSdkairelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 DIAMVFQNYALYPHMTVYDNMAFG-LKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 157 FLMDEPLSNLDAKLrvsmRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMSatknpqgNGTIgkIEQ 226
Cdd:PRK11124 163 LLFDEPTAALDPEI----TAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYME-------NGHI--VEQ 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-209 |
2.29e-36 |
|
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: 131.56 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 12 KYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALY 89
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 pHMTVYDNMAFGLKLRKykkddiDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03245 91 -YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 159 MDEPLSNLDaklrvsMRAEIAKIHR----RIGSTTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03245 164 LDEPTSAMD------MNSEERLKERlrqlLGDKTLIIITH-RPSLLDLVDRIIVM 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-211 |
5.97e-36 |
|
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: 131.02 E-value: 5.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVE---DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEvvnDKSPKDRD-- 78
Cdd:COG4181 9 IELRGLTKTVGTGAG-ELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 -------IAMVFQNYALYPHMTVYDNMAFGLKLRKyKKDDIDRrvkeAAEIL---GLTEFLERKPADLSGGQRQRVAMGR 148
Cdd:COG4181 85 arlrarhVGFVFQSFQLLPTLTALENVMLPLELAG-RRDARAR----ARALLervGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKlrvsMRAEIAK----IHRRIGSTTIYVTHDQteamTLA---DRIVIMSA 211
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAA----TGEQIIDllfeLNRERGTTLVLVTHDP----ALAarcDRVLRLRA 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-209 |
1.95e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 135.88 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 13 YPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYP 90
Cdd:TIGR02857 331 YPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 91 HmTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:TIGR02857 410 G-TIAENIRLA------RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDqTEAMTLADRIVIM 209
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-248 |
3.35e-35 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 129.56 E-value: 3.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD------- 76
Cdd:TIGR03005 1 VRFSDVTKRFGILT--VLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpad 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 --------RDIAMVFQNYALYPHMTVYDNMAFGLKLRK-YKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMG 147
Cdd:TIGR03005 79 ekhlrqmrNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 148 RAIVRDAKVFLMDEPLSNLDAKLrvsmRAEIAKIHRRIGS----TTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGK 223
Cdd:TIGR03005 159 RALAMRPKVMLFDEVTSALDPEL----VGEVLNVIRRLASehdlTMLLVTHEMGFAREFADRVCFFDK----------GR 224
|
250 260
....*....|....*....|....*
gi 501958613 224 IEQVGSPQELYNLPANKFVAGFIGS 248
Cdd:TIGR03005 225 IVEQGKPDEIFRQPKEERTREFLSK 249
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-209 |
4.48e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 127.35 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGevvndkspkDRDIAMVFQNYAL---YPhMTV 94
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFGL-----KLRKYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:NF040873 75 RDLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501958613 170 LRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMtLADRIVIM 209
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-209 |
4.56e-35 |
|
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: 136.15 E-value: 4.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 12 KYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALY 89
Cdd:TIGR03375 472 AYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 pHMTVYDNMAFGlklRKYKKDDidrRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:TIGR03375 552 -YGTLRDNIALG---APYADDE---EILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 159 MDEPLSNLDaklrvsMRAEIAKIHR----RIGSTTIYVTHdQTEAMTLADRIVIM 209
Cdd:TIGR03375 625 LDEPTSAMD------NRSEERFKDRlkrwLAGKTLVLVTH-RTSLLDLVDRIIVM 672
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-233 |
1.69e-34 |
|
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: 126.78 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIAMVFQNYALYPHMTVYD 96
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFGLKLRKykKDDIDRRVKEAAEIL-GLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 175
Cdd:cd03224 95 NLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 176 AEIAKIhRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:cd03224 173 EAIREL-RDEGVTILLVEQNARFALEIADRAYVLER----------GRVVLEGTAAEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-234 |
3.35e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 126.19 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYpHMTVYDNMAFGlklrkykKDDIDR-RVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRA 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG-------RPGATReEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDQTEAMTlADRIVIMSAtknpqgngtiGKIEQVGS 229
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLED----------GKIVERGT 219
|
....*
gi 501958613 230 PQELY 234
Cdd:cd03251 220 HEELL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-209 |
9.11e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.92 E-value: 9.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RD--IA 80
Cdd:COG3845 6 LELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGL---KLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 158 LMDEPLSNLD----AKLRVSMRAEIAKihrriGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG3845 164 ILDEPTAVLTpqeaDELFEILRRLAAE-----GKSIIFITHKLREVMAIADRVTVL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-167 |
3.57e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDI-----SEGELKIDGEVVNDKSpKD-----RDIAMVFQNYALY 89
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYDPD-VDvvelrRRVGMVFQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PhMTVYDNMAFGLKLRKYK-KDDIDRRVKEAAEILGLTEflE-----RKPA-DLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:COG1117 105 P-KSIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALWD--EvkdrlKKSAlGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
....*
gi 501958613 163 LSNLD 167
Cdd:COG1117 182 TSALD 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-233 |
4.63e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.65 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELnlKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RD 78
Cdd:COG4604 1 MIEI--KNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFGlklR------KYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQR--VAMgrAI 150
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFG---RfpyskgRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 151 VRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMsatKNpqgngtiGKIEQVGSP 230
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM---KD-------GRVVAQGTP 220
|
...
gi 501958613 231 QEL 233
Cdd:COG4604 221 EEI 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-247 |
6.94e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 123.41 E-value: 6.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEgELKIDGEV----VNDKSPK------DRDIAMVFQNYALYP 90
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGEVrlfgRNIYSPDvdpievRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 91 HMTVYDNMAFGLKLRKY--KKDDIDRRV----KEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 165 NLDAKLRVSMRAEIAKIHRRIgsTTIYVTHDQTEAMTLADRIVIMsatknpqgngTIGKIEQVGSPQELYNLPAN----K 240
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFL----------YLGKLIEVGPTRKVFENPEHelteK 246
|
....*..
gi 501958613 241 FVAGFIG 247
Cdd:PRK14267 247 YVTGALG 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-209 |
1.22e-32 |
|
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: 121.21 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTThYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpKDRDIAMVFQN 85
Cdd:cd03226 2 IENISFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 86 --YALYPHmTVYDNMAFGLKlrkykkdDIDRRVKEAAEIL---GLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLK-------ELDAGNEQAETVLkdlDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 161 EPLSNLDAKlrvSMRaEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03226 152 EPTSGLDYK---NME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-237 |
2.93e-32 |
|
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: 127.11 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiSEGELKIDGEVVNDKSPKD-----RDIAMVFQN-YA-LYPHM 92
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 TVYDNMAFGLKL--RKYKKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDak 169
Cdd:COG4172 380 TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-- 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 170 lrVSMRAEI----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKI-EQvGSPQELYNLP 237
Cdd:COG4172 458 --VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD----------GKVvEQ-GPTEQVFDAP 517
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-209 |
4.27e-32 |
|
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: 120.08 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVnDKSPKDRdIAMVF 83
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 164 SNLDAKLRVSMRAEIAKIhRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03269 157 SGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-234 |
4.64e-32 |
|
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: 120.72 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPN-TTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMV 82
Cdd:cd03249 3 FKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPhMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIV 151
Cdd:cd03249 83 SQEPVLFD-GTIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 152 RDAKVFLMDEPLSNLDAKlrvSMRAEIAKIHR-RIGSTTIYVTHDQTeamTL--ADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:cd03249 156 RNPKILLLDEATSALDAE---SEKLVQEALDRaMKGRTTIVIAHRLS---TIrnADLIAVLQN----------GQVVEQG 219
|
....*.
gi 501958613 229 SPQELY 234
Cdd:cd03249 220 THDELM 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-209 |
9.93e-32 |
|
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: 117.53 E-value: 9.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---RDIA 80
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQnyalyphmtvydnmafglklrkykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-210 |
1.18e-31 |
|
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: 118.83 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTthYAVEDFDLDIkDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGE-VVNDKSPKDRDIAMV 82
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501958613 163 LSNLDAKLRVSMRAEIAkihrRIGSTTIYV--THDQTEAMTLADRIVIMS 210
Cdd:cd03264 158 TAGLDPEERIRFRNLLS----ELGEDRIVIlsTHIVEDVESLCNQVAVLN 203
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-248 |
1.27e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 120.29 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVV-------NDKSPKDRD--------IAMVFQNYALY 89
Cdd:COG4598 28 SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRRqlqrirtrLGMVFQSFNLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHMTVYDNMAFG----LKLRKykkddidRRVKEAAEIL----GLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG4598 108 SHMTVLENVIEApvhvLGRPK-------AEAIERAEALlakvGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 162 PLSNLDAK-----LRVsMRAeIAKIHRrigsTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNL 236
Cdd:COG4598 181 PTSALDPElvgevLKV-MRD-LAEEGR----TMLVVTHEMGFARDVSSHVVFLHQ----------GRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 501958613 237 PANKFVAGFIGS 248
Cdd:COG4598 245 PKSERLRQFLSS 256
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-209 |
1.52e-31 |
|
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: 118.47 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYpnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF 83
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFGLKLRKYKKddidRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 164 SNLDAKLRVSMRAEIAKiHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03268 155 NGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGII 199
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-233 |
4.31e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 117.71 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 15 NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVND--KSPKDRDIAMVFQNYALYPHm 92
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 TVYDNMAFGlklRKYKKDDidrRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03254 92 TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIhrRIGSTTIYVTHDQTeamTL--ADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLS---TIknADKILVLDD----------GKIIEEGTHDEL 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-209 |
5.44e-31 |
|
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: 118.75 E-value: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTT------HYAV-EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD 76
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 -----RDIAMVFQNY--ALYPHMTVydNMAFGLKLRKYKKDDIDRRVKEAAEILGL----TEFLERKPADLSGGQRQRVA 145
Cdd:TIGR02769 83 rrafrRDVQLVFQDSpsAVNPRMTV--RQIIGEPLRHLTSLDESEQKARIAELLDMvglrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 146 MGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-231 |
5.80e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 120.75 E-value: 5.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 35 VFvGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS------PKDRDIAMVFQNYALYPHMTVYDNMAFGLKlrKYK 108
Cdd:PRK11144 29 IF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 109 KDDIDRRVkeaaEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGST 188
Cdd:PRK11144 106 VAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501958613 189 TIYVTHDQTEAMTLADRIVIMSatknpqgNGTI---GKIEQV-GSPQ 231
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLE-------QGKVkafGPLEEVwASSA 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-238 |
7.33e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.97 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKI-DGEVVNDKSPKD-----RDIAMVFQnyalYP-HM 92
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKlkplrKKVGIVFQ----FPeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 ----TVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTE-FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 168 AKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPA 238
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK----------GTVFLQGTPREIFADPD 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-209 |
1.18e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.49 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTT---HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR--D 78
Cdd:COG1101 2 LELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYAL--YPHMTVYDNMA--------FGLKLRKyKKDDIDrRVKEAAEILGLTefLERKPAD----LSGGQRQRV 144
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGL-TKKRRE-LFRELLATLGLG--LENRLDTkvglLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 145 AMGRAIVRDAKVFLMDEPLSNLDAKlrvsmRAEI-----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPK-----TAALvleltEKIVEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-239 |
5.73e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.90 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 17 THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIsEGELKIDGEV-----------VNDKSPKdRDIAMVFQN 85
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerrVNLNRLR-RQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 86 YALYPhMTVYDNMAFGLKL----RKYKKDDIDRRVKEAAEILG-LTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSATKNpqgngTIGKIEQVGSPQELYNLPAN 239
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN-----RIGQLVEFGLTKKIFNSPHD 249
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
25-206 |
7.60e-30 |
|
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: 114.37 E-value: 7.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR------DIAMVFQNYALYPHMTVYDNM 98
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPDFTALENV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:TIGR02211 105 AMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLM 184
|
170 180
....*....|....*....|....*...
gi 501958613 179 AKIHRRIGSTTIYVTHDqteaMTLADRI 206
Cdd:TIGR02211 185 LELNRELNTSFLVVTHD----LELAKKL 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-209 |
1.03e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.17 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTT-------HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN--D 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 72 KSPKD---RDIAMVFQNY--ALYPHMTVYDNMAFGLK-LRKYKKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRV 144
Cdd:PRK10419 81 RAQRKafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 145 AMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-233 |
1.31e-29 |
|
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: 113.92 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 16 TTHY----AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIAMVFQNYAL 88
Cdd:COG0410 10 HAGYggihVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 YPHMTVYDNMAFGLKLRKyKKDDIDRRVkeaAEILG----LTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:COG0410 90 FPSLTVEENLLLGAYARR-DRAEVRADL---ERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 165 NLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:COG0410 166 GLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLER----------GRIVLEGTAAEL 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-247 |
1.80e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.49 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGeLKIDGEVV-NDKSPKD---------RDIAMVFQNYA 87
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfHGKNLYApdvdpvevrRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHmTVYDNMAFGLKLRKYKKD-D--IDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGYKGDmDelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 165 NLDAKLRVSMRAEIAKIHRRIgsTTIYVTHDQTEAMTLADRIVIMSATKNPQGnGTIGKIEQVGSPQELYNLPANK---- 240
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVELTEGG-GRYGYLVEFDRTEKIFNSPQQQatrd 257
|
....*..
