|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-375 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 614.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIA 80
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND----------GRIQQVGTPEELYDRPANL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 241 FVAGFIGSPAMNFINVKLEGGYIVTNGLNLKVPEGAlkvlkeKGYDGKELIFGIRPEDVNteaafLETFPESVVKATISV 320
Cdd:COG3839 229 FVAGFIGSPPMNLLPGTVEGGGVRLGGVRLPLPAAL------AAAAGGEVTLGIRPEHLR-----LADEGDGGLEATVEV 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 321 SELLGSESHLYCQVGDNEFIAKVDARDYLGTGETIELGFDLNKAHFFDKETEKTV 375
Cdd:COG3839 298 VEPLGSETLVHVRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-373 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 524.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIA 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG----------GVAEQIGTPVEVYEKPAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 241 FVAGFIGSPAMNFINVKL-EGGYIVTNGLNLKVPEGALKVLkekgYDGKELIFGIRPEDvnteaaFLETFPESVVKATIS 319
Cdd:PRK11650 230 FVASFIGSPAMNLLDGRVsADGAAFELAGGIALPLGGGYRQ----YAGRKLTLGIRPEH------IALSSAEGGVPLTVD 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 320 VSELLGSESHLYCQVGDNEFIAKVDARDYLGTGETIELGFDLNKAHFFDKETEK 373
Cdd:PRK11650 300 TVELLGADNLAHGRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGR 353
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-369 |
1.28e-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: 1.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIA 80
Cdd:COG3842 3 MPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND----------GRIEQVGTPEEIYERPATR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 241 FVAGFIGSpaMNFINVKL---EGGYIVTNGLNLKVPEGAlkvlkeKGYDGKELIFGIRPEDVnteaAFLETFPESVVKAT 317
Cdd:COG3842 231 FVADFIGE--ANLLPGTVlgdEGGGVRTGGRTLEVPADA------GLAAGGPVTVAIRPEDI----RLSPEGPENGLPGT 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 318 ISVSELLGSESHLYCQVGDN-EFIAKVDARDYLG--TGETIELGFDLNKAHFFDK 369
Cdd:COG3842 299 VEDVVFLGSHVRYRVRLGDGqELVVRVPNRAALPlePGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-367 |
3.22e-152 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 433.69 E-value: 3.22e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNSeHYSvEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIA 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDV-VIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA----------GRVAQVGKPLELYHYPANR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 241 FVAGFIGSPAMNFINVKLEGGYI------VTNGLNLKVP-EGA-LKVlkekgydGKELIFGIRPED-VNTEAAfletfpE 311
Cdd:PRK11000 229 FVAGFIGSPKMNFLPVKVTATAIeqvqveLPNRQQVWLPvEGRgVQV-------GANMSLGIRPEHlLPSDIA------D 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 312 SVVKATISVSELLGSESHLYCQV--GDNEFIAKVDARDYLGTGETIELGFDLNKAHFF 367
Cdd:PRK11000 296 VTLEGEVQVVEQLGNETQIHIQIpaIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLF 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-228 |
3.41e-139 |
|
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: 394.70 E-value: 3.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND----------GQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-338 |
2.08e-117 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 344.44 E-value: 2.08e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNsehYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN-NVAPKDRDIA 80
Cdd:COG1118 2 SIEVRNISKRFGS---FTLlDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ----------GRIEQVGTPDEVYDRPATP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 241 FVAGFIGspAMNFINVKLEGGYIVTNGLNLKVPEGAlkvlkekgYDGKELIFgIRPEDVnteAAFLETFPESVVKATISV 320
Cdd:COG1118 229 FVARFLG--CVNVLRGRVIGGQLEADGLTLPVAEPL--------PDGPAVAG-VRPHDI---EVSREPEGENTFPATVAR 294
|
330
....*....|....*...
gi 881073645 321 SELLGSESHLYCQVGDNE 338
Cdd:COG1118 295 VSELGPEVRVELKLEDGE 312
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-228 |
4.20e-115 |
|
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: 333.33 E-value: 4.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPnsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE----------GRIVQVG 213
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-367 |
2.06e-111 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 329.65 E-value: 2.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 2 VELNLKNIYKKYP--NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV-----NNVAP 74
Cdd:NF040933 1 VTVRVENVTKIFKkgKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVaspgkIIVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 75 KDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 155 KVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRI-VIMSatknpagtgtiGRVEQIGSPQEV 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAgVINN-----------GKFQQVGKPEEI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 234 YKNPVNKFVAGFIGSpaMNFINVKLEGGYIVTNGlNLKVPegalkvLKEKGYDGKELIFGIRPEDVNTEAAFLETFPE-- 311
Cdd:NF040933 230 YDNPANIFVARLIGD--INLLEGKVEEEGLVDGN-DLKIP------LPNPKLEAGEVIIGIRPEDIDISESDMRLPPGfv 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 312 SVVKATISVSELLGSESHLYCQ-VGDNEFIAKVDARDYLGTGETIELGFDLNKAHFF 367
Cdd:NF040933 301 EVGKGRVKVSSYAGGVFRVVVSpIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-247 |
1.24e-109 |
|
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: 320.34 E-value: 1.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSehYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK----------GKIQQIGTPEEIYEEPANRFVA 228
|
....
gi 881073645 244 GFIG 247
Cdd:cd03300 229 DFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-256 |
1.65e-104 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 312.65 E-value: 1.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRD----------GRIEQDGTPREIYEEPKNLFVA 242
|
250
....*....|...
gi 881073645 244 GFIGSpamnfINV 256
Cdd:PRK09452 243 RFIGE-----INI 250
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-326 |
6.65e-102 |
|
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: 305.04 E-value: 6.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIA 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA--FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:TIGR03265 160 EPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH----------GVIEQVGTPQEIYRHPATP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 241 FVAGFIGSpaMNFINVKLEGGYivtnglNLKVPEGALKVLKEKGYDGKELIFGIRPEDVNTEAAFLEtfpESVVKATISV 320
Cdd:TIGR03265 230 FVADFVGE--VNWLPGTRGGGS------RARVGGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNA---ANLLLARVED 298
|
....*.