gi 501958613 241 FVAGFIG 247
Cdd:PRK14243 258 YVSGRFG 264
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-237 |
2.24e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.96 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 14 PNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-----DIAMVFQN--Y 86
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 ALYPHMTVYDNMAFGLKLR--KYKKDDIDRRVKEAAEILGLTEFL-ERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK15079 110 SLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 164 SNLDaklrVSMRAEIA----KIHRRIGSTTIYVTHDQTEAMTLADRIVIMsatknpqgngTIGKIEQVGSPQELYNLP 237
Cdd:PRK15079 190 SALD----VSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKHISDRVLVM----------YLGHAVELGTYDEVYHNP 253
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-244 |
3.24e-29 |
|
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: 118.67 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAM 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHmTVYDNMAFGlklrkyKKDDIDR-RVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRA 149
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG------RTEQADRaEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 150 IVRDAKVFLMDEPLSNLDAKlrvSMRAEIAKIHRRI-GSTTIYVTHDQTeAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNE---SERLVQAALERLMqGRTTLVIAHRLS-TIEKADRIVVMDD----------GRIVERG 549
|
250
....*....|....*.
gi 501958613 229 SPQELynLPANKFVAG 244
Cdd:TIGR02203 550 THNEL--LARNGLYAQ 563
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-278 |
5.56e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS-------PKD 76
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 RdiamvfqnyALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG4152 80 R---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLD---AKLrvsMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:COG4152 151 LILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINK----------GRKVLSGSVDEI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501958613 234 YN-LPANKFVAGFIGSPAM--NFFEVVVKDgqiISEDGLDIAIPEGQA 278
Cdd:COG4152 217 RRqFGRNTLRLEADGDAGWlrALPGVTVVE---EDGDGAELKLEDGAD 261
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-206 |
7.56e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.22 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 11 KKYP--NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSP------KDRDIAMV 82
Cdd:PRK11629 13 KRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501958613 163 LSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDqteaMTLADRI 206
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-246 |
1.32e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.98 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDI--- 79
Cdd:PRK10619 5 KLNVIDLHKRYGE--HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 ------------AMVFQNYALYPHMTVYDN-MAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERK-PADLSGGQRQRVA 145
Cdd:PRK10619 83 dknqlrllrtrlTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 146 MGRAIVRDAKVFLMDEPLSNLDAKLrvsmRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiG 222
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQ----------G 228
|
250 260
....*....|....*....|....
gi 501958613 223 KIEQVGSPQELYNLPANKFVAGFI 246
Cdd:PRK10619 229 KIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-233 |
1.90e-28 |
|
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: 116.06 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGEL--KIDGEVVN--DKSPKDRD-----IAMVFQNYALYP 90
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDmtKPGPDGRGrakryIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 91 HMTVYDNM--AFGLKLrkykKDDIDRRvkEAAEIL---GLTE-----FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:TIGR03269 379 HRTVLDNLteAIGLEL----PDELARM--KAVITLkmvGFDEekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD----------GKIVKIGDPEEI 515
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-282 |
4.17e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVF 83
Cdd:PRK13648 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNyalyPH-----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK13648 90 QN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTlADRIVIMSAtknpqgngtiGKIEQVGSPQELYnlpa 238
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNK----------GTVYKEGTPTEIF---- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 501958613 239 nkfvagfigspamnffevvvKDGQIISEDGLDIAIPEGQAKMLE 282
Cdd:PRK13648 231 --------------------DHAEELTRIGLDLPFPIKINQMLG 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-235 |
4.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 7 KHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL---EDISEGELKIDGEVVNDKSPKD-RD-IAM 81
Cdd:PRK13640 9 KHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiREkVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNY-ALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK13640 89 VFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 161 EPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAmTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDD----------GKLLAQGSPVEIFS 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-199 |
5.27e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.48 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR------DIAMVFQNYALYPHMTVYDNM 98
Cdd:PRK10584 30 ELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:PRK10584 110 ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180
....*....|....*....|.
gi 501958613 179 AKIHRRIGSTTIYVTHDQTEA 199
Cdd:PRK10584 190 FSLNREHGTTLILVTHDLQLA 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-195 |
5.88e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.19 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RDIAMVFQNYALYPHMTV 94
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180
....*....|....*....|.
gi 501958613 175 RAEIAKIHrRIGSTTIYVTHD 195
Cdd:PRK10908 177 LRLFEEFN-RVGVTVLMATHD 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-209 |
6.83e-28 |
|
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: 107.69 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RD-IAM 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHmTVYDNMafglklrkykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIhRRIGSTTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVL 168
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-232 |
7.51e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.72 E-value: 7.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIA 80
Cdd:PRK11231 2 TLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFG----LKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 157 FLMDEPLSNLDaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:PRK11231 160 VLLDEPTTYLD----INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLAN----------GHVMAQGTPEE 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-234 |
7.86e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 26 LDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNY-ALYPHMTVYDNMAFGL 102
Cdd:PRK13642 28 FSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGATVEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 103 KLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIH 182
Cdd:PRK13642 108 ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 183 RRIGSTTIYVTHDQTEAMTlADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13642 188 EKYQLTVLSITHDLDEAAS-SDRILVMKA----------GEIIKEAAPSELF 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
1.12e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.83 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVF 83
Cdd:PRK13647 7 VEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNyalyPH-----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK13647 86 QD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
3.17e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.91 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdGEVVNDKSPK----- 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSlsqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 76 ------DRDIAMVFQNYALYPHMTVYDNMAFG-LKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGR 148
Cdd:PRK11264 78 glirqlRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKI--HRRigsTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQ 226
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQ----------GRIVE 224
|
250
....*....|.
gi 501958613 227 VGSPQELYNLP 237
Cdd:PRK11264 225 QGPAKALFADP 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-244 |
3.58e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.08 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGL-----EDISEGELKIDGEVV--NDKSPKDRDIAMVFQNYALYPHMTVYDN 97
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRRVQMVFQIPNPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAFGLKLRKY--KKDDIDRRVKEAAEILGLTEFLERK---PA-DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:PRK14247 103 VALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 172 VSMRAEIAKIHRRIgsTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLP----ANKFVAG 244
Cdd:PRK14247 183 AKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYK----------GQIVEWGPTREVFTNPrhelTEKYVTG 247
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-237 |
6.52e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.90 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RDIAMVFQN-YA-LYPHMTVYD--------NMAFG 101
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVGQileeplliNTSLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 LKLRKYKKDDIDRRVkeaaeilGL-TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEI-- 178
Cdd:PRK11308 127 AAERREKALAMMAKV-------GLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD----VSVQAQVln 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501958613 179 --AKIHRRIGSTTIYVTHDQTEAMTLADRIVIMsatknpqgngTIGKIEQVGSPQELYNLP 237
Cdd:PRK11308 196 lmMDLQQELGLSYVFISHDLSVVEHIADEVMVM----------YLGRCVEKGTKEQIFNNP 246
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
8.69e-27 |
|
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: 111.30 E-value: 8.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 2 VELNLKHIYKKYPnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDI 79
Cdd:TIGR02868 333 PTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNyalyPHM---TVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVA 145
Cdd:TIGR02868 412 SVCAQD----AHLfdtTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501958613 146 MGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHD 195
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-210 |
9.32e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 105.33 E-value: 9.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 28 IKDKEFIVFVGPSGCGKSTTLRMIAGLED--ISEGELKIDGEVVNDKSPKDRdIAMVFQNYALYPHMTVYDNMAFGLKLR 105
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETLMFAAKLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 106 KykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklrvSMRAEIAKIHRRI 185
Cdd:cd03213 111 G-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS----SSALQVMSLLRRL 157
|
170 180
....*....|....*....|....*....
gi 501958613 186 ---GSTTIYVTHD-QTEAMTLADRIVIMS 210
Cdd:cd03213 158 adtGRTIICSIHQpSSEIFELFDKLLLLS 186
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-240 |
1.21e-26 |
|
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: 105.91 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED----ISEGELKIDGEVVNDKSPKDRDIAMVFQN--YALYPHMT 93
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 VYDNMAFGLKLRKYKKDDIDRRVKEAAEILGL---TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL 170
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 171 RVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANK 240
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD----------GRIVERGTVKEIFYNPKHE 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-235 |
3.49e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.25 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEdISE------GELKIDGEVVNDKSPKD-- 76
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISEtgqtivGDYAIPANLKKIKEVKRlr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 RDIAMVFQ--NYALYPHmTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGL-TEFLERKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK13645 90 KEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE----------GKVISIGSPFEI 238
|
..
gi 501958613 234 YN 235
Cdd:PRK13645 239 FS 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-233 |
1.24e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.39 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 28 IKDKEFIVFVGPSGCGKSTTLRMIAGLedIS-EGELKIDGEVVNDKSPKD--RDIAMVFQNYALyPHMTVYDNMAFGlkl 104
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 105 rkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK--LR 171
Cdd:PRK11174 447 ---NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHseQL 523
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 172 VsMRAeIAKIHRriGSTTIYVTH--DQTEAMtlaDRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:PRK11174 524 V-MQA-LNAASR--RQTTLMVTHqlEDLAQW---DQIWVMQD----------GQIVQQGDYAEL 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-233 |
1.35e-25 |
|
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: 103.08 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYpNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVF 83
Cdd:cd03253 3 FENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYpHMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVR 152
Cdd:cd03253 82 QDTVLF-NDTIGYNIRYG------RPDATDEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 153 DAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDQTEAMTlADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKD----------GRIVERGTHEE 221
|
.
gi 501958613 233 L 233
Cdd:cd03253 222 L 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-211 |
1.49e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.82 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN--DKSPKDRDIA 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHmTVYDNMA-FGlklrkykkDDID-RRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMG 147
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIArFG--------ENADpEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 148 RAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHdQTEAMTLADRIVIMSA 211
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQD 528
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-246 |
1.90e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.59 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN--------DKSPKDRDIAMVFQNYALYPHM 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 TVYDNMAFGLKLRKYK-KDDIDRRVKEAAEILGL----TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 168 AKLRVSMRAEIAKIHRRIgsTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAGFI 246
Cdd:PRK14246 186 IVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYN----------GELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
32-218 |
2.22e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 32 EFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHmTVYDNMAFGLKLRKyKK 109
Cdd:PRK10247 34 EFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNLIFPWQIRN-QQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 110 DDIDRRVKEAAEiLGLTE-FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGST 188
Cdd:PRK10247 112 PDPAIFLDDLER-FALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIA 190
|
170 180 190
....*....|....*....|....*....|
gi 501958613 189 TIYVTHDQTEaMTLADRIVimsaTKNPQGN 218
Cdd:PRK10247 191 VLWVTHDKDE-INHADKVI----TLQPHAG 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-234 |
2.89e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.66 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 10 YKKYPNT--THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS------PKDRDIAM 81
Cdd:PRK13643 9 YTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQnyalYPHM-----TVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK13643 89 VFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHrRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEK----------GHIISCGTPSDVF 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-234 |
3.18e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.24 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 15 NTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSP--KDRDIA-MVFQNyalyPH 91
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 92 -----MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:PRK13633 96 nqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 167 DAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTlADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS----------GKVVMEGTPKEIF 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-210 |
8.09e-25 |
|
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: 101.06 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIykkypnTTHY----AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-- 77
Cdd:TIGR03410 1 LEVSNL------NVYYgqshILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 -DIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILglTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:TIGR03410 75 aGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 157 FLMDEPLSNLDAklrvSMRAEIAKIHRRI----GSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:TIGR03410 153 LLLDEPTEGIQP----SIIKDIGRVIRRLraegGMAILLVEQYLDFARELADRYYVME 206
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
22-233 |
8.46e-25 |
|
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: 106.19 E-value: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN--DKSPKDRDIAMVFQNYALYPHmTVYDNMA 99
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFENIA 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 100 FGLKLrkykkdDIDRrVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD- 167
Cdd:TIGR03797 549 GGAPL------TLDE-AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEATSALDn 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 168 ----------AKLRVSmRAEIAkiHRRigSTtiyVTHdqteamtlADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:TIGR03797 622 rtqaivseslERLKVT-RIVIA--HRL--ST---IRN--------ADRIYVLDA----------GRVVQQGTYDEL 671
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-235 |
1.33e-24 |
|
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: 100.31 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 32 EFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEvvnDKSPKDRDIAMVFQNYAL---YPhMTVYDNMAFGLK----- 103
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGRTghigw 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 104 LRKYKKDDIdRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD---AKLRVSMRAEIAK 180
Cdd:TIGR03771 83 LRRPCVADF-AAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFIELAG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 181 ihrrIGSTTIYVTHDQTEAMTLADRIVIMSatknpqgngtiGKIEQVGSPQELYN 235
Cdd:TIGR03771 162 ----AGTAILMTTHDLAQAMATCDRVVLLN-----------GRVIADGTPQQLQD 201
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
21-237 |
1.50e-24 |
|
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: 105.41 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDkSPKDR---DIAMVFQNYALYpHMTVYDN 97
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREE-IPREVlanSVAMVDQDIFLF-EGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAfgLKLRKYKKDDIDRRVKEAA---EIL----GLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL 170
Cdd:TIGR03796 573 LT--LWDPTIPDADLVRACKDAAihdVITsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPET 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 171 RVSMRAEIakihRRIGSTTIYVTHdQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLP 237
Cdd:TIGR03796 651 EKIIDDNL----RRRGCTCIIVAH-RLSTIRDCDEIIVLER----------GKVVQRGTHEELWAVG 702
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-242 |
2.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.45 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVND--KSPKDRDI-A 80
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQN-YALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDqTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPAN 239
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDR----------GKIVLEGEPENVLSDVSL 228
|
...