gi 881073645 321 SELLGS 326
Cdd:TIGR03265 299 MEFLGA 304
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-343 |
3.46e-94 |
|
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: 284.39 E-value: 3.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRV 116
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 117 QEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQ 196
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 197 TEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFIGSPAM-NFINVKLEGGYIVTNGLNLKVPEG 275
Cdd:TIGR01187 162 EEAMTMSDRIAIMRK----------GKIAQIGTPEEIYEEPANLFVARFIGEINVfEATVIERKSEQVVLAGVEGRRCDI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 276 ALKVLKEkgyDGKELIFGIRPEDVN----TEAAFLETFPESVVKATISVSellGSESHLYCQVGDNEFIAKV 343
Cdd:TIGR01187 232 YTDVPVE---KDQPLHVVLRPEKIVieeeDEANSSNAIIGHVIDITYLGM---TLEVHVRLETGQKVLVSEF 297
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-230 |
4.66e-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: 281.59 E-value: 4.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYP--NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVnnvAPKDRDIAM 81
Cdd:COG1116 8 LELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV---TGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 162 PLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtkNPagtGTIGRVEQIGSP 230
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA--RP---GRIVEEIDVDLP 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-248 |
4.78e-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: 280.76 E-value: 4.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMV 82
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFGLKLRK----YSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 159 MDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK----------GRIEQVGTPDEVYDHPA 229
|
250
....*....|
gi 881073645 239 NKFVAGFIGS 248
Cdd:cd03296 230 SPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-299 |
5.03e-94 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 285.07 E-value: 5.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK----------GKIMQIGSPQELYRQPASRFMA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 244 GFIGSPamNFINVKLEGGYIVTNGLNLKVPEGALKVLKekgyDGKELIfGIRPEDV 299
Cdd:PRK11432 235 SFMGDA--NIFPATLSGDYVDIYGYRLPRPAAFAFNLP----DGECTV-GVRPEAI 283
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-336 |
1.53e-90 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 275.80 E-value: 1.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:NF040840 2 IRIENLSKDW---KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:NF040840 79 QNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMsatKNpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:NF040840 159 SALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIM---LN-------GRLSQVGDVREVFRRPKNEFVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 244 GFIGspAMNFI----NVKLEGGYIVTNGLNLKVPEgalkvlKEKGydgkELIFGIRPEDVNTEAAFLETFPESVVKATIS 319
Cdd:NF040840 229 RFVG--FENIIegvaEKGGEGTILDTGNIKIELPE------EKKG----KVRIGIRPEDITISTEKVKTSARNEFKGKVE 296
|
330
....*....|....*..
gi 881073645 320 VSELLGSESHLYCQVGD 336
Cdd:NF040840 297 EIEDLGPLVKLTLDVGI 313
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-228 |
3.28e-90 |
|
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: 270.50 E-value: 3.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNS--EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPkdrDIAM 81
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 162 PLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtkNPagtGTIGRVEQIG 228
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA--RP---GRIVAEVEVD 219
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
8-247 |
4.25e-89 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 268.21 E-value: 4.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 8 NIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVFQNYA 87
Cdd:TIGR00968 5 NISKRFGSFQ--ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 88 LYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 168 AKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFIG 247
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN----------GKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-248 |
2.47e-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: 2.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNSeHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RD 78
Cdd:COG1125 1 MIEF--ENVTKRYPDG-TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGL--KEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMRE----------GRIVQYDTPEEILAN 227
|
250
....*....|..
gi 881073645 237 PVNKFVAGFIGS 248
Cdd:COG1125 228 PANDFVADFVGA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-247 |
2.70e-85 |
|
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: 258.42 E-value: 2.70e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNsehYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMsatKNpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM---LN-------GKLIQVGKPEEVFKKPKNEFVA 227
|
....
gi 881073645 244 GFIG 247
Cdd:cd03299 228 EFLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-299 |
4.92e-83 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 257.84 E-value: 4.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:PRK11607 20 LEIRNLTKSF-DGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR----------GKFVQIGEPEEIYEHPTTRYSA 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881073645 244 GFIGSPAM--NFINVKLEGGYIV-TNGLN--LKVPEGALKVlkekgyDGKELIFGIRPEDV 299
Cdd:PRK11607 248 EFIGSVNVfeGVLKERQEDGLVIdSPGLVhpLKVDADASVV------DNVPVHVALRPEKI 302
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-249 |
7.57e-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: 249.91 E-value: 7.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSeHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGL--KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVN 239
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN----------GEIVQVGTPDEILRSPAN 229
|
250
....*....|
gi 881073645 240 KFVAGFIGSP 249
Cdd:cd03295 230 DFVAEFVGAD 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-247 |
1.26e-74 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 235.36 E-value: 1.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVFQNYALYPHMTVYDNMAFGL 102
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 103 KL----RKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:PRK10851 100 TVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 179 AKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFIG 247
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ----------GNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
6.63e-72 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 222.06 E-value: 6.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPnsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN----NVAPKDRDI 79
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYPHMTVYDNMAFGlklrkyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-246 |
8.05e-72 |
|
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: 225.22 E-value: 8.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD------RDIAMVFQNYALYPHMTV 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 175 RAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFI 246
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD----------GRLVQVGTPEEILTNPANDYVREFF 261
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
21-286 |
2.60e-69 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 222.03 E-value: 2.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAP------KDRDIAMVFQNYALYPHMTV 94
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:TIGR01186 89 LQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 175 RAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFIG------S 248
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKA----------GEIVQVGTPDEILRNPANEYVEEFIGkvdlsqV 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 881073645 249 PAMNFINVKLEGGYI-VTNGlnlKVPEGALKVLKEKGYD 286
Cdd:TIGR01186 239 FDAERIAQRMNTGPItKTAD---KGPRSALQLMRDERVD 274
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-246 |
6.66e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 221.52 E-value: 6.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD------RDIAMVFQNYALYPHMTV 94
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:COG4175 123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 175 RAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMsatKNpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFI 246
Cdd:COG4175 203 QDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM---KD-------GRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-228 |
1.71e-68 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 214.85 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 18 HYSVEDFNLDIK---DKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN------NVAPKDRDIAMVFQNYAL 88
Cdd:cd03297 7 EKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkkiNLPPQQRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 YPHMTVYDNMAFGLKlRKYSKEDIDkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:cd03297 87 FPHLNVRENLAFGLK-RKRNREDRI-SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 169 KLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED----------GRLQYIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-237 |
4.69e-67 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 211.42 E-value: 4.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNyalyP-----HMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1122 80 VFQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD----------GRIVADGTPREVFSD 224
|
.