gi 501958613 240 KFV 242
Cdd:PRK13644 229 QTL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-194 |
3.27e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.79 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLdiKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRdIAMVFQNYALYPHMTVYDNMAFGL 102
Cdd:PRK13539 22 SFTL--AAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 103 KLRkykkDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlRVSMRAEIAKIH 182
Cdd:PRK13539 99 AFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELIRAH 173
|
170
....*....|..
gi 501958613 183 RRIGSTTIYVTH 194
Cdd:PRK13539 174 LAQGGIVIAATH 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-234 |
4.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpKDRDI-------AMVFQnyalYPHM 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-KNKDIkqirkkvGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 -----TVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTE-FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:PRK13649 97 qlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 167 DAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEK----------GKLVLSGKPKDIF 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-209 |
5.44e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.70 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL---EDISEGELKIDGEVVNDKSPKDRDI-------AMVFQNYA 87
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrksrantGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHMTVYDNMAFGLK---------LRKYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK09984 97 LVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 159 MDEPLSNLDAK-LRVSMRAeIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK09984 176 ADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
6.45e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN-DKSP--KDRD-I 79
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSllEVRKtV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQN-----YAlyPhmTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:PRK13639 81 GIVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 155 KVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSD----------GKIIKEGTPKEVF 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-209 |
7.20e-24 |
|
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: 97.54 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 9 IYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEvvndkspkdrdIAMVFQNyAL 88
Cdd:cd03250 9 TWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 YPHMTVYDNMAFGLKL--RKYKKddidrrVKEAA------EILG---LTEFLERKpADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:cd03250 77 IQNGTIRENILFGKPFdeERYEK------VIKACalepdlEILPdgdLTEIGEKG-INLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 158 LMDEPLSNLDAklRVSmraeiAKI-------HRRIGSTTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03250 150 LLDDPLSAVDA--HVG-----RHIfencilgLLLNNKTRILVTH-QLQLLPHADQIVVL 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-209 |
9.16e-24 |
|
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: 97.99 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 17 THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVndkspkdrdiAMVFQNYALYPHMTVYD 96
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRA 176
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190
....*....|....*....|....*....|...
gi 501958613 177 EIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-250 |
1.04e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYAL---------- 88
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfefdvrqvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 ----YPHMTVYDNMafglklrkykkDDIDRR-VKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK09536 99 emgrTPHRSRFDTW-----------TETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELynLPANKFVA 243
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLAD----------GRVRAAGPPADV--LTADTLRA 234
|
....*..
gi 501958613 244 GFIGSPA 250
Cdd:PRK09536 235 AFDARTA 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-235 |
1.11e-23 |
|
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: 98.00 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKypnttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIAM 81
Cdd:cd03218 5 NLSKRYGK-----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 162 PLSNLDAKLRVSMRAEIAKIHRR-IGsttIYVT-HDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYE----------GKVLAEGTPEEIAA 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-210 |
1.13e-23 |
|
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: 98.17 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RDIAMVF-QNYALYPHMTVYDN 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAE 177
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|...
gi 501958613 178 IAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:cd03267 196 LKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-233 |
1.29e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.52 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHMTVYDNMA 99
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 100 FGLK-----LRKYKKDDIDRrVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK10253 104 RGRYphqplFTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 175 RAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:PRK10253 183 LELLSELNREKGYTLAAVLHDLNQACRYASHLIALRE----------GKIVAQGAPKEI 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-233 |
1.34e-23 |
|
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: 97.94 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGE--VVNDKSPKDRDIAMVF 83
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYpHMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVR 152
Cdd:cd03252 83 QENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 153 DAKVFLMDEPLSNLDAKlrvSMRAEIAKIHRRI-GSTTIYVTHDQTEAMTlADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:cd03252 156 NPRILIFDEATSALDYE---SEHAIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEK----------GRIVEQGSHD 221
|
..
gi 501958613 232 EL 233
Cdd:cd03252 222 EL 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-246 |
1.67e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEgELKIDGEVV----NDKSPKD------RDIAMVFQNYALY 89
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVynghNIYSPRTdtvdlrKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PhMTVYDNMAFGLKLRKYK-KDDIDRRVKEA---AEILG-LTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK14239 99 P-MSIYENVVYGLRLKGIKdKQVLDEAVEKSlkgASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 165 NLDAKlrVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKFVAG 244
Cdd:PRK14239 178 ALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLD----------GDLIEYNDTKQMFMNPKHKETED 245
|
..
gi 501958613 245 FI 246
Cdd:PRK14239 246 YI 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-210 |
1.82e-23 |
|
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: 95.96 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 16 TTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD---IAMV---FQNYALY 89
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHMTVYDNMAFglklrkykkddidrrvkeaaeilglteflerkPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDak 169
Cdd:cd03215 91 LDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD-- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501958613 170 lrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:cd03215 137 --VGAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMY 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
23-207 |
2.81e-23 |
|
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: 97.08 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEG-ELKIDGEVVNDKSPKD--RDIAMV---FQNYaLYPHMTVYD 96
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElrKRIGLVspaLQLR-FPRDETVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMA------FGLkLRKYKKDDIdRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL 170
Cdd:COG1119 100 VVLsgffdsIGL-YREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501958613 171 RVSMRAEIAKIHRRIGSTTIYVTHDQ-------TEAMTLAD-RIV 207
Cdd:COG1119 178 RELLLALLDKLAAEGAPTLVLVTHHVeeippgiTHVLLLKDgRVV 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
3.26e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEfIV-FVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS------ 73
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 74 ------PKDrdiAMVFQNyalyphMTVYDN-MAFgLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAM 146
Cdd:COG1137 78 lgigylPQE---ASIFRK------LTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 147 GRAIVRDAKVFLMDEPLSNLDAkLRVsmrAEIAKI-----HRRIGsttIYVT-HDQTEAMTLADRIVIMSAtknpqgngt 220
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDP-IAV---ADIQKIirhlkERGIG---VLITdHNVRETLGICDRAYIISE--------- 211
|
250
....*....|....*..
gi 501958613 221 iGKIEQVGSPQELYNLP 237
Cdd:COG1137 212 -GKVLAEGTPEEILNNP 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-233 |
4.45e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.81 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 8 HIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQN 85
Cdd:PRK13657 339 DVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 86 YALYpHMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKPA-----------DLSGGQRQRVAMGRAIVRDA 154
Cdd:PRK13657 418 AGLF-NRSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 155 KVFLMDEPLSNLDAKLRVSMRAEIAKIhrRIGSTTIYVTHDQTeamTL--ADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS---TVrnADRILVFDN----------GRVVESGSFDE 555
|
.
gi 501958613 233 L 233
Cdd:PRK13657 556 L 556
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-237 |
5.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKkypnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMV 82
Cdd:PRK13652 8 DLCYSYS----GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQN---YALYPhmTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK13652 84 FQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLP 237
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK----------GRIVAYGTVEEIFLQP 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-233 |
6.55e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.58 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNdksPKDRDIAM----VFQNYALYPHMTVY 95
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRRrvgyMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 96 DNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 175
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 176 AEIAKIHRRIGsTTIYV-THDQTEAMtLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:NF033858 438 RLLIELSREDG-VTIFIsTHFMNEAE-RCDRISLMHA----------GRVLASDTPAAL 484
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-233 |
8.19e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.37 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-----RDIAMVFQNYALYPHMTVYD 96
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFGLKLRKYKKDDIDRR-VKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 175
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 176 AEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSATknpqgngtigKIEQVGSPQEL 233
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADK----------KIVAHGSAQAL 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-208 |
9.76e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYK-KYpnTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RDIAMVF 83
Cdd:COG4586 24 LKGLFRrEY--REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFaRRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 -QNYALYPHMTVYDNmaFGLkLRK-YK--KDDIDRRVKEAAEILGLTEFLE---RKpadLSGGQRQR--VAMgrAIVRDA 154
Cdd:COG4586 102 gQRSQLWWDLPAIDS--FRL-LKAiYRipDAEYKKRLDELVELLDLGELLDtpvRQ---LSLGQRMRceLAA--ALLHRP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 155 KVFLMDEPLSNLD--AKLRVsmRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVI 208
Cdd:COG4586 174 KILFLDEPTIGLDvvSKEAI--REFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-233 |
1.33e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 2 VELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RD-I 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYPHmTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLE-RKPAD---------LSGGQRQRVAMGRA 149
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGLEKLLEdDKGLNawlgeggrqLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDQTeAMTLADRIVIMSatknpqgNGTIgkIEQvGS 229
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMD-------NGQI--IEQ-GT 556
|
....
gi 501958613 230 PQEL 233
Cdd:PRK11160 557 HQEL 560
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-209 |
1.74e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.15 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD-IAMV 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYpHMTVYDNmafglklrkykkddIDRRvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03247 81 NQRPYLF-DTTLRNN--------------LGRR--------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501958613 163 LSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHDQTeAMTLADRIVIM 209
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFL 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-209 |
2.01e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.77 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 19 YAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS-----PKDRDIAMVFQN-YA-LYPH 91
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 92 MTVYDNMAFGLKLRKY-KKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDak 169
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD-- 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501958613 170 lrVSMRAEIAK----IHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10261 496 --VSIRGQIINllldLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-233 |
2.88e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 98.66 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK--DRDIAM 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHmTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAI 150
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALC------NPGAPFEHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 151 VRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGSTTIYVTHdQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSP 230
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEK----------GQIAESGRH 675
|
...
gi 501958613 231 QEL 233
Cdd:TIGR01846 676 EEL 678
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-241 |
3.09e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTT----LRMIAglediSEGELKIDGEVVNDKSPKD-----RDIAMVFQ--NY 86
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 ALYPHMTVYDNMAFGLKL--RKYKKDDIDRRVKEAAEILGL-TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSatknpQGNgtigKIEQvGSPQELYNLPANKF 241
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR-----QGE----VVEQ-GDCERVFAAPQQEY 521
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-243 |
4.45e-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: 94.01 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 12 KYPnTTHYAVEDFDL-----DIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVndkSPKDRDIAMVFQny 86
Cdd:cd03237 2 TYP-TMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKPQYIKADYE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 alyphMTVYDNMAF---GLKLRKYKKDDIdrrvkeaAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03237 76 -----GTVRDLLSSitkDFYTHPYFKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDaklrVSMRAEIAKIHRRIG----STTIYVTHDQTEAMTLADRIVIMSatknpqgnGTIGKIEQVGSPQELYNlPAN 239
Cdd:cd03237 144 AYLD----VEQRLMASKVIRRFAenneKTAFVVEHDIIMIDYLADRLIVFE--------GEPSVNGVANPPQSLRS-GMN 210
|
....
gi 501958613 240 KFVA 243
Cdd:cd03237 211 RFLK 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-233 |
6.28e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD-IAMV 82
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMA-----FGLKLRKykkddIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLvfgryFGLSAAA-----ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSATKnpqgngtigKIEQvGSPQEL 233
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGR---------KIAE-GAPHAL 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-232 |
8.07e-22 |
|
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: 96.74 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 13 YPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGevvNDKSPKDRDiamvfqnyALYPHM 92
Cdd:COG4618 340 PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWDRE--------ELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 ------------TVYDNMA-FGlklrkykkDDIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGR 148
Cdd:COG4618 409 gylpqdvelfdgTIAENIArFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTeAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRD----------GRVQAFG 548
|
....
gi 501958613 229 SPQE 232
Cdd:COG4618 549 PRDE 552
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-167 |
1.02e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.63 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIA 80
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYpHMTVYDNMAFGLKlRKYKKDDIDRrvkeAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRA 149
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-EQYSREQIEE----AARMAYAMDFINKMDngldtvigengVLLSGGQRQRIAIARA 494
|
170
....*....|....*...
gi 501958613 150 IVRDAKVFLMDEPLSNLD 167
Cdd:PRK11176 495 LLRDSPILILDEATSALD 512
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-245 |
1.03e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPN--TTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVV----NDKSPKDR 77
Cdd:PRK10535 5 LELKDIRRSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 --DIAMVFQNYALYPHMTVYDNMAF-----GLKLRKYKKddidrRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAI 150
Cdd:PRK10535 85 reHFGFIFQRYHLLSHLTAAQNVEVpavyaGLERKQRLL-----RAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 151 VRDAKVFLMDEPLSNLDAKLRVSMRAeIAKIHRRIGSTTIYVTHDQTEAMTlADRIVIMSATKNPQGNGTIGKIEQVGSP 230
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGT 237
|
250
....*....|....*..
gi 501958613 231 QELYNLPA--NKFVAGF 245
Cdd:PRK10535 238 EPVVNTASgwRQFVSGF 254
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
1.52e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVnDKSPKD-----RD 78
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQ--NYALYPhMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLtEFLERKPAD-LSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK13636 84 VGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE----------GRVILQGNPKEVF 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-209 |
1.64e-21 |
|
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: 91.76 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 13 YPNTTHYAV-EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK--DRDIAMVFQNYALY 89
Cdd:cd03248 21 YPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHmTVYDNMAFGLKlrkykkDDIDRRVKEAAEILGLTEFLE-----------RKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03248 101 AR-SLQDNIAYGLQ------SCSFECVKEAAQKAHAHSFISelasgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501958613 159 MDEPLSNLDAKLRVSMRAEIAKIHRRigsTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVL 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-232 |
2.83e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 17 THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVndkSPkdRDIAMVFQnyalyPHMTVYD 96
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS---AL--LELGAGFH-----PELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 NMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRvsMRA 176
Cdd:COG1134 108 NIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ--KKC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 177 EiAKIHRRI--GSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:COG1134 186 L-ARIRELResGRTVIFVSHSMGAVRRLCDRAIWLEK----------GRLVMDGDPEE 232
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
3-235 |
2.87e-21 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 95.34 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG---EVVNDKSPKdRDI 79
Cdd:TIGR01192 334 AVEFRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGidiNTVTRESLR-KSI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYpHMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKPAD-----------LSGGQRQRVAMGR 148
Cdd:TIGR01192 412 ATVFQDAGLF-NRSIRENIRLG------REGATDEEVYEAAKAAAAHDFILKRSNGydtlvgergnrLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIhrRIGSTTIYVTHdQTEAMTLADRIVIMSAtknpqgngtiGKIEQVG 228
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDAL--RKNRTTFIIAH-RLSTVRNADLVLFLDQ----------GRLIEKG 551
|
....*..
gi 501958613 229 SPQELYN 235
Cdd:TIGR01192 552 SFQELIQ 558
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-168 |
4.47e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdgevvndksPKDRDIAMVFQNYALYPHMTVYDNMAFG 101
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPPLDDDLTVLDTVLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 LK-LRKYKKD-------------------------------DIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGR 148
Cdd:COG0488 86 DAeLRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPeEDLDRPVSELSGGWRRRVALAR 165
|
170 180
....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDA 168
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLDL 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-210 |
6.70e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 16 TTHYAVEDFDLDIKDKEfIV-FVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---RDIAMVFQN---YAL 88
Cdd:COG1129 263 SVGGVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 YPHMTVYDNMAFGLkLRKYKKDDIDRRVKEAAEILGLTEFLERKPAD-------LSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG1129 342 VLDLSIRENITLAS-LDRLSRGGLLDRRRERALAEEYIKRLRIKTPSpeqpvgnLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501958613 162 PLSNLDaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:COG1129 421 PTRGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMR 468
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-210 |
7.71e-21 |
|
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: 90.02 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 10 YKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED---ISEGELKIDGEVVNDKSPKDRdIAMVFQNY 86
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 ALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEI----LGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501958613 163 LSNLD---AKLRVSMRAEIAKIHRrigstTIYVTHDQ--TEAMTLADRIVIMS 210
Cdd:cd03234 171 TSGLDsftALNLVSTLSQLARRNR-----IVILTIHQprSDLFRLFDRILLLS 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-232 |
1.23e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.17 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHMTVYDNM 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIV-------RDAKVFLMDEPLSNLDAK-- 169
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAhq 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 170 LRVsMRaeIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:COG4559 177 HAV-LR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQ----------GRLVAQGTPEE 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
1.29e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-DI 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 80 AMVFQNYALYPHMTVYDNMA-----FGLKLRKYKkddidrrvkeaAEILGLTEF--LERKP----ADLSGGQRQRVAMGR 148
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLvfgryFGMSTREIE-----------AVIPSLLEFarLESKAdarvSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLR----VSMRAEIAKihrriGSTTIYVTHDQTEAMTLADRIVIMSATKnpqgngtigKI 224
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGR---------KI 251
|
....*....
gi 501958613 225 EQvGSPQEL 233
Cdd:PRK13536 252 AE-GRPHAL 259
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
1.37e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL----------EDISEGELKIDGEVVNDKSP 74
Cdd:PRK13631 26 NLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 75 KD--------RDIAMVFQ--NYALYPHmTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTE-FLERKPADLSGGQRQR 143
Cdd:PRK13631 106 KKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 144 VAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMrAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGK 223
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK----------GK 253
|
250
....*....|.
gi 501958613 224 IEQVGSPQELY 234
Cdd:PRK13631 254 ILKTGTPYEIF 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-209 |
1.39e-20 |
|
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: 93.21 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTT----LRMIAGLEDISEGELKIDGEVVNDKSPKD------RDIAMVFQN--YA 87
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHMTVYDNMAFGLKL-RKYKKDDIDRRVKEAAEILGLTEfLERK----PADLSGGQRQRV--AMgrAIVRDAKVFLMD 160
Cdd:COG4172 105 LNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRldayPHQLSGGQRQRVmiAM--ALANEPDLLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 161 EPLSNLDaklrVSMRAEI----AKIHRRIGSTTIYVTHDqteaMTL----ADRIVIM 209
Cdd:COG4172 182 EPTTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGVvrrfADRVAVM 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-210 |
1.52e-20 |
|
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: 93.92 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-DIAMVFQ 84
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 85 NYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 165 NLDAKLRVSMRAEIAKIhrRIGSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-211 |
1.59e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.03 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKI--DGEVVNDKSPKDRDIAMVFQNYALY-------- 89
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFL-ERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501958613 169 KLRVSMRAEIAKIHRRiGSTTIYVTHDqTEAM-TLADRIVIMSA 211
Cdd:COG4778 186 ANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTP 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-194 |
2.23e-20 |
|
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: 87.80 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK-DRDIAMVFQNYALYPHMTVYDNM 98
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGLKLRKYKkddiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlRVSMRAEI 178
Cdd:TIGR01189 95 HFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGL 169
|
170
....*....|....*.
gi 501958613 179 AKIHRRIGSTTIYVTH 194
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-208 |
3.30e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---RDIA 80
Cdd:PRK11288 5 LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGL---KLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 158 LMDEPLSNLDAKlrvsmraEIAKIHRRI------GSTTIYVTHDQTEAMTLADRIVI 208
Cdd:PRK11288 163 AFDEPTSSLSAR-------EIEQLFRVIrelraeGRVILYVSHRMEEIFALCDAITV 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
37-233 |
3.54e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHMTVYDNMAFGL-----KLRKYKK 109
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELVAIGRypwhgALGRFGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 110 DDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTT 189
Cdd:PRK10575 123 AD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTV 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501958613 190 IYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:PRK10575 202 IAVLHDINMAARYCDYLVALRG----------GEMIAQGTPAEL 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-237 |
1.13e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSpkDRDIA---MV--FQNYALYPHMTV 94
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP--GHQIArmgVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAF------------GL----KLRKYKKDDIDRrvkeAA---EILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK11300 98 IENLLVaqhqqlktglfsGLlktpAFRRAESEALDR----AAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSATKnPQGNGTigkieqvgsPQELYN 235
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT-PLANGT---------PEEIRN 243
|
..
gi 501958613 236 LP 237
Cdd:PRK11300 244 NP 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-234 |
1.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKkyPNTTHYA--VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN----DKSPKD-- 76
Cdd:PRK13641 7 NVDYIYS--PGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 RDIAMVFQnyalYPHM-----TVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTE-FLERKPADLSGGQRQRVAMGRAI 150
Cdd:PRK13641 85 KKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 151 VRDAKVFLMDEPLSNLDAKLRVSMrAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSP 230
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEH----------GKLIKHASP 229
|
....
gi 501958613 231 QELY 234
Cdd:PRK13641 230 KEIF 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-209 |
2.55e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIA 80
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNM---------AFGLKLRKYKKddIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIV 151
Cdd:PRK09700 84 IIYQELSVIDELTVLENLyigrhltkkVCGVNIIDWRE--MRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 152 RDAKVFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-235 |
5.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKS------PKDRD 78
Cdd:PRK13646 7 NVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQnyalYPHMTVYDN-----MAFGLKLRKYKKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGRAIVR 152
Cdd:PRK13646 87 IGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 153 DAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE----------GSIVSQTSPKE 232
|
...
gi 501958613 233 LYN 235
Cdd:PRK13646 233 LFK 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-246 |
9.39e-19 |
|
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: 87.87 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKspkDRDIAMVFQNY-ALYPHM---TVY 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsgSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 96 DNMAFGLKlRKYKKDDIDRRVkEAAEI--------LGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAAC-EIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 168 AKLRVSMRAEIAKIHRRigsTTIYVTHDQTEAmTLADRIVIMSAtknpqgngtiGKIEQVGSPQELynLPANKFVAGFI 246
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDH----------GKIIEQGSHDEL--LDRNGFYASLI 706
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-235 |
9.66e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 9.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 1 MVELNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVND---KSPKDR 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 DIAMVFQNYALYPHMTVYDNMAFGLKLRK-YKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIhRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQ----------GHLIAHGTPTEILQ 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-232 |
1.15e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYAL-YPhMTVYDN 97
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-FTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVR------DAKVFLMDEPLSNLDakLR 171
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD--LA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 172 ---VSMRaeIAK--IHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQE 232
Cdd:PRK13548 175 hqhHVLR--LARqlAHER-GLAVIVVLHDLNLAARYADRIVLLHQ----------GRLVADGTPAE 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-208 |
2.64e-18 |
|
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: 86.38 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 9 IYKKYPntthyaveDFDLD-----IKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGElkIDGEVvnDKSPK------DR 77
Cdd:COG1245 347 LTKSYG--------GFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDL--KISYKpqyispDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 78 DiamvfqnyalyphMTVYDNmafglkLRKYKKDDIDRRV--KEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:COG1245 415 D-------------GTVEEF------LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 156 VFLMDEPLSNLDaklrVSMRAEIAKIHRRI----GSTTIYVTHDQTEAMTLADRIVI 208
Cdd:COG1245 476 LYLLDEPSAHLD----VEQRLAVAKAIRRFaenrGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-216 |
2.99e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdgevvndksPKDRDIAMVFQN-Y--------AL-YP 90
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQRpYlplgtlreALlYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 91 HMTvydnmafglklrkykkDDI-DRRVKEAAEILGLTEFLER--KPAD----LSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:COG4178 450 ATA----------------EAFsDAELREALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501958613 164 SNLDAKLRVSMraeIAKIHRRIGSTT-IYVTHdQTEAMTLADRIVIMSATKNPQ 216
Cdd:COG4178 514 SALDEENEAAL---YQLLREELPGTTvISVGH-RSTLAAFHDRVLELTGDGSWQ 563
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-233 |
4.24e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.63 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 9 IYKKYPntthyaveDFDLD-----IKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGElkIDGEVvndkspkdrDIAMVF 83
Cdd:PRK13409 346 LTKKLG--------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPEL---------KISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNmafglkLRKYKKDDIDRRVK-EAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:PRK13409 407 QYIKPDYDGTVEDL------LRSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 163 LSNLDaklrVSMRAEIAKIHRRI----GSTTIYVTHDQTEAMTLADRIVIMSatknpqgnGTIGKIEQVGSPQEL 233
Cdd:PRK13409 481 SAHLD----VEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLMVFE--------GEPGKHGHASGPMDM 543
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-233 |
6.66e-18 |
|
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: 85.26 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYpHMTVYDNMAFGlklrkykKDDIDR 114
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYG-------RPDASE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 115 R-VKEAAEILGLTEFLERKPA-----------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIH 182
Cdd:COG5265 462 EeVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA 541
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 183 RriGSTTIYVTH------DqteamtlADRIVIMSAtknpqgnGTIgkIEQvGSPQEL 233
Cdd:COG5265 542 R--GRTTLVIAHrlstivD-------ADEILVLEA-------GRI--VER-GTHAEL 579
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-238 |
1.18e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.67 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTlrmIAGLEDI-------SEGELKIDGEVVNDKSPKDRDIAMVFQN--YALYPH 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLT---CAAALGIlpagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 92 MTVYDNMAFGLKLRKykKDDIDRRVKEAAEILGLTE---FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:PRK10418 96 HTMHTHARETCLALG--KPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 169 KLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPA 238
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH----------GRIVEQGDVETLFNAPK 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-234 |
1.80e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 26 LDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVnDKSPKD-----RDIAMVFQNyalyPHMTVY----- 95
Cdd:PRK13638 22 LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGllalrQQVATVFQD----PEQQIFytdid 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 96 DNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 175
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 176 AEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PRK13638 177 AIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQ----------GQILTHGAPGEVF 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-208 |
2.08e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKI------------DGEVVND- 71
Cdd:PRK13651 7 NIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkEKEKVLEk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 72 -----------KSPKD--RDIAMVFQ--NYALYpHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTE-FLERKPAD 135
Cdd:PRK13651 87 lviqktrfkkiKKIKEirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501958613 136 LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVI 208
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIF 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-208 |
2.38e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIS--EGELKIDGEVVNDKSPKDRD--- 78
Cdd:PRK13549 6 LEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTErag 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEIL---GLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqlKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501958613 156 VFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRI-VI 208
Cdd:PRK13549 164 LLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTIcVI 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-211 |
2.39e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN--DKSPKDRDIAMVFQN--YALYPHMTVY 95
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 96 DNMAFGLKLR-KYKKDDIDRRVKEAAEILGL-TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVS 173
Cdd:PRK15112 108 QILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD----MS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501958613 174 MRAEIA----KIHRRIGSTTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:PRK15112 184 MRSQLInlmlELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-167 |
2.92e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdGEVVNdkspkdrdIAMVF 83
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYA-LYPHMTVYDNMafglklRKYKKDDIDRRVKEAAEILGLT-EFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG0488 385 QHQEeLDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
....*.