gi 881073645 237 P 237
Cdd:COG1122 225 Y 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
1.50e-66 |
|
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: 209.65 E-value: 1.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNS--EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD--- 78
Cdd:cd03255 1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 ---IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMtLADRIVIMS 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELR 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-247 |
1.39e-64 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 205.37 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnsEHYSVEdFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:COG3840 2 LRLDDLTYRY---GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLR-KYSKEDIdKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGlKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 163 LSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFV 242
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVAD----------GRIAADGPTAALLDGEPPPAL 226
|
....*
gi 881073645 243 AGFIG 247
Cdd:COG3840 227 AAYLG 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-210 |
3.16e-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: 3.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVF 83
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNyalyP-HM----TVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03225 82 QN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 881073645 159 MDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-210 |
4.11e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 203.74 E-value: 4.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVE---DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD-- 78
Cdd:COG1136 5 LELRNLTKSYGTGEG-EVTalrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 ----IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG1136 84 rrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 155 KVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQtEAMTLADRIVIMS 210
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLR 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-299 |
8.30e-63 |
|
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: 204.95 E-value: 8.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN------NVAPKDRDIAMVFQNYALYPHMTVYD 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 97 NMAFGLKLRKYSKEDIDkrVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLrvsmRA 176
Cdd:COG4148 97 NLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR----KA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 177 EI----AKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGfiGSPAMN 252
Cdd:COG4148 171 EIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQ----------GRVVASGPLAEVLSRPDLLPLAG--GEEAGS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 881073645 253 FINVKLEgGYIVTNGL-NLKVPEGALKVLKEKGYDGKELIFGIRPEDV 299
Cdd:COG4148 239 VLEATVA-AHDPDYGLtRLALGGGRLWVPRLDLPPGTRVRVRIRARDV 285
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-237 |
6.92e-61 |
|
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: 203.98 E-value: 6.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYP---NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---- 76
Cdd:COG1123 261 LEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 -RDIAMVFQN--YALYPHMTVYDNMAFGLKLRK-YSKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDaklrVSMRAEI----AKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQI 227
Cdd:COG1123 421 LEPKLLILDEPTSALD----VSVQAQIlnllRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD----------GRIVED 486
|
250
....*....|
gi 881073645 228 GSPQEVYKNP 237
Cdd:COG1123 487 GPTEEVFANP 496
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
8.59e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 195.67 E-value: 8.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGT--VVNNVAPKDRdIAM 81
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvARDPAEVRRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 162 PLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDK----------GRIVADGTPDEL 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-246 |
5.50e-60 |
|
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: 193.66 E-value: 5.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNSEHYsvEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD-- 78
Cdd:COG1127 5 MIEV--RNLTKSFGDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 ---IAMVFQNYALYPHMTVYDNMAFGLK-LRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG1127 81 rrrIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 155 KVFLMDEPLSNLDAklrVSMRA---EIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQ 231
Cdd:COG1127 161 EILLYDEPTAGLDP---ITSAVideLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD----------GKIIAEGTPE 227
|
250
....*....|....*
gi 881073645 232 EVYKNPvNKFVAGFI 246
Cdd:COG1127 228 ELLASD-DPWVRQFL 241
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
4.62e-58 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 189.69 E-value: 4.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYP--NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvAP-KDR 77
Cdd:COG4525 1 MSMLTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPgADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 diAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-209 |
8.54e-57 |
|
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: 185.78 E-value: 8.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEH--YSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDI 79
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNY--ALYPHMTVYDNMAFGLKLRKysKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 157 FLMDEPLSNLDaklrVSMRAEI----AKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1124 160 LLLDEPTSALD----VSVQAEIlnllKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-211 |
2.59e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.49 E-value: 2.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RD 78
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFG-------LK--LRKYSKEDIDkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRA 149
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKL-RVSMRAeIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSA 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 |
9.48e-56 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 182.40 E-value: 9.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNS--EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-- 76
Cdd:cd03258 1 MIEL--KNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 ---RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:cd03258 79 karRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK----------GEVVEEGTVEEV 228
|
....
gi 881073645 234 YKNP 237
Cdd:cd03258 229 FANP 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-196 |
3.29e-55 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 180.63 E-value: 3.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNSeHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---- 76
Cdd:COG2884 1 MIRF--ENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 -RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:COG2884 78 rRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 881073645 156 VFLMDEPLSNLDAKLRVS-MRAeIAKIHRRiGATTIYVTHDQ 196
Cdd:COG2884 158 LLLADEPTGNLDPETSWEiMEL-LEEINRR-GTTVLIATHDL 197
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-237 |
5.56e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 180.58 E-value: 5.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNSEhysV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvAPKD--- 76
Cdd:COG1126 1 MIEI--ENLHKSFGDLE---VlKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKdin 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 ---RDIAMVFQNYALYPHMTVYDNMAFGL-KLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVR 152
Cdd:COG1126 74 klrRKVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 153 DAKVFLMDEPLSNLDAKlrvsMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGS 229
Cdd:COG1126 154 EPKVMLFDEPTSALDPE----LVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDG----------GRIVEEGP 219
|
....*...
gi 881073645 230 PQEVYKNP 237
Cdd:COG1126 220 PEEFFENP 227
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-213 |
1.55e-54 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 179.94 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNS--EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPkdrDIAM 81
Cdd:NF040729 2 LKIQNISKTFINNkkENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP---DRGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 881073645 162 PLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDK 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-209 |
7.75e-54 |
|
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: 176.95 E-value: 7.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN----NVAPKDRDI 79
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYPHMTVYDNMAFGL-KLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 159 MDEPLSNLDAKlrvsMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03262 159 FDEPTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-246 |
1.21e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 177.59 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDI- 79
Cdd:PRK09493 1 MIEF--KNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 ---AMVFQNYALYPHMTVYDNMAFG-LKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK09493 77 qeaGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 156 VFLMDEPLSNLDAKLrvsmRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:PRK09493 157 LMLFDEPTSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDK----------GRIAEDGDPQV 222
|
250
....*....|....
gi 881073645 233 VYKNPVNKFVAGFI 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 |
3.58e-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: 175.77 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYP--NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---- 77
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 -DIAMVFQNY--ALYPHMTVYDNMAFGLKLRK--YSKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-240 |
1.20e-52 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 175.05 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR-DIAMV 82
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 163 LSNLDAKLRVSMRAEIAKiHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:COG4555 160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK----------GKVVAQGSLDELREEIGEE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-237 |
1.46e-52 |
|
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: 182.03 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIT---EGECSIDGTVVNNVAPKDR--D 78
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQN--YALYPhMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD----------GRIVEDGPPEEILAA 233
|
.
gi 881073645 237 P 237
Cdd:COG1123 234 P 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
1.78e-52 |
|
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: 174.23 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RDIA 80
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLK-LRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYD----------GKIVAEGTPEEL 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
2.10e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.08 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIykKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:COG4619 1 LELEGL--SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPhMTVYDNMAFGLKLRKysKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-292 |
2.13e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 177.19 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYP--NSEHYSVEDFNLDIKDKEfiVF--VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD 76
Cdd:COG1135 1 MIEL--ENLSKTFPtkGGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 -----RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:COG1135 77 lraarRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDAK-----LRVsmraeIAKIHRRIGATTIYVTHDqteaM----TLADRIVIMSAtknpagtgtiG 222
Cdd:COG1135 157 NNPKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLEN----------G 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 223 RVEQIGSPQEVYKNPVNKFVAGFIGSPamnfinvkleggyivtngLNLKVPEGALKVLKEKGYDGK--ELIF 292
Cdd:COG1135 218 RIVEQGPVLDVFANPQSELTRRFLPTV------------------LNDELPEELLARLREAAGGGRlvRLTF 271
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-233 |
6.69e-52 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 173.31 E-value: 6.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHMTVYDNMAFGLK-----LRKYSKEDIDKrVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYphlglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD----------GRIVAQGPPEEV 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-233 |
1.01e-51 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 172.37 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RD 78
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFGL---------KLRKYSKEDIdkrvQEAAEIL---GLKEFLDRKPADLSGGQRQRVAM 146
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEK----QRALAALervGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 147 GRAIVRDAKVFLMDEPLSNLDAKL-RVSMRAeIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVE 225
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKD----------GRIV 224
|
....*...
gi 881073645 226 QIGSPQEV 233
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-231 |
3.14e-51 |
|
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: 170.72 E-value: 3.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPkdrDIAMVFQNYALYPHMTVYDNMAF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 GLK--LRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI 178
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 179 AKIHRRIGATTIYVTHDQTEAMTLADRIVIMsaTKNPAgtGTIGRVEQIGSPQ 231
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVML--TNGPA--ANIGQILEVPFPR 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-237 |
3.88e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 171.87 E-value: 3.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 5 NLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RDI 79
Cdd:TIGR04521 5 NVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQnyalYPHM-----TVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKE-FLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:TIGR04521 85 GLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK----------GKIVLDGTPREV 230
|
....
gi 881073645 234 YKNP 237
Cdd:TIGR04521 231 FSDV 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-233 |
6.68e-51 |
|
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: 180.80 E-value: 6.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYpHMTVYDNMAFGlklrkysKEDI-DKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGR 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG-------DPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 149 AIVRDAKVFLMDEPLSNLDAKLRvsmraeiAKIHRRI-----GATTIYVTHDqTEAMTLADRIVIMSAtknpagtgtiGR 223
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETE-------AIILENLrrllkGRTVIIIAHR-LSTIRLADRIIVLDK----------GR 686
|
250
....*....|
gi 881073645 224 VEQIGSPQEV 233
Cdd:COG2274 687 IVEDGTHEEL 696
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-233 |
6.80e-51 |
|
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: 169.67 E-value: 6.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDI-----TEGECSIDGTVVNNVAPKD-- 76
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 --RDIAMVFQNYALYPhMTVYDNMAFGLKLRKY-SKEDIDKRVQEAAEILGL-KEFLDR-KPADLSGGQRQRVAMGRAIV 151
Cdd:cd03260 79 lrRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIgaTTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQ 231
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLN----------GRLVEFGPTE 225
|
..
gi 881073645 232 EV 233
Cdd:cd03260 226 QI 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-236 |
8.24e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 171.07 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV---NNVAPKDRDIAMV 82
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:TIGR04520 83 FQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAmTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNK----------GKIVAEGTPREIFSQ 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-299 |
2.73e-50 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 172.22 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVA------PKDRDIAMVFQNYALYPHMTVYD 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 97 NMAFGLKlrKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRA 176
Cdd:TIGR02142 95 NLRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 177 EIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYknpvnkfvagfiGSPAMNFINv 256
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED----------GRVAAAGPIAEVW------------ASPDLPWLA- 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 257 KLEGGYIV---------TNGL-NLKVPEGALKVLKEKGYDGKELIFGIRPEDV 299
Cdd:TIGR02142 230 REDQGSLIegvvaehdqHYGLtALRLGGGHLWVPENLGPTGARLRLRVPARDV 282
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
16-209 |
3.07e-50 |
|
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: 167.67 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 16 SEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVFQNYALYPHMTVY 95
Cdd:cd03298 9 SYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 96 DNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 175
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....
gi 881073645 176 AEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-232 |
3.30e-49 |
|
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: 164.99 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGT-VVNNVAPKDRDIAMV 82
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 163 LSNLDAKLRVSMRAEIAKIhrRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSD----------GKLRCIGSPQE 218
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-211 |
4.18e-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: 164.73 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNSeHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---- 76
Cdd:TIGR02673 1 MIEF--HNVSKAYPGG-VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 -RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:TIGR02673 78 rRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
15-210 |
1.40e-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: 163.49 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 15 NSEHYSVEdFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVFQNYALYPHMTV 94
Cdd:TIGR01277 9 EYEHLPME-FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFG----LKLRKYSKEdidkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL 170
Cdd:TIGR01277 88 RQNIGLGlhpgLKLNAEQQE----KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 881073645 171 RVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-237 |
5.05e-48 |
|
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: 165.23 E-value: 5.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHY--SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED---ITEGECSIDGTVVNNVAPKD-- 76
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 ----RDIAMVFQN-Y-ALYPHMTVYDNMAFGLKL-RKYSKEDIDKRVQEAAEILGL---KEFLDRKPADLSGGQRQRVAM 146
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 147 GRAIVRDAKVFLMDEPLSNLDaklrVSMRAEI----AKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtGTIg 222
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVAVMYA-------GRI- 229
|
250
....*....|....*
gi 881073645 223 rVEqIGSPQEVYKNP 237
Cdd:COG0444 230 -VE-EGPVEELFENP 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-232 |
7.01e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 165.34 E-value: 7.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 13 YPNsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYp 90
Cdd:COG1132 349 YPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 HMTVYDNMAFGlklrkysKEDI-DKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:COG1132 427 SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 159 MDEPLSNLDAklrvsmRAEiAKIHRRI-----GATTIYVTH------DqteamtlADRIVIMSAtknpagtgtiGRVEQI 227
Cdd:COG1132 500 LDEATSALDT------ETE-ALIQEALerlmkGRTTIVIAHrlstirN-------ADRILVLDD----------GRIVEQ 555
|
....*
gi 881073645 228 GSPQE 232
Cdd:COG1132 556 GTHEE 560
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-234 |
2.10e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 157.20 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKY-PNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV--NNVAPKDRDIA 80
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK13650 85 MVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEaMTLADRIVIMsatKNpagtgtiGRVEQIGSPQEVY 234
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM---KN-------GQVESTSTPRELF 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-209 |
3.95e-45 |
|
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: 152.92 E-value: 3.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYpHMTVYDNMafglklrkyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 881073645 162 PLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDqTEAMTLADRIVIM 209
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVL 167
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-212 |
6.22e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 153.79 E-value: 6.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAG-LEDI--TEGECSIDGTVVNNVAPKDRDIAMVFQNYALYPHMTVYDN 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGLKlRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAE 177
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 881073645 178 I-AKIHRRiGATTIYVTHDQTEAMtLADRIVIMSAT 212
Cdd:COG4136 176 VfEQIRQR-GIPALLVTHDEEDAP-AAGRVLDLGNW 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-195 |
9.41e-45 |
|
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: 153.33 E-value: 9.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSeHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNN-----VAPKDRDIA 80
Cdd:cd03292 3 FINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHD 195
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-209 |
9.74e-45 |
|
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: 151.78 E-value: 9.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR-DIAMV 82
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMafglklrkyskedidkrvqeaaeilglkefldrkpaDLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 163 LSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAIL 168
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-283 |
2.72e-44 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 157.50 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD------RDIAMVFQNYALYPHMTV 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 175 RAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFIGSPAMNFI 254
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN----------GEVVQVGTPDEILNNPANDYVRTFFRGVDISQV 273
|
250 260 270
....*....|....*....|....*....|...