gi 501958613 162 PLSNLD 167
Cdd:COG0488 459 PTNHLD 464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-233 |
3.55e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.54 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 58 SEGELKIDGEVVNDKSPKD-RDIAMVFQNYALYPHMTVYDNMAFGlklrkyKKDDIDRRVKEAAEILGLTEFLERKP--- 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 134 --------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHdQTEAMTLADR 205
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|....*...
gi 501958613 206 IVIMSatkNPQGNGTIgkIEQVGSPQEL 233
Cdd:PTZ00265 1428 IVVFN---NPDRTGSF--VQAHGTHEEL 1450
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-282 |
3.63e-17 |
|
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: 83.46 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVvndkspkdrdiAMVFQNyALYPHMTVYDNMAFGLKL 104
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 105 RKYKKddidRRVKEAAEILGLTEFLE--------RKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL-RVSMR 175
Cdd:TIGR00957 726 NEKYY----QQVLEACALLPDLEILPsgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFE 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 176 AEIAKIHRRIGSTTIYVTHDQTeAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELynLPANKFVAGFIGSPAMNFFE 255
Cdd:TIGR00957 802 HVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSG----------GKISEMGSYQEL--LQRDGAFAEFLRTYAPDEQQ 868
|
250 260
....*....|....*....|....*..
gi 501958613 256 VVVKDGQIISEDGldiaiPEGQAKMLE 282
Cdd:TIGR00957 869 GHLEDSWTALVSG-----EGKEAKLIE 890
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-212 |
6.52e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNdKSPKDRDIAMVFQNYAL---YP---- 90
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNLVAYVPQSEEVdwsFPvlve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 91 ---HMTVYDNMAFglkLRKYKKDDiDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK15056 99 dvvMMGRYGHMGW---LRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 501958613 168 AKLRVSMRAEIAKIhRRIGSTTIYVTHDQTEAMTLADRIVIMSAT 212
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGT 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-239 |
6.82e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 32 EFIVFVGPSGCGKSTTLRMIAGLediSEGELKIDGEVVNDKSPKDRDI-----AMVFQNYALYPHMTVYDNMAFGLKLR- 105
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGMPIDAKEmraisAYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 106 --KYKKDDIDRRVKEAAEILGLtefleRKPAD-----------LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklrv 172
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLQALGL-----RKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS---- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 173 SMRAEIAKIHRRI---GSTTIYVTHDQT-EAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL--------YNLPAN 239
Cdd:TIGR00955 200 FMAYSVVQVLKGLaqkGKTIICTIHQPSsELFELFDKIILMAE----------GRVAYLGSPDQAvpffsdlgHPCPEN 268
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-194 |
1.08e-16 |
|
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: 77.92 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 32 EFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK-DRDIAMVFQNYALYPHMTVYDNMAFglklrkYKKD 110
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRF------WHAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 111 DIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaKLRVSMRAEIAKIHRRIGSTTI 190
Cdd:cd03231 101 HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVARFAEAMAGHCARGGMVV 179
|
....
gi 501958613 191 YVTH 194
Cdd:cd03231 180 LTTH 183
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-168 |
1.20e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.69 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 7 KHIYKKYPNTTHYAV-EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK--DRDIAMVF 83
Cdd:TIGR00958 482 QDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHmTVYDNMAFGLklRKYKKDDIDRRVKEAAEILGLTEF-------LERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:TIGR00958 562 QEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFpngydteVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170
....*....|..
gi 501958613 157 FLMDEPLSNLDA 168
Cdd:TIGR00958 639 LILDEATSALDA 650
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-196 |
2.26e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 17 THYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEdiSEGELKIDGEVVNDKSPKDRDIAmvfqnyalyphmtvyd 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--KGTPVAGCVDVPDNQFGREASLI---------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 97 nmafglklrkykkDDIDRR--VKEAAEIL---GLTE--FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:COG2401 104 -------------DAIGRKgdFKDAVELLnavGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*..
gi 501958613 170 LRVSMRAEIAKIHRRIGSTTIYVTHDQ 196
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
38-209 |
4.34e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 38 GPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSP---KDRDIAMVFQNYALYPHMTVYDNMAFGLKlrkyKKDDIDR 114
Cdd:PRK15439 44 GGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPLLFPNLSVKENILFGLP----KRQASMQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 115 RVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklrvsmrAEIAKIHRRI------GST 188
Cdd:PRK15439 120 KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP-------AETERLFSRIrellaqGVG 192
|
170 180
....*....|....*....|.
gi 501958613 189 TIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK15439 193 IVFISHKLPEIRQLADRISVM 213
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
247-300 |
5.25e-16 |
|
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: 71.46 E-value: 5.25e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 247 GSPAMNFFEV-VVKDGQIISEDGLDIAIPEGQAkmLEAAGYKDKKVIFGIRPEDI 300
Cdd:pfam17912 1 GSPPMNFLPAtVVEDGLLVLGGGVTLPLPEGQV--LALKLYVGKEVILGIRPEHI 53
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-230 |
6.56e-16 |
|
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: 75.99 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 12 KYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTT----LRMIagleDISEGELKIDGEVVNDKSPKD--RDIAMVFQN 85
Cdd:cd03244 11 RYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 86 YALYPHmTVYDNMA-FGLKlrkykkddIDRRVKEAAEILGLTEFLERKP-----------ADLSGGQRQRVAMGRAIVRD 153
Cdd:cd03244 87 PVLFSG-TIRSNLDpFGEY--------SDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 154 AKVFLMDEPLSNLD----AKLRVSMRAEIAkihrriGSTTIYVTHdQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGS 229
Cdd:cd03244 158 SKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDK----------GRVVEFDS 220
|
.
gi 501958613 230 P 230
Cdd:cd03244 221 P 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-210 |
6.97e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVvNDKSPKDRDIAMVFQNYALYPHMTVYDNMAF--GL 102
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRFMAYLGHLPGLKADLSTLENLHFlcGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 103 KLRKYKkddidRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlRVSMRAEIAKIH 182
Cdd:PRK13543 110 HGRRAK-----QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAH 183
|
170 180
....*....|....*....|....*...
gi 501958613 183 RRIGSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK13543 184 LRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-234 |
9.32e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 9.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG--------EVV--NDKSPKD------RDIAMVF 83
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIelSEQSAAQmrhvrgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QN--YALYPHMTVYDNMAFGLKLRK-YKKDDIDRRVKEAAEILGLTE---FLERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSatknpQGNGT-IGKIEQV-GSPQELY 234
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY-----QGEAVeTGSVEQIfHAPQHPY 264
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-209 |
9.93e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.29 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDkspkdrDIAMVF 83
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTVYDNMAFG-------LKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-209 |
1.40e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK---DRDIAMV 82
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEI---LGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501958613 160 DEPLSNLDAKLRVSMRAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITIL 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-210 |
3.45e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEfIVFV-GPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRDIAMVF------QNYALYPHM 92
Cdd:COG3845 273 ALKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 93 TVYDNMAfglkLRKYKKDD------IDRR-VKEAAEILgLTEF------LERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:COG3845 352 SVAENLI----LGRYRRPPfsrggfLDRKaIRAFAEEL-IEEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 160 DEPLSNLDAklrvsmrAEIAKIHRRI------GSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:COG3845 427 AQPTRGLDV-------GAIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMY 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-210 |
4.37e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---RDIAMVFQNY---ALYPHMTV 94
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFG--LKLRKYK------KDDIDRRVKEAA-EILGLT-EFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK09700 359 AQNMAISrsLKDGGYKgamglfHEVDEQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501958613 165 NLDaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK09700 439 GID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFC 483
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-248 |
5.68e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.15 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL---EDISEGELKIDG-EVVN---DKSPKDR--DIAMVFQN--YAL 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGrEILNlpeKELNKLRaeQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 89 YPHMTVYDNMAFGLKLRKY--KKDDIDRRVK--EAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGmsKAEAFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 165 NLDaklrVSMRAEIA----KIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANK 240
Cdd:PRK09473 191 ALD----VTVQAQIMtllnELKREFNTAIIMITHDLGVVAGICDKVLVMYA----------GRTMEYGNARDVFYQPSHP 256
|
....*...
gi 501958613 241 FVAGFIGS 248
Cdd:PRK09473 257 YSIGLLNA 264
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-205 |
6.48e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 16 TTHY----AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDkSPKDR----DIAMVFQNYA 87
Cdd:PRK11614 12 SAHYgkiqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKimreAVAIVPEGRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHMTVYDNMAFGLKLRKykKDDIDRRVKEAAEILG-LTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:PRK11614 91 VFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 501958613 167 DAKLRVSMRAEIAKIhRRIGSTTIYVTHDQTEAMTLADR 205
Cdd:PRK11614 169 APIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADR 206
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-237 |
6.51e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.90 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 13 YPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVND---KSPKDRdIAMVFQNYALY 89
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqlDSWRSR-LAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHmTVYDNMAFGlklrkyKKDDIDRRVKEAA-------EILGL-----TEFLERKpADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK10789 402 SD-TVANNIALG------RPDATQQEIEHVArlasvhdDILRLpqgydTEVGERG-VMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 158 LMDEPLSNLDAKlrvsMRAEIAKIHRRIGST-TIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNL 236
Cdd:PRK10789 474 ILDDALSAVDGR----TEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQH----------GHIAQRGNHDQLAQQ 539
|
.