gi 881073645 255 NVKLEGGYIVTNGLNLKV----PEGALKVLKEK 283
Cdd:PRK10070 274 FSAKDIARRTPNGLIRKTpgfgPRSALKLLQDE 306
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-236 |
4.37e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 154.05 E-value: 4.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 5 NLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDI----A 80
Cdd:PRK13637 7 NLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQ--NYALYPHmTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLK--EFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK13637 87 LVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNK----------GKCELQGTPREVFKE 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
4.56e-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: 149.34 E-value: 4.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNM 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRK----PADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-235 |
1.01e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.86 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN--NVAPKDRDIAM 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeeTVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNK----------GEILEEGTPEEIFK 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
1.14e-43 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 151.78 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVApKDRdiAMVF 83
Cdd:PRK11248 2 LQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER--GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLS 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-208 |
3.06e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 150.12 E-value: 3.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 24 FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVFQNYALYPHMTVYDNMAFG-- 101
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 102 --LKLRKYSKEdidkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIA 179
Cdd:PRK10771 98 pgLKLNAAQRE----KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|
gi 881073645 180 KIHRRIGATTIYVTHDQTEAMTLADR-IVI 208
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRsLVV 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-233 |
4.00e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 4.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnNVAPKDRDIAMVFQNYALYPH--MTVYDNM 98
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYVPQRAEVDWDfpITVRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFGLK-----LRKYSKEDIDkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVS 173
Cdd:COG1121 99 LMGRYgrrglFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 174 MRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSatknpagtgtiGRVEQIGSPQEV 233
Cdd:COG1121 178 LYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN-----------RGLVAHGPPEEV 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-236 |
5.07e-43 |
|
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: 157.23 E-value: 5.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 2 VELNLKNIYKKYPNsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDI 79
Cdd:COG4988 335 PSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALyPHMTVYDNMAFGlklrkysKEDI-DKRVQEAAEILGLKEFLDRKPAD-----------LSGGQRQRVAMG 147
Cdd:COG4988 414 AWVPQNPYL-FAGTIRENLRLG-------RPDAsDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 148 RAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDqTEAMTLADRIVIMSAtknpagtgtiGRVEQI 227
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDD----------GRIVEQ 552
|
....*....
gi 881073645 228 GSPQEVYKN 236
Cdd:COG4988 553 GTHEELLAK 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-236 |
7.34e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.14 E-value: 7.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNlkNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN--NVAPKDRD 78
Cdd:PRK13632 7 MIKVE--NVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK13632 85 IGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAmTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSE----------GKLIAQGKPKEI 229
|
...
gi 881073645 234 YKN 236
Cdd:PRK13632 230 LNN 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-237 |
9.61e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.42 E-value: 9.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RDIAMVFQN-YA-LYPHMT 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAFGLKL-RKYSKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklr 171
Cdd:COG4608 114 VGDIIAEPLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD---- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 172 VSMRAEI----AKIHRRIGATTIYVTHDqteamtL------ADRIVIMsatknpagtgTIGRVEQIGSPQEVYKNP 237
Cdd:COG4608 190 VSIQAQVlnllEDLQDELGLTYLFISHD------LsvvrhiSDRVAVM----------YLGKIVEIAPRDELYARP 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-248 |
1.12e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.88 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYPNS--EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-- 76
Cdd:PRK11153 1 MIEL--KNISKVFPQGgrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 ---RDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK11153 79 karRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA----------GRLVEQGTVSEV 228
|
250
....*....|....*
gi 881073645 234 YKNPVNKFVAGFIGS 248
Cdd:PRK11153 229 FSHPKHPLTREFIQS 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-234 |
1.04e-41 |
|
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: 146.29 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSeHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RD 78
Cdd:TIGR02315 2 LEVENLSKVYPNG-KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNM---AFGLK------LRKYSKEDIdKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRA 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKL-RVSMRAeIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTsKQVMDY-LKRINKEDGITVIINLHQVDLAKKYADRIVGLKA----------GEIVFDG 228
|
....*.
gi 881073645 229 SPQEVY 234
Cdd:TIGR02315 229 APSELD 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-209 |
1.07e-41 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 146.75 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVapKDrDIAMVF 83
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA--RE-DTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKlrkyskEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
2.72e-41 |
|
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: 144.30 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvNNVAPKDR-------- 77
Cdd:TIGR03608 1 LKNISKKFGD--KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKkaskfrre 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 DIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 158 LMDEPLSNLDAKlrvsMRAEIAKIHRRI---GATTIYVTHDqTEAMTLADRIV 207
Cdd:TIGR03608 157 LADEPTGSLDPK----NRDEVLDLLLELndeGKTIIIVTHD-PEVAKQADRVI 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-213 |
3.80e-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: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPnsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVF 83
Cdd:cd00267 2 IENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QnyalyphmtvydnmafglklrkyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-213 |
4.06e-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: 143.77 E-value: 4.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK-DRDIAMVFQNYALYPHMTVYDNMAF 100
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 GLKLRKYSKEDIDkrVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlrvsMRAEIAK 180
Cdd:COG4133 99 WAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA----GVALLAE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 881073645 181 I---HRRIGATTIYVTHDQTEAmtLADRIVIMSATK 213
Cdd:COG4133 173 LiaaHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-209 |
4.97e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.77 E-value: 4.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN---NVAPKD--- 76
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 --RDIAMVFQNYALYPHMTVYDNM-AFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:COG4161 80 lrQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 154 AKVFLMDEPLSNLDAKLrvsmRAEIAKIHRRIGATTI---YVTHDQTEAMTLADRIVIM 209
Cdd:COG4161 160 PQVLLFDEPTAALDPEI----TAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYM 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-237 |
1.40e-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: 143.35 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIAMVFQNYALYPHMTVYDN 97
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGLKLRK----------YSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:cd03219 96 VMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 168 AKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP 237
Cdd:cd03219 176 PEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQ----------GRVIAEGTPDEVRNNP 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-209 |
1.63e-40 |
|
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: 142.34 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYpHMTVYDNMAFGLKLRKyskediDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRA 149
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 150 IVRDAKVFLMDEPLSNLDaklrvsMRAEIAKIHR----RIGATTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD------MNSEERLKERlrqlLGDKTLIIITH-RPSLLDLVDRIIVM 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-237 |
2.88e-40 |
|
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: 142.87 E-value: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIAMVFQNYALYPHMTVYDN 97
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFG-------------LKLRKYSKED--IDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:COG0411 100 VLVAaharlgrgllaalLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 163 LSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVeqI--GSPQEVYKNP 237
Cdd:COG0411 180 AAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF----------GRV--IaeGTPAEVRADP 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-212 |
1.02e-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: 140.36 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvNNVAPKDRDIAMVFQNYAL---YPhMTVYDN 97
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---KPLEKERKRIGYVPQRRSIdrdFP-ISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGL-----KLRKYSKEDIDKrVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRV 172
Cdd:cd03235 91 VLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 881073645 173 SMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAT 212
Cdd:cd03235 170 DIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-237 |
3.52e-39 |
|
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: 146.83 E-value: 3.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 2 VELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDI 79