gi 501958613 237 P 237
Cdd:PRK10789 540 S 540
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-247 |
9.96e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 36 FVGPSGCGKSTTLRMIAGLEDISEGeLKIDGEVV---------NDKSPKDRDIAMVFQNYALYPhMTVYDNMAFGLKL-- 104
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrsifnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAhk 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 105 ---RKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKI 181
Cdd:PRK14271 130 lvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 182 HRRIgsTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPAN----KFVAGFIG 247
Cdd:PRK14271 210 ADRL--TVIIVTHNLAQAARISDRAALFFD----------GRLVEEGPTEQLFSSPKHaetaRYVAGLSG 267
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-169 |
1.11e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNdkspKDRDiamVFQNYALY--------PHMT 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 94 VYDNMAFGLKLRKYKKDDidrRVKEAAEILGLTEFlERKPAD-LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGF-EDVPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-210 |
1.18e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---RDIAMVFQNY---ALYPHMTVY 95
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 96 DNMA---------FGLKLRKYKKDDIDRRVKEAAEILglTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:PRK11288 350 DNINisarrhhlrAGCLINNRWEAENADRFIRSLNIK--TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501958613 167 DaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK11288 428 D----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMR 470
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-196 |
1.56e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.41 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVED------FDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ISEGELKIDGEVVNDKSPKDR---DIAMVFQNY 86
Cdd:COG0396 7 HVSVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 ALYPHMTVYD--NMAFGlKLRKYKKDDID--RRVKEAAEILGL-TEFLERkPAD--LSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:COG0396 87 VEIPGVSVSNflRTALN-ARRGEELSAREflKLLKEKMKELGLdEDFLDR-YVNegFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 501958613 160 DEPLSNLDA-KLRVsMRAEIAKIHRRiGSTTIYVTHDQ 196
Cdd:COG0396 165 DETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQ 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-209 |
2.03e-14 |
|
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: 74.48 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL--EDISEGELKIDGEVVNDKSPKDRD--- 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTErag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFG----LKLRKYKKDDIDRRVKEAAEILGLTEFLERKP-ADLSGGQRQRVAMGRAIVRD 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 154 AKVFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-210 |
2.62e-14 |
|
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: 71.14 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGledISEGELKIDGEVVND-------KSPKD 76
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYNgipykefAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 77 RDIAMVFQNYALYPHMTVYDNMAFGLKLRKykkDDIDRRVkeaaeilglteflerkpadlSGGQRQRVAMGRAIVRDAKV 156
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNLDaklrvSMRA-EIAKIHR---RIGSTTIYVTHDQT--EAMTLADRIVIMS 210
Cdd:cd03233 140 LCWDNSTRGLD-----SSTAlEILKCIRtmaDVLKTTTFVSLYQAsdEIYDLFDKVLVLY 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-209 |
3.29e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.05 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGledisegELKID-GEVvnDKSPKDRDIAMVFQNYALYPHMT-VYDNmafglKLRKYKK----D 110
Cdd:COG1245 105 LGPNGIGKSTALKILSG-------ELKPNlGDY--DEEPSWDEVLKRFRGTELQDYFKkLANG-----EIKVAHKpqyvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 111 DIDRRVK-----------------EAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:COG1245 171 LIPKVFKgtvrellekvdergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 501958613 174 MraeiAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1245 251 V----ARLIRELaeeGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-233 |
3.63e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 24 FDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiSEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHMTVYDNMAFG 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 LKlRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVR-------DAKVFLMDEPLSNLDAKLRVSM 174
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 175 RAEIAKIHRRiGSTTIYVTHDQTEAMTLADRIVIMSatknpqgNGTI---GKIEQVGSPQEL 233
Cdd:COG4138 173 DRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLK-------QGKLvasGETAEVMTPENL 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
38-194 |
5.64e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 38 GPSGCGKSTTLRMIAGLEDISEGELKIDGEVVN-DKSPKDRDIAMVFQNYALYPHMTVYDNMAFGLKLrkykkDDIDRRV 116
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF-----SPGAVGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 117 KEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlrvSMRAEIAKI--HRRIGSTTIYVTH 194
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL---SLLTIITKIqeHRAKGGAVLLTSH 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-255 |
1.14e-13 |
|
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: 70.09 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 16 TTH-YAVEDFDLD----IKDKEFIVFVGPSGCGKSTTLRMIAGledisegELKID-GEvvNDKSPKDRDIAMVFQNYALY 89
Cdd:cd03236 6 PVHrYGPNSFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAG-------KLKPNlGK--FDDPPDWDEILDEFRGSELQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHMTVYDNMafglKLRKYKK----DDIDRRVK-----------------EAAEILGLTEFLERKPADLSGGQRQRVAMGR 148
Cdd:cd03236 77 NYFTKLLEG----DVKVIVKpqyvDLIPKAVKgkvgellkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 149 AIVRDAKVFLMDEPLSNLDAKLRVSMraeiAKIHRRIGSTTIY---VTHDQTEAMTLADRIVIMSATKNPQGNGTIGKIE 225
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKQRLNA----ARLIRELAEDDNYvlvVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSV 228
|
250 260 270
....*....|....*....|....*....|
gi 501958613 226 QVGspqelynlpANKFVAGFIGSPAMNFFE 255
Cdd:cd03236 229 REG---------INEFLDGYLPTENMRFRE 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-209 |
1.49e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.06 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPK--DRDIAMVFQNYALYPHmTVYDNMA 99
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 100 FGlklrkykKDDIDRRVKEAAEILGLTEFLERKPA-----------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:PRK10790 437 LG-------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501958613 169 KLRVSMRAEIAKIHRRigsTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10790 510 GTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVL 547
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-215 |
2.41e-13 |
|
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: 67.18 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdgevvndksPKDRDIAMVFQNyalyPHMTVydnmaf 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLPL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 GLkLRK---YKKDDIdrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAE 177
Cdd:cd03223 78 GT-LREqliYPWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 501958613 178 IAKIHRRIGSTTIYVTHdQTEAMTLADRIVIMSATKNP 215
Cdd:cd03223 130 LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-209 |
3.24e-13 |
|
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: 68.13 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD------IAMVFQNYALYpHMTV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFGLKLRKykkddidRRVKEAAEILGL------------TEFLERKpADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03290 96 EENITFGSPFNK-------QRYKAVTDACSLqpdidllpfgdqTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501958613 163 LSNLDAKLRVS-MRAEIAKIHRRIGSTTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03290 168 FSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAM 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-209 |
3.91e-13 |
|
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: 69.12 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEvvndkspkdrdIAMVFQNYALYPHmTVYDNMAF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 GLKLRKYKKDDIDRRVKEAAEILGLTE----FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRA 176
Cdd:cd03291 121 GVSYDEYRYKSVVKACQLEEDITKFPEkdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD----VFTEK 196
|
170 180 190
....*....|....*....|....*....|....*
gi 501958613 177 EIAK--IHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03291 197 EIFEscVCKLMANKTRILVTSKMEHLKKADKILIL 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-237 |
4.57e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED----ISEGELKIDGEVVNDKSPKDR------DIAMVFQN--YA 87
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHMTVYDNMAFGLKL-----RKYKKDdidrRVKEAAEILGL---TEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVhqggnKKTRRQ----RAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 160 DEPLSNLDaklrVSMRAEIA----KIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:PRK11022 178 DEPTTALD----VTIQAQIIelllELQQKENMALVLITHDLALVAEAAHKIIVMYA----------GQVVETGKAHDIFR 243
|
..
gi 501958613 236 LP 237
Cdd:PRK11022 244 AP 245
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-245 |
4.62e-13 |
|
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: 66.83 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 27 DIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNdkspkdrdiamvfqnyalyphmtvydnmafglklrk 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 107 YKKDDIDrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIG 186
Cdd:cd03222 65 YKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 187 STTIYVTHDQTEAMTLADRIVIMSAtkNPQGNGTIGKieqvgsPQELYNlPANKFVAGF 245
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEG--EPGVYGIASQ------PKGTRE-GINRFLRGY 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-209 |
5.75e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGledisegELKIDGEVVNDKSPKDRDIAMvFQNYALYPHMT-VYDNmafglKLRKYKK----DD 111
Cdd:PRK13409 105 LGPNGIGKTTAVKILSG-------ELIPNLGDYEEEPSWDEVLKR-FRGTELQNYFKkLYNG-----EIKVVHKpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 112 IDRRVK-----------------EAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK13409 172 IPKVFKgkvrellkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 501958613 175 raeiAKIHRRI--GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK13409 252 ----ARLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-235 |
5.86e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLR-MIAGLEDISEGELKIDGEVvndkspkdrdiAMVFQNYALYpHMTVYDNMAFG 101
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 LKL---RKYKKDDIDRRVKEAAEILG--LTEFLERKpADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklRVSMRA 176
Cdd:PLN03130 703 SPFdpeRYERAIDVTALQHDLDLLPGgdLTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA--HVGRQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 177 EIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYN 235
Cdd:PLN03130 780 FDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHE----------GMIKEEGTYEELSN 828
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-209 |
6.64e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKidgevvndkspKDRDIAMVFQNyALYPHMTVYDNMAFGL 102
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 103 KLRKYKKDDIDRRVKEAAEILGLTEFLE----RKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL--RVSMRA 176
Cdd:PTZ00243 746 EEDAARLADAVRVSQLEADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRVVEEC 825
|
170 180 190
....*....|....*....|....*....|...
gi 501958613 177 EIAKIHrriGSTTIYVTHdQTEAMTLADRIVIM 209
Cdd:PTZ00243 826 FLGALA---GKTRVLATH-QVHVVPRADYVVAL 854
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-207 |
7.60e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 25 DLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAmvfqnyalyphMTVYDNMAFGL 102
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNVE-----------GTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 103 K-----LRKYK---------------------KDDIDR--------RVKEAAEILGLTEflERKPADLSGGQRQRVAMGR 148
Cdd:PRK11147 92 EeqaeyLKRYHdishlvetdpseknlnelaklQEQLDHhnlwqlenRINEVLAQLGLDP--DAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 149 AIVRDAKVFLMDEPLSNLDaklrvsmraeIAKIH------RRIGSTTIYVTHDQTEAMTLADRIV 207
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD----------IETIEwlegflKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-167 |
8.92e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 28 IKDKEFIVFVGPSGCGKSTTLRMIAGLEDiSEGELKIDGEVVNDKSPKD----RD---------IAM-VFQNYALYPHmt 93
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLHQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 vydnmafglklRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVR-------DAKVFLMDEPLSNL 166
Cdd:PRK03695 96 -----------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
.
gi 501958613 167 D 167
Cdd:PRK03695 165 D 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-277 |
1.09e-12 |
|
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: 69.06 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDI--SEGEL---------------------------------KI 64
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvgepcpvcggtlepeEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 65 DGEVVNDKSPKD--RDIAMVFQ-NYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQR 141
Cdd:TIGR03269 95 DFWNLSDKLRRRirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 142 QRVAMGRAIVRDAKVFLMDEPLSNLD---AKLRVSMRAEIAKIHrrigSTTIYVTHDQTEAMT-LADRIVIMSAtknpqg 217
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAVKAS----GISMVLTSHWPEVIEdLSDKAIWLEN------ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 218 ngtiGKIEQVGSPQELynlpANKFVAGF----------IGSPAMNFFEV-----VVKDGQIISEDGLDIAIPEGQ 277
Cdd:TIGR03269 245 ----GEIKEEGTPDEV----VAVFMEGVsevekeceveVGEPIIKVRNVskryiSVDRGVVKAVDNVSLEVKEGE 311
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-209 |
1.10e-12 |
|
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: 67.16 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDG------EVVNDKSPKDRDIA-----MVFQNYALYPH 91
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelELYQLSEAERRRLMrtewgFVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 92 MTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEF----LERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:TIGR02323 101 MRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdptrIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 168 aklrVSMRAEIAKIHRRI----GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02323 181 ----VSVQARLLDLLRGLvrdlGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
1.26e-12 |
|
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: 64.78 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNttHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELkidgevvndKSPKDRDIAMVF 83
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------TWGSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QnyalyphmtvydnmafglklrkykkddidrrvkeaaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRrigsTTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-209 |
1.48e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKI---DGEVVN--DKSPKDR------DIAMVFQNYA- 87
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDlyALSEAERrrllrtEWGFVHQHPRd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 -LYPHMTVYDN-----MAFGLklRKYkkddidRRVKEAAeilglTEFLER----------KPADLSGGQRQRVAMGRAIV 151
Cdd:PRK11701 101 gLRMQVSAGGNigerlMAVGA--RHY------GDIRATA-----GDWLERveidaariddLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 152 RDAKVFLMDEPLSNLDaklrVSMRAEIAKIHRRI----GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK11701 168 THPRLVFMDEPTGGLD----VSVQARLLDLLRGLvrelGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-211 |
1.53e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 6 LKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIS----EGELKIDGEVVNDKSPKDR-DIA 80
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRgDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLRK--------YKKDDIDRRVKEAAEILGLTEFLERKPAD-----LSGGQRQRVAMG 147
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFAARCKTpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 148 RAIVRDAKVFLMDEPLSNLDAklrvSMRAEIAKIHR---RIGSTTIYVTHDQT--EAMTLADRIVIMSA 211
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDS----ATALEFIRALKtsaNILDTTPLVAIYQCsqDAYELFDKVIVLYE 286
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-209 |
3.13e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.40 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEvvndkspkdrdIAMVFQNYALYPHmTVYDNMAF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 GLKLRKYKKDDIDRRVKEAAEILGLTE----FLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRA 176
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQLEEDIALFPEkdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VVTEK 585
|
170 180 190
....*....|....*....|....*....|....*
gi 501958613 177 EIAK--IHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR01271 586 EIFEscLCKLMSNKTRILVTSKLEHLKKADKILLL 620
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-234 |
5.01e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 16 TTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLR-MIAGLEDISEGELKIDGEVVndKSPKdrdIAMVFqnyalypHMTV 94
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVA--YVPQ---VSWIF-------NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFGLKL---RKYKKDDIDRRVKEAAEILG--LTEFLERKpADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:PLN03232 696 RENILFGSDFeseRYWRAIDVTALQHDLDLLPGrdLTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 170 LRVSMRAEIAKiHRRIGSTTIYVThDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELY 234
Cdd:PLN03232 775 VAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSE----------GMIKEEGTFAELS 827
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-211 |
7.71e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTThYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIA 80
Cdd:PRK10522 322 TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMtvydnmafglkLRKYKKDDIDRRVKEAAEILGLTEFLERKPA-----DLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK10522 401 AVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHDQtEAMTLADRIVIMSA 211
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRN 524
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-171 |
9.60e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 9.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 24 FDLDIK--DKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNdKSPKDRdIAMVFQNYALYPHMTVYDNMAFG 101
Cdd:PRK13541 17 FDLSITflPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-NIAKPY-CTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 102 LKLRkykkdDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:PRK13541 95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-167 |
1.28e-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: 65.73 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIdGEVVndkspkdrDIAMVFQNY-ALYPHMTVYDNMAFGLKLRKYKKDDIDRR 115
Cdd:TIGR03719 354 IGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSR 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 116 VkeaaeILGLTEFL----ERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:TIGR03719 425 A-----YVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-168 |
1.95e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 32 EFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdgeVVNDKSPKD---RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYK 108
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTI---LANNRKPTKqilKRTGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 109 ---KDDIDRRVKEAAEILGLTE---------FLErkpaDLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:PLN03211 172 sltKQEKILVAESVISELGLTKcentiignsFIR----GISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-230 |
2.34e-11 |
|
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: 62.43 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 28 IKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHmTVYDNM-AFGlkl 104
Cdd:cd03369 31 VKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRSNLdPFD--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 105 rKYKKDDIDR--RVKEAAEilglteflerkpaDLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAK-I 181
Cdd:cd03369 107 -EYSDEEIYGalRVSEGGL-------------NLSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALIQKtI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501958613 182 HRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSP 230
Cdd:cd03369 169 REEFTNSTILTIAHRLRTIIDYDKILVMDA----------GEVKEYDHP 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-214 |
3.30e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 22 EDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKI-DGEVVNDKSPK--DRDIAMVFQNYALYPHmTVYDNM 98
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 AFGL-------KLRKY-------KKDDIDRRVKEAAEILGL----------TEFLERK---------------------- 132
Cdd:PTZ00265 481 KYSLyslkdleALSNYynedgndSQENKNKRNSCRAKCAGDlndmsnttdsNELIEMRknyqtikdsevvdvskkvlihd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 133 ----------------PADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGSTTIYVTHdQ 196
Cdd:PTZ00265 561 fvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-R 639
|
250
....*....|....*...
gi 501958613 197 TEAMTLADRIVIMSATKN 214
Cdd:PTZ00265 640 LSTIRYANTIFVLSNRER 657
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-233 |
5.11e-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: 64.05 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKYPNTTHYAVEDFDLDIKDKEfIVF-VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD-RD-IAM 81
Cdd:COG4615 332 GVTYRYPGEDGDEGFTLGPIDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQlFSA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQNYALYPHMTVYDNMAFGLKLRKY-KKDDIDRRVKEAAEILGLTeflerkpaDLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG4615 411 VFSDFHLFDRLLGLDGEADPARARELlERLELDHKVSVEDGRFSTT--------DLSQGQRKRLALLVALLEDRPILVFD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 161 E------P----------LSNLdaklrvsmraeiakihRRIGSTTIYVTHDQTeAMTLADRIVIMSAtknpqgngtiGKI 224
Cdd:COG4615 483 EwaadqdPefrrvfytelLPEL----------------KARGKTVIAISHDDR-YFDLADRVLKMDY----------GKL 535
|
....*....
gi 501958613 225 EQVGSPQEL 233
Cdd:COG4615 536 VELTGPAAL 544
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-209 |
5.23e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTT----LRMIAGLEDI-SEGELKIDGE-VVNDKSPKDR-----DIAMVFQN--YA 87
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGEsLLHASEQTLRgvrgnKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHMTVYDNMAFGLKLRKYKKddidrrvKEAA--EILGLtefLERK------------PADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSLHRGMR-------REAArgEILNC---LDRVgirqaakrltdyPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 154 AKVFLMDEPLSNLDaklrVSMRAEI----AKIHRRIGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK15134 175 PELLIADEPTTALD----VSVQAQIlqllRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-196 |
7.36e-11 |
|
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: 61.00 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVED------FDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ISEGELKIDGEVVNDKSPKDR---DIAMVFQNY 86
Cdd:cd03217 7 HVSVGGkeilkgVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 ALYPhmtvydnmafGLKLRKYKkddidRRVKEAaeilglteflerkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:cd03217 87 PEIP----------GVKNADFL-----RYVNEG----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190
....*....|....*....|....*....|..
gi 501958613 167 DAklrVSMR--AEIAKIHRRIGSTTIYVTHDQ 196
Cdd:cd03217 136 DI---DALRlvAEVINKLREEGKSVLIITHYQ 164
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-209 |
8.42e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD---RDIAMVFQNY---ALYPHMTV 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 95 YDNMAFgLKLRKYKKDDIdrRVKEAAEILGLTEFLE----RKPA------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK10762 348 KENMSL-TALRYFSRAGG--SLKHADEQQAVSDFIRlfniKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501958613 165 NLDaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10762 425 GVD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-233 |
1.29e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 5 NLKHIYKKypnTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR---DIAM 81
Cdd:NF033858 6 GVSHRYGK---TV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 82 VFQ----NyaLYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:NF033858 81 MPQglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 158 LMDE------PLSnldaklrvsmRAE----IAKIHRRIGSTTIYVThdqTEAMTLADR---IVIMSAtknpqgngtiGKI 224
Cdd:NF033858 159 ILDEpttgvdPLS----------RRQfwelIDRIRAERPGMSVLVA---TAYMEEAERfdwLVAMDA----------GRV 215
|
....*....
gi 501958613 225 EQVGSPQEL 233
Cdd:NF033858 216 LATGTPAEL 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-207 |
1.66e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKidgevvndKSPKDRdIAMVFQNYALYPHM--TVYDNMaf 100
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQKLYLDTTLplTVNRFL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 101 glKLRK-YKKDDID---RRVKEAaeilgltEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRA 176
Cdd:PRK09544 91 --RLRPgTKKEDILpalKRVQAG-------HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|.
gi 501958613 177 EIAKIHRRIGSTTIYVTHDQTEAMTLADRIV 207
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-208 |
4.69e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIS--EGELKIDGEVVNDKSPKD---RD 78
Cdd:NF040905 2 LEMRGITKTFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDseaLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEIL---GLTEFLERKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLakvGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 156 VFLMDEPLSNLDAK-------LRVSMRAEiakihrriGSTTIYVTHDQTEAMTLADRIVI 208
Cdd:NF040905 160 LLILDEPTAALNEEdsaalldLLLELKAQ--------GITSIIISHKLNEIRRVADSITV 211
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-209 |
4.82e-10 |
|
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: 58.41 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDIS--EGELKIDGevvndkSPKD----RDIAMVFQNYALYPHMTVYDNMAFGLKLRkykkd 110
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTAGviTGEILING------RPLDknfqRSTGYVEQQDVHSPNLTVREALRFSALLR----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 111 didrrvkeaaeilglteflerkpaDLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklrvSMRAEIAKIHRRIGST-- 188
Cdd:cd03232 108 ------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVRFLKKLADSgq 159
|
170 180
....*....|....*....|...
gi 501958613 189 TIYVTHDQTEAMTLA--DRIVIM 209
Cdd:cd03232 160 AILCTIHQPSASIFEkfDRLLLL 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-209 |
9.59e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYA-VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGL-EDISEGELKIDGEVVNDKSPKD---RD 78
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQN---YALYPHMTVYDNMAFGLkLRKYKKDDidrRVKEAAEILGLTEFLER------KP----ADLSGGQRQRVA 145
Cdd:TIGR02633 338 IAMVPEDrkrHGIVPILGVGKNITLSV-LKSFCFKM---RIDAAAELQIIGSAIQRlkvktaSPflpiGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 146 MGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVD----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-167 |
1.46e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 34 IVFV-GPSGCGKSTTLRMIAGLEDISEGELKIdGEVVndkspkdrDIAMVFQNY-ALYPHMTVYDNMAFGLKLRKYKKDD 111
Cdd:PRK11819 352 IVGIiGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNRE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 112 IDRRVKEAAeilglteF------LERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK11819 423 IPSRAYVGR-------FnfkggdQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-209 |
2.90e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTThyAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDRD---IA 80
Cdd:PRK10762 5 LQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 81 MVFQNYALYPHMTVYDNMAFGLKLR-KYKKDDIDRRVKEAAEIL---GLTEFLERKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKLLarlNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 157 FLMDEPLSNL-----DAKLRV--SMRAEiakihrriGSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10762 163 IIMDEPTDALtdtetESLFRVirELKSQ--------GRGIVYISHRLKEIFEICDDVTVF 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-167 |
4.02e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLE--DISEGELKIDGEVVNDKSPKDRD---IAMVFQNYALYPHMTVY 95
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 96 D--NMAFGLKLRKYKKDDID-----RRVKEAAEILGLTE-FLERKPAD-LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:CHL00131 103 DflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
.
gi 501958613 167 D 167
Cdd:CHL00131 183 D 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-195 |
5.20e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 2 VELNLKHIYKKY------------------PNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELK 63
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipkhKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 64 IDGEVvndkspkdrdiAMVFQNYALYPHMTVYDNMAFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQR 143
Cdd:PRK13546 83 RNGEV-----------SVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501958613 144 VAMGRAIVRDAKVFLMDEPLSNLDAKLrvsMRAEIAKIH--RRIGSTTIYVTHD 195
Cdd:PRK13546 152 LGFSINITVNPDILVIDEALSVGDQTF---AQKCLDKIYefKEQNKTIFFVSHN 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-167 |
6.51e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLR-MIAGLEDISeGELKIDGEVvndkspkdrDIAMvFQNY--ALYPHMTVYDN 97
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTKL---------EVAY-FDQHraELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAFGlklrkykKDDI-----DRRVkeaaeiLG-LTEFL-----ERKPAD-LSGGQRQRVAMGRAIVRDAKVFLMDEPLSN 165
Cdd:PRK11147 404 LAEG-------KQEVmvngrPRHV------LGyLQDFLfhpkrAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
..
gi 501958613 166 LD 167
Cdd:PRK11147 471 LD 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-195 |
6.87e-09 |
|
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: 57.25 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 34 IVFVGPSGCGKSTTLRMIAGLEDISEGELKIDgevvndkspKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKD--- 110
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------PGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 111 ---------------------------------DIDRRVKEAAEILGLTEFlERKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:TIGR03719 105 eisakyaepdadfdklaaeqaelqeiidaadawDLDSQLEIAMDALRCPPW-DADVTKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 501958613 158 LMDEPLSNLDAKlrvSMrAEIAKIHRRIGSTTIYVTHD 195
Cdd:TIGR03719 184 LLDEPTNHLDAE---SV-AWLERHLQEYPGTVVAVTHD 217
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-194 |
2.91e-08 |
|
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: 55.53 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIdgevvndksPKDRDIAMVFQNyalyPHMT------- 93
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTlgtlrdq 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 -VYDNMAFGLKLRKYKkddiDRRVKEAAEILGLTEFLERKP-----AD----LSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:TIGR00954 535 iIYPDSSEDMKRRGLS----DKDLEQILDNVQLTHILEREGgwsavQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 501958613 164 SnldaKLRVSMRAEIAKIHRRIGSTTIYVTH 194
Cdd:TIGR00954 611 S----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-209 |
6.54e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKDR-DIAMVF-----QNYALYPHMT--- 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPlaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 94 -----VYDNMAFGLKLRKykkddiDRRVKEA-AEILGLTEFLERKPA-DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:PRK15439 361 nvcalTHNRRGFWIKPAR------ENAVLERyRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501958613 167 DaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK15439 435 D----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-209 |
8.46e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 58 SEGELKIDGEVVNDKSPKD---RDIAMVFQN---YALYPHMTVYDNMAFGLkLRKYKKDdidRRVKEAAEILGLTEFLER 131
Cdd:PRK13549 316 WEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITLAA-LDRFTGG---SRIDDAAELKTILESIQR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 132 ----------KPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAKIHRRI---GSTTIYVTHDQTE 198
Cdd:PRK13549 392 lkvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPE 467
|
170
....*....|.
gi 501958613 199 AMTLADRIVIM 209
Cdd:PRK13549 468 VLGLSDRVLVM 478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
37-241 |
1.12e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALY---------PHMTVYDNMAFGLKLR 105
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFsgtvrfnidPFSEHNDADLWEALER 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 106 KYKKDDIDRRVkeaaeiLGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAK-IHRR 184
Cdd:PLN03232 1348 AHIKDVIDRNP------FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQRtIREE 1417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 185 IGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKF 241
Cdd:PLN03232 1418 FKSCTMLVIAHRLNTIIDCDKILVLSS----------GQVLEYDSPQELLSRDTSAF 1464
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-209 |
1.66e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 52.60 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED----ISEGELKIDGEVVNDKSPKDR------DIAMVFQN--YA 87
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 88 LYPHMTVYDNMAFGLKLRKYKKDDIDR---RVKEAAEIL---GLTE---FLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:COG4170 102 LDPSAKIGDQLIEAIPSWTFKGKWWQRfkwRKKRAIELLhrvGIKDhkdIMNSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 159 MDEPLSNLDAKLRvsmraeiAKIHR------RIGSTTI-YVTHDQTEAMTLADRIVIM 209
Cdd:COG4170 182 ADEPTNAMESTTQ-------AQIFRllarlnQLQGTSIlLISHDLESISQWADTITVL 232
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
294-368 |
1.90e-07 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 48.00 E-value: 1.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 294 GIRPEDISsnqiVHDtyPNANVTAEVLVSELLGSETMLYVKL-GQTEFASRVDA--RDFHNPGEKVSLTFNVAKGHFF 368
Cdd:pfam08402 2 AIRPEKIR----LAA--AANGLSGTVTDVEYLGDHTRYHVELaGGEELVVRVPNahARPPAPGDRVGLGWDPEDAHVL 73
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-233 |
2.50e-07 |
|
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: 53.03 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 12 KYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALY 89
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 90 PHMTVYDNMAFGlklrKYKKDDidrrVKEAAEILGLTEFLERKPA-----------DLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:TIGR00957 1373 SGSLRMNLDPFS----QYSDEE----VWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 159 MDEPLSNLDAKLRVSMRAeiakihrrigstTIYVTHDQTEAMTLADRI-VIMSATKnpqgngTI----GKIEQVGSPQEL 233
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQS------------TIRTQFEDCTVLTIAHRLnTIMDYTR------VIvldkGEVAEFGAPSNL 1506
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-167 |
4.13e-07 |
|
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: 52.22 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiSEGELKIDGEVVNDKSPKDRDIAmv 82
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 fqnYALYPHMTVYDNMAFGLKLRKYKKDDiDRRVKEAAEILGLTEFLERKPADL-----------SGGQRQRVAMGRAIV 151
Cdd:TIGR01271 1294 ---FGVIPQKVFIFSGTFRKNLDPYEQWS-DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369
|
170
....*....|....*.