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYpHMTVYDNMAFGlklrkysKEDI-DKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMG 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 148 RAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDQTeAMTLADRIVIMSAtknpagtgtiGRVEQI 227
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLED----------GRIVEQ 550
|
250
....*....|
gi 881073645 228 GSPQEVYKNP 237
Cdd:COG4987 551 GTHEELLAQN 560
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-209 |
3.98e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN---NVAPKD-----R 77
Cdd:PRK11124 5 LNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 DIAMVFQNYALYPHMTVYDNMAFG-LKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 157 FLMDEPLSNLDAKLrvsmRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK11124 163 LLFDEPTAALDPEI----TAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYM 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-209 |
7.12e-39 |
|
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: 138.27 E-value: 7.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKY--PNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDG-TVVNNVAPKDRDIA 80
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 161 EPLSNLDAKLRVSMRaEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03266 162 EPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-209 |
1.81e-38 |
|
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: 145.78 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYpHMTVYDNMAFGlklRKYSKediDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRA 149
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG---APYAD---DEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 150 IVRDAKVFLMDEPLSNLDaklrvsMRAEIAKIHR----RIGATTIYVTHdQTEAMTLADRIVIM 209
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMD------NRSEERFKDRlkrwLAGKTLVLVTH-RTSLLDLVDRIIVM 672
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-209 |
2.06e-38 |
|
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: 135.64 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVF 83
Cdd:cd03214 2 VENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QnyalyphmtvydnmafglklrkyskedidkrvqeAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILL 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-211 |
2.01e-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: 132.17 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVE---DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnNVAPKDRD-- 78
Cdd:COG4181 9 IELRGLTKTVGTGAG-ELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 -------IAMVFQNYALYPHMTVYDNMAFGLKLRkySKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:COG4181 85 arlrarhVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 152 RDAKVFLMDEPLSNLDAKlrvsMRAEIAK----IHRRIGATTIYVTHDQteamTLA---DRIVIMSA 211
Cdd:COG4181 163 TEPAILFADEPTGNLDAA----TGEQIIDllfeLNRERGTTLVLVTHDP----ALAarcDRVLRLRA 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-232 |
2.09e-36 |
|
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: 131.72 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 7 KNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDG-TVVNNVAPKDRDIAMVFQN 85
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 86 YALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSN 165
Cdd:cd03265 82 LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 166 LDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH----------GRIIAEGTPEE 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-233 |
3.07e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 132.13 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELnlKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RD 78
Cdd:COG4604 1 MIEI--KNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFGlklR-KYSK-----EDIDKrVQEAAEILGLKEFLDRKPADLSGGQRQR--VAMgrAI 150
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFG---RfPYSKgrltaEDREI-IDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 151 VRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMsatKNpagtgtiGRVEQIGSP 230
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM---KD-------GRVVAQGTP 220
|
...
gi 881073645 231 QEV 233
Cdd:COG4604 221 EEI 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-246 |
1.45e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.54 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGeCSIDGTVV---NNVAPKDRD-------IAMVFQNYALYP 90
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPG-ARVEGEILldgEDIYDPDVDvvelrrrVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 hMTVYDNMAFGLKLRKY-SKEDIDKRVQEAAEILGL----KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSN 165
Cdd:COG1117 106 -KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 166 LD----AKLRVSMRaEIAKIHrrigaTTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKF 241
Cdd:COG1117 185 LDpistAKIEELIL-ELKKDY-----TIVIVTHNMQQAARVSDYTAFFYL----------GELVEFGPTEQIFTNPKDKR 248
|
....*
gi 881073645 242 VAGFI 246
Cdd:COG1117 249 TEDYI 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-209 |
1.49e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.51 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvnnvapkDRDIAMVFQNYAL---YPhMTVYDN 97
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP-LTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGL-----KLRKYSKEDiDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRV 172
Cdd:NF040873 78 VAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 881073645 173 SMRAEIAKIHRRiGATTIYVTHDQTEAMtLADRIVIM 209
Cdd:NF040873 157 RIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-209 |
4.37e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 4.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPnsehySV---EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-RD- 78
Cdd:COG1129 5 LEMRGISKSFG-----GVkalDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 -IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEIL---GLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLarlGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881073645 155 KVFLMDEPLSNLDAKlrvsmraEIAKIHRRI------GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1129 160 RVLILDEPTASLTER-------EVERLFRIIrrlkaqGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-233 |
1.47e-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: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIA 80
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKysKEDIDKRVQEAAEIL-GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLER----------GRVVLEGTAAEL 219
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
24-248 |
4.45e-34 |
|
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: 126.48 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 24 FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV-------NNVAPKD--------RDIAMVFQNYAL 88
Cdd:TIGR03005 19 LNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrnGPLVPADekhlrqmrNKIGMVFQSFNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 YPHMTVYDNMAFGLKLRK-YSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:TIGR03005 99 FPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 168 AKLrvsmRAEIAKIHRRIGA----TTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVA 243
Cdd:TIGR03005 179 PEL----VGEVLNVIRRLASehdlTMLLVTHEMGFAREFADRVCFFDK----------GRIVEQGKPDEIFRQPKEERTR 244
|
....*
gi 881073645 244 GFIGS 248
Cdd:TIGR03005 245 EFLSK 249
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-209 |
5.03e-34 |
|
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: 132.03 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 13 YPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYP 90
Cdd:TIGR02857 331 YPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 HmTVYDNMAFGlklRKYSKEDidkRVQEAAEILGLKEF-----------LDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:TIGR02857 410 G-TIAENIRLA---RPDASDA---EIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDqTEAMTLADRIVIM 209
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-247 |
5.23e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 126.50 E-value: 5.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIT-----EGECSIDGTVVNN--VAPKD--RDIAMVFQNYALYPH 91
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEvrREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 92 MTVYDNMAFGLKLRKY--SKEDIDKRVQEAAEILGL----KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSN 165
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 166 LDAKLRVSMRAEIAKIHRRIgaTTIYVTHDQTEAMTLADRIVIMsatknpagtgTIGRVEQIGSPQEVYKNPVN----KF 241
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFL----------YLGKLIEVGPTRKVFENPEHelteKY 247
|
....*.
gi 881073645 242 VAGFIG 247
Cdd:PRK14267 248 VTGALG 253
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-248 |
5.25e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.45 E-value: 5.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV-------NNVAPKD 76
Cdd:COG4598 9 LEVRDLHKSF--GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 RD--------IAMVFQNYALYPHMTVYDNMAFG----LKLRKyskedidKRVQEAAEIL----GLKEFLDRKPADLSGGQ 140
Cdd:COG4598 87 RRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApvhvLGRPK-------AEAIERAEALlakvGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 141 RQRVAMGRAIVRDAKVFLMDEPLSNLDAK-----LRVsMRAeIAKIHRrigaTTIYVTHDQTEAMTLADRIVIMSAtknp 215
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPElvgevLKV-MRD-LAEEGR----TMLVVTHEMGFARDVSSHVVFLHQ---- 229
|
250 260 270
....*....|....*....|....*....|...
gi 881073645 216 agtgtiGRVEQIGSPQEVYKNPVNKFVAGFIGS 248
Cdd:COG4598 230 ------GRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-209 |
1.18e-33 |
|
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: 123.87 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYPHMTVYDNMAFGLKLRKYSKedidKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 881073645 164 SNLDAKLRVSMRAEIAKiHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03268 155 NGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGII 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-238 |
3.01e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 126.91 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 35 VFvGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN------NVAPKDRDIAMVFQNYALYPHMTVYDNMAFGLKlrKYS 108
Cdd:PRK11144 29 IF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 109 KEDIDKRVQeaaeILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGAT 188
Cdd:PRK11144 106 VAQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 189 TIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQ----------GKVKAFGPLEEVWASSA 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-235 |
1.37e-32 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 121.95 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYpHMTVYDNMAFGlklrkysKEDI-DKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRA 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG-------RPGAtREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGS 229
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLED----------GKIVERGT 219
|
....*.
gi 881073645 230 PQEVYK 235
Cdd:cd03251 220 HEELLA 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-237 |
1.94e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 123.21 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSI-DGTVVNNVAPKD-----RDIAMVFQnyalYP-HM--- 92
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKlkplrKKVGIVFQ----FPeHQlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 93 -TVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKE-FLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL 170
Cdd:PRK13634 101 eTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 171 RVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP 237
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK----------GTVFLQGTPREIFADP 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-209 |
2.17e-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: 120.44 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPnsEHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvNNVAPKDR--DIAMV 82
Cdd:cd03226 2 IENISFSYK--KGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERrkSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQN--YALYPHmTVYDNMAFGLKlrkyskeDIDKRVQEAAEIL---GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:cd03226 77 MQDvdYQLFTD-SVREELLLGLK-------ELDAGNEQAETVLkdlDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 158 LMDEPLSNLDAKlrvSMRaEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03226 149 IFDEPTSGLDYK---NME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-237 |
2.48e-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: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiTEGECSIDGTVVNNVAPKD-----RDIAMVFQN-YA-LYPHMT 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAFGLKL--RKYSKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDakl 170
Cdd:COG4172 381 VGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--- 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 171 rVSMRAEI----AKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGR-VEQiGSPQEVYKNP 237
Cdd:COG4172 458 -VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD----------GKvVEQ-GPTEQVFDAP 517
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-236 |
4.75e-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: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPN-SEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMV 82
Cdd:cd03249 3 FKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPhMTVYDNMAFGLklrkysKEDIDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAIV 151
Cdd:cd03249 83 SQEPVLFD-GTIAENIRYGK------PDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDAKlrvSMRAEIAKIHR-RIGATTIYVTHDQTeamTL--ADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:cd03249 156 RNPKILLLDEATSALDAE---SEKLVQEALDRaMKGRTTIVIAHRLS---TIrnADLIAVLQN----------GQVVEQG 219
|
....*...
gi 881073645 229 SPQEVYKN 236
Cdd:cd03249 220 THDELMAQ 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-209 |
7.56e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.95 E-value: 7.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPN------SEHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVA 73
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 74 PKD-----RDIAMVFQNY--ALYPHMTVYDNMAFGLK-LRKYSKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRV 144
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 145 AMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVM 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-209 |
1.55e-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: 120.30 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNS------EHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD 76
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakQRAPVlTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 -----RDIAMVFQNY--ALYPHMTVYDNMAFGLK-LRKYSKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMG 147
Cdd:TIGR02769 83 rrafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 148 RAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-210 |
2.20e-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: 118.06 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIkDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD-IAMV 82
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 163 LSNLDAKLRVSMRAEIAkihrRIGATTIYV--THDQTEAMTLADRIVIMS 210
Cdd:cd03264 158 TAGLDPEERIRFRNLLS----ELGEDRIVIlsTHIVEDVESLCNQVAVLN 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-209 |
2.29e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.42 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKK-YPNS--EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR--D 78
Cdd:COG1101 2 LELKNLSKTfNPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYAL--YPHMTVYDNMA--------FGLKLRKySKEDIDKRVQEAAEI-LGLKEFLDRKPADLSGGQRQRVAMG 147
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGL-TKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 148 RAIVRDAKVFLMDEPLSNLDAKlrvsmRAEI-----AKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPK-----TAALvleltEKIVEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-237 |
3.30e-31 |
|
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: 118.16 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIA 80
Cdd:COG0410 4 LEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKySKEDIDKRVQEAAEIL-GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP 237
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLER----------GRIVLEGTAAELLADP 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-209 |
7.49e-31 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 115.39 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-RD-IAM 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHmTVYDNMafglklrkyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 881073645 162 PLSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVL 168
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-244 |
1.13e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.76 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDI--- 79
Cdd:PRK10619 5 KLNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 ------------AMVFQNYALYPHMTVYDN-MAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRK-PADLSGGQRQRVA 145
Cdd:PRK10619 83 dknqlrllrtrlTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 146 MGRAIVRDAKVFLMDEPLSNLDAKLrvsmRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiG 222
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQ----------G 228
|
250 260
....*....|....*....|....*.
gi 881073645 223 RVEQIGSPQEVYKNP----VNKFVAG 244
Cdd:PRK10619 229 KIEEEGAPEQLFGNPqsprLQQFLKG 254
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-206 |
1.18e-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: 116.30 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKY-PNSEHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---- 77
Cdd:TIGR02211 2 LKCENLGKRYqEGKLDTRVlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 --DIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDqteaMTLADRI 206
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-237 |
1.20e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.43 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR-----DIAMVFQN--YALYPHM 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 93 TVYDNMAFGLKLR--KYSKEDIDKRVQEAAEILGLKEFL-DRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDak 169
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD-- 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 170 lrVSMRAEIA----KIHRRIGATTIYVTHDQTEAMTLADRIVIMsatknpagtgTIGRVEQIGSPQEVYKNP 237
Cdd:PRK15079 194 --VSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKHISDRVLVM----------YLGHAVELGTYDEVYHNP 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
3.23e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.90 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPnsehySV---EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-RD- 78
Cdd:COG3845 6 LELRGITKRFG-----GVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 -IAMVFQNYALYPHMTVYDNMAFGL---KLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG3845 81 gIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 155 KVFLMDEPLSNLD----AKLRVSMRAEIAKihrriGATTIYVTHDQTEAMTLADRIVIM-----SATKNPAGT 218
Cdd:COG3845 161 RILILDEPTAVLTpqeaDELFEILRRLAAE-----GKSIIFITHKLREVMAIADRVTVLrrgkvVGTVDTAET 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-239 |
4.26e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 116.29 E-value: 4.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDItEGECSIDGTVV----------NNVAPKDRDIAMVFQNYALYP 90
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVEffnqniyerrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 hMTVYDNMAFGLKL----RKYSKEDIDKRVQEAAEILG-LKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSN 165
Cdd:PRK14258 102 -MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 166 LDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSATKNpagtgTIGRVEQIGSPQEVYKNPVN 239
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN-----RIGQLVEFGLTKKIFNSPHD 249
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-244 |
4.43e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.78 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 25 NLDIKDKEFIVFVGPSGCGKSTTLRMIAGL-----EDITEGECSIDGTVV--NNVAPKDRDIAMVFQNYALYPHMTVYDN 97
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRRVQMVFQIPNPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGLKLRKY--SKEDIDKRVQEAAEILGL----KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:PRK14247 103 VALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 172 VSMRAEIAKIHRRIgaTTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP----VNKFVAG 244
Cdd:PRK14247 183 AKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYK----------GQIVEWGPTREVFTNPrhelTEKYVTG 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-209 |
5.31e-30 |
|
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: 114.30 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvNNVAPKDRD-IAMV 82
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNrIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 163 LSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03269 156 FSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-209 |
5.41e-30 |
|
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: 112.91 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---RDIA 80
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQnyalyphmtvydnmafglklrkyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVL 155
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-247 |
9.58e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 115.26 E-value: 9.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 8 NIYkkYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGeCSIDGTVV---NNVAPKD-------R 77
Cdd:PRK14243 17 NVY--YGS--FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgKNLYAPDvdpvevrR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 DIAMVFQNYALYPHmTVYDNMAFGLKLRKYsKEDIDKRVQEAAEILGL----KEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK14243 92 RIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIgaTTIYVTHDQTEAMTLADRIVIMSATKNPAGtGTIGRVEQIGSPQEV 233
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVELTEGG-GRYGYLVEFDRTEKI 246
|
250
....*....|....*...