gi 501958613 152 RDAKVFLMDEPLSNLD 167
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLD 1385
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-168 |
4.70e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLEDISEGELKIDgevvndkspKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYKKD------ 110
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEGEARPA---------PGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDrfneiy 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 111 ------------------------------DIDRRVKEAAEILGLteflerKPAD-----LSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK11819 110 aayaepdadfdalaaeqgelqeiidaadawDLDSQLEIAMDALRC------PPWDakvtkLSGGERRRVALCRLLLEKPD 183
|
170
....*....|...
gi 501958613 156 VFLMDEPLSNLDA 168
Cdd:PRK11819 184 MLLLDEPTNHLDA 196
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-235 |
5.26e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.62 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIsEGELKIDGEVVNDKSPKDRDIAmv 82
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 fqnYALYPHMTVYDNMAFGLKLRKYKKDDiDRRVKEAAEILGLTEFLERKPADL-----------SGGQRQRVAMGRAIV 151
Cdd:cd03289 79 ---FGVIPQKVFIFSGTFRKNLDPYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 152 RDAKVFLMDEPLSNLDAklrVSMRAEIAKIHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQ 231
Cdd:cd03289 155 SKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEE----------NKVRQYDSIQ 221
|
....
gi 501958613 232 ELYN 235
Cdd:cd03289 222 KLLN 225
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-206 |
7.09e-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: 48.52 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 31 KEFIVFVGPSGCGKSTTLRMIAG-LEDISEGELKIDGEvvndkspkdrdiamvfqnyalyphmtvydnmafglklrkykk 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 110 ddidrRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI-----AKIHRR 184
Cdd:smart00382 40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSE 114
|
170 180
....*....|....*....|..
gi 501958613 185 IGSTTIYVTHDQTEAMTLADRI 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-209 |
7.79e-07 |
|
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: 49.56 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 23 DFDLDIKDKEFIVFVGPSGCGKST----------------TLRMIA--GLEDISEGEL-KIDGevvndKSPKdrdIAMVF 83
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveSLSAYArqFLGQMDKPDVdSIEG-----LSPA---IAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 84 QNYALYPHMTV------YDnmafglKLRK-YKKDDIDRRVKEAAEI-LG-LTefLERKPADLSGGQRQRVAMGRAIVR-- 152
Cdd:cd03270 85 KTTSRNPRSTVgtvteiYD------YLRLlFARVGIRERLGFLVDVgLGyLT--LSRSAPTLSGGEAQRIRLATQIGSgl 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501958613 153 DAKVFLMDEPLSNLDAKLRVSMRAEIAKIhRRIGSTTIYVTHDQtEAMTLADRIVIM 209
Cdd:cd03270 157 TGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDI 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-218 |
9.41e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 4 LNLKHIYKKYPNTTHYavEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGledisegELKID-GEVvndKSPKDRDIAMV 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLF--KNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-------ELEPDsGTV---KWSENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 83 FQNYALY--PHMTVYDNMAfglKLRKYKKDDIDRRvkeaaEILGLTEFLE---RKPAD-LSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK15064 388 AQDHAYDfeNDLTLFDWMS---QWRQEGDDEQAVR-----GTLGRLLFSQddiKKSVKvLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501958613 157 FLMDEPLSNLDAKLRVSMRAEIAKIHrrigSTTIYVTHDQTEAMTLADRIVIMSATK--NPQGN 218
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMALEKYE----GTLIFVSHDREFVSSLATRIIEITPDGvvDFSGT 519
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
109-209 |
1.11e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 109 KDDIDRRVKEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGST 188
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100
....*....|....*....|.
gi 501958613 189 TIYVTHDQTEAMTLADRIVIM 209
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVI 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-167 |
7.74e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVED------FDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ISEGELKIDGEVVNDKSPKDR---DIAMVFQny 86
Cdd:PRK09580 8 HVSVEDkailrgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 alYPHMTVYDNMAFGLK-----LRKYkkddidrRVKEAAEILGLTEFLERK------PADL---------SGGQRQRVAM 146
Cdd:PRK09580 86 --YPVEIPGVSNQFFLQtalnaVRSY-------RGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDI 156
|
170 180
....*....|....*....|.
gi 501958613 147 GRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-210 |
9.69e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 20 AVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSP------------KDRDIAMVFQNY- 86
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvtEERRSTGIYAYLd 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 87 ----ALYPHMTVYDNMAFGLKLRKYKKDD---IDR-RVKeaaeilglTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK10982 343 igfnSLISNIRNYKNKVGLLDNSRMKSDTqwvIDSmRVK--------TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501958613 159 MDEPLSNLD--AKLRV-SMRAEIAKIHRRIgsttIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK10982 415 LDEPTRGIDvgAKFEIyQLIAELAKKDKGI----IIISSEMPELLGITDRILVMS 465
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-176 |
1.03e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 37 VGPSGCGKSTTLRMIAGLED--ISEGELKIDGevvndkSPKDRDI-----AMVFQNYALYPHMTVYDNMAFGLKLRKYKK 109
Cdd:PLN03140 912 MGVSGAGKTTLMDVLAGRKTggYIEGDIRISG------FPKKQETfarisGYCEQNDIHSPQVTVRESLIYSAFLRLPKE 985
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501958613 110 DDIDRRVKEAAEILGLTEFLERKPA--------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK-LRVSMRA 176
Cdd:PLN03140 986 VSKEEKMMFVDEVMELVELDNLKDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRT 1061
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
252-300 |
2.49e-05 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 40.89 E-value: 2.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 501958613 252 NFFEVVVKDGQIISeDGLDIAIPEgqakmleAAGYKDKKVIFGIRPEDI 300
Cdd:pfam17850 1 NLFHGRVEDGRVRI-GGLALPLPE-------LAGAEGSEVVAYVRPHDL 41
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-167 |
2.78e-05 |
|
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: 45.28 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 3 ELNLKHIYKKYPNTTHYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNdKSP----KDRd 78
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-KLPlhtlRSR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 IAMVFQNYALYPhmtvyDNMAFGLKLRKYKKDDidrRVKEAAEILGLTEFLERKPADL-----------SGGQRQRVAMG 147
Cdd:cd03288 97 LSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 168
|
170 180
....*....|....*....|
gi 501958613 148 RAIVRDAKVFLMDEPLSNLD 167
Cdd:cd03288 169 RAFVRKSSILIMDEATASID 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-241 |
2.97e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 28 IKDKEFIVFVGPSGCGKSTTL----RMIagleDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHmTVYDNM--- 98
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVdpf 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 99 -------------AFGLKLR-KYKKDDIDRRVKEAAeilglteflerkpADLSGGQRQRVAMGRAIV-RDAKVFLMDEPL 163
Cdd:PTZ00243 1408 leassaevwaaleLVGLRERvASESEGIDSRVLEGG-------------SNYSVGQRQLMCMARALLkKGSGFILMDEAT 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 164 SNLDAKLRVSMRAEIAKIHRriGSTTIYVTHdqtEAMTLA--DRIVIMSAtknpqgngtiGKIEQVGSPQELYNLPANKF 241
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFS--AYTVITIAH---RLHTVAqyDKIIVMDH----------GAVAEMGSPRELVMNRQSIF 1539
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-209 |
4.34e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 38 GPSGCGKSTTLRMIAGLED---ISEGELKIDGEvvndksPKD----RDIAMVFQNYALYPHMTVYDNMAFGLKLR----- 105
Cdd:TIGR00956 796 GASGAGKTTLLNVLAERVTtgvITGGDRLVNGR------PLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpksv 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 106 -KYKKDDIdrrVKEAAEILGLTEFlerkpAD---------LSGGQRQRVAMGRAIVRDAKVFL-MDEPLSNLDAKLRVSm 174
Cdd:TIGR00956 870 sKSEKMEY---VEEVIKLLEMESY-----ADavvgvpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS- 940
|
170 180 190
....*....|....*....|....*....|....*....
gi 501958613 175 raeIAKIHRRIGST--TIYVTHDQTEAMTLA--DRIVIM 209
Cdd:TIGR00956 941 ---ICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLL 976
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-216 |
1.34e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDfDLDIKDKEFIVFVGPSGCGKSTTLRMIAgledisegelkidgevvndkspkdrdiamvfqnYALyphmtvydn 97
Cdd:cd03227 9 SYFVPN-DVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LAL--------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 maFGLKLRKYKKDDIDRRVKEAAEILGLTEFLERkpadLSGGQRQRVA----MGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:cd03227 46 --GGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ----LSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501958613 174 MrAEIAKIHRRIGSTTIYVTHDQtEAMTLADRIVIMSATKNPQ 216
Cdd:cd03227 120 L-AEAILEHLVKGAQVIVITHLP-ELAELADKLIHIKKVITGV 160
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
92-209 |
2.74e-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: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 92 MTVYDNMAF--GLKLRKYKKDDIDRRVKEAAEILG---------LTefLERKPADLSGGQRQRVAM----GRAIVrdAKV 156
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLGflidvgldyLS--LSRAAGTLSGGEAQRIRLatqiGSGLT--GVL 511
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 501958613 157 FLMDEPLSNLDAklRVSMR-AEIAKIHRRIGSTTIYVTHDQtEAMTLADRIVIM 209
Cdd:TIGR00630 512 YVLDEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDI 562
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
129-228 |
5.55e-04 |
|
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: 40.38 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 129 LERKPADLSGGQRQRVAMGRAIVRDAK--VFLMDEPLSNLDAKLRVSMRAEIAKIhRRIGSTTIYVTHDQTeAMTLADRI 206
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLD-VLSSADWI 158
|
90 100
....*....|....*....|..
gi 501958613 207 VIMSatknPQGNGTIGKIEQVG 228
Cdd:cd03238 159 IDFG----PGSGKSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-233 |
7.70e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 27 DIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVVNDKSPKD--RDIAMVFQNYALYPHmTVYDNM-AFGlk 103
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFSG-TVRFNLdPFN-- 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 104 lrkyKKDDIDrrVKEAAEILGLTEFLERKPADL-----------SGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrV 172
Cdd:PLN03130 1338 ----EHNDAD--LWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD----V 1407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501958613 173 SMRAEIAK-IHRRIGSTTIYVTHDQTEAMTLADRIVIMSAtknpqgngtiGKIEQVGSPQEL 233
Cdd:PLN03130 1408 RTDALIQKtIREEFKSCTMLIIAHRLNTIIDCDRILVLDA----------GRVVEFDTPENL 1459
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-167 |
1.56e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 21 VEDFDLDIKDKEFIV-------------FVGPSGCGKSTTLRMIA--GLEDISEG--ELKIDGEVVNDKSPK-----DRD 78
Cdd:PLN03073 180 MENFSISVGGRDLIVdasvtlafgrhygLVGRNGTGKTTFLRYMAmhAIDGIPKNcqILHVEQEVVGDDTTAlqcvlNTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 79 I---------AMVFQNYALYPHMTVYDNMAFGLKlRKYKKDDIDRRVKE----------------AAEIL-GLT---EFL 129
Cdd:PLN03073 260 IertqlleeeAQLVAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEiykrlelidaytaearAASILaGLSftpEMQ 338
|
170 180 190
....*....|....*....|....*....|....*...
gi 501958613 130 ERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
113-167 |
2.41e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 2.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 501958613 113 DRRVKEAAE---ILGLTEFLERKP-ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK10938 375 DRQQKLAQQwldILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-164 |
5.06e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 18 HYAVEDFDLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDISEGELKIDGEVvndkspkdrdiAMVFQNYALYPHMTVYDN 97
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 98 MAF-GLK--LRKYKKDDIDRRVKEAAEIlglTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK13545 106 IELkGLMmgLTKEKIKEIIPEIIEFADI---GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
33-99 |
8.63e-03 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 37.25 E-value: 8.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501958613 33 FIVFVGPSGCGKSTTLRMIAglediseGELKIDG-EVVNDKSPKDRDIAMVFQNYALYPHMTVYDNMA 99
Cdd:cd01672 2 FIVFEGIDGAGKTTLIELLA-------ERLEARGyEVVLTREPGGTPIGEAIRELLLDPEDEKMDPRA 62
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
13-119 |
8.66e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501958613 13 YPNTTH-YAVEDFDLDIKDKE-FIVFVGPSGCGKSTTLRMIagLEDIsegelkidgevvndksPKDRDIAMVFqnyalYP 90
Cdd:COG3267 23 FLSPSHrEALARLEYALAQGGgFVVLTGEVGTGKTTLLRRL--LERL----------------PDDVKVAYIP-----NP 79
|
90 100 110
....*....|....*....|....*....|....
gi 501958613 91 HMTVYD-----NMAFGLKLRKYKKDDIDRRVKEA 119
Cdd:COG3267 80 QLSPAEllraiADELGLEPKGASKADLLRQLQEF 113
|
|
| |