gi 881073645 234 YKNPVNK----FVAGFIG 247
Cdd:PRK14243 247 FNSPQQQatrdYVSGRFG 264
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-233 |
2.67e-29 |
|
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: 113.09 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYpNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:cd03254 2 EIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHmTVYDNMAFGlklRKYSKEDidkRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRA 149
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIhrRIGATTIYVTHDQTeamTL--ADRIVIMSAtknpagtgtiGRVEQI 227
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLS---TIknADKILVLDD----------GKIIEE 218
|
....*.
gi 881073645 228 GSPQEV 233
Cdd:cd03254 219 GTHDEL 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-237 |
2.88e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.45 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnVAPKD------RDIAMVFQN-YA-LYPHMTVYDNMAFGLKLR-KY 107
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQDLL-KADPEaqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 108 SKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEI----AKIH 182
Cdd:PRK11308 126 SAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD----VSVQAQVlnlmMDLQ 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 183 RRIGATTIYVTHDQTEAMTLADRIVIMsatknpagtgTIGRVEQIGSPQEVYKNP 237
Cdd:PRK11308 202 QELGLSYVFISHDLSVVEHIADEVMVM----------YLGRCVEKGTKEQIFNNP 246
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-206 |
3.43e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.99 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYS--VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAP------K 75
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 76 DRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDqteaMTLADRI 206
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-213 |
8.55e-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: 117.51 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAM 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHmTVYDNMAFGlKLRKYSKEdidkRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAI 150
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRA----EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 151 VRDAKVFLMDEPLSNLDAKlrvSMRAEIAKIHRRI-GATTIYVTHDQTeAMTLADRIVIMSATK 213
Cdd:TIGR02203 485 LKDAPILILDEATSALDNE---SERLVQAALERLMqGRTTLVIAHRLS-TIEKADRIVVMDDGR 544
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-210 |
9.48e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvaPKDRD-IAmv 82
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRrIG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 fqnY-----ALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:COG4152 75 ---YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 158 LMDEPLSNLD---AKLrvsMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:COG4152 152 ILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIIN 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-211 |
1.25e-28 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.68 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHmTVYDNMA-FGlklrkyskEDIDKR-VQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMG 147
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIArFG--------ENADPEkIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 148 RAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHdQTEAMTLADRIVIMSA 211
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQD 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-233 |
1.44e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.64 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNM 98
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFG----LKL-RKYSKEDiDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVS 173
Cdd:PRK11231 98 AYGrspwLSLwGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD----IN 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 174 MRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK11231 173 HQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLAN----------GHVMAQGTPEEV 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-238 |
1.50e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 13 YPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL---EDITEGECSIDGTVVNNVAPKD-RD-IAMVFQNY- 86
Cdd:PRK13640 15 YPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiREkVGIVFQNPd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 87 ALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:PRK13640 95 NQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 167 DAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAmTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDD----------GKLLAQGSPVEIFSKVE 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
1.78e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.38 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED-----ITEGECSIDGTVVNN---- 71
Cdd:PRK11264 1 MSAIEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTARSLSqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 72 -VAPKDRDIAMVFQNYALYPHMTVYDNMAFG-LKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRA 149
Cdd:PRK11264 79 lIRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKI--HRRigaTTIYVTHDQTEAMTLADRIVIMSAtknpagtGTIgrVEQi 227
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQ-------GRI--VEQ- 225
|
250
....*....|
gi 881073645 228 GSPQEVYKNP 237
Cdd:PRK11264 226 GPAKALFADP 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-199 |
1.88e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 110.64 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 26 LDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR------DIAMVFQNYALYPHMTVYDNMA 99
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 100 FGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIA 179
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180
....*....|....*....|
gi 881073645 180 KIHRRIGATTIYVTHDQTEA 199
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLA 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-236 |
2.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.10 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 7 KNIYKKYPNSE----HYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDG---TVVNNVAPKDRDI 79
Cdd:PRK13633 8 KNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:PRK13633 88 GMVFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 155 KVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSPQEVY 234
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS----------GKVVMEGTPKEIF 232
|
..
gi 881073645 235 KN 236
Cdd:PRK13633 233 KE 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-234 |
3.64e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.34 E-value: 3.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKY-PNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGT--VVNNVAPKDRDIA 80
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNY-ALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSPQEVY 234
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKA----------GEIIKEAAPSELF 228
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-240 |
2.38e-27 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 107.84 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED----ITEGECSIDGTVVNNVAPKDRDIAMVFQN--YALYPHMTV 94
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFGLKLRKYSKEDIDKRVQEAAEILGL---KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 172 VSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNK 240
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD----------GRIVERGTVKEIFYNPKHE 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-195 |
2.87e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 107.27 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLdiKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-----RDIAMVFQNYALYPHMTVYDN 97
Cdd:PRK10908 22 TFHM--RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAE 177
Cdd:PRK10908 100 VAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRL 179
|
170
....*....|....*...
gi 881073645 178 IAKIHrRIGATTIYVTHD 195
Cdd:PRK10908 180 FEEFN-RVGVTVLMATHD 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
4.54e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.30 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVF 83
Cdd:PRK13648 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK13648 90 QN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 159 MDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNK----------GTVYKEGTPTEIFD 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
6.30e-27 |
|
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: 111.82 E-value: 6.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEH---YSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECS-------IDGTV--VNN 71
Cdd:TIGR03269 280 IKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKpgPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 72 VAPKDRDIAMVFQNYALYPHMTVYDNM--AFGLKLrkySKEDIDKRVQEAAEILGL-----KEFLDRKPADLSGGQRQRV 144
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 145 AMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRV 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD----------GKI 506
|
....*....
gi 881073645 225 EQIGSPQEV 233
Cdd:TIGR03269 507 VKIGDPEEI 515
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-249 |
6.58e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.28 E-value: 6.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 10 YKKYPNSEHYS--VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNN------VAPKDRDIAM 81
Cdd:PRK13643 9 YTYQPNSPFASraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQnyalYPHM-----TVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK13643 89 VFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHrRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEK----------GHIISCGTPSDVFQ 233
|
250
....*....|....
gi 881073645 236 NpVNKFVAGFIGSP 249
Cdd:PRK13643 234 E-VDFLKAHELGVP 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-211 |
2.15e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.18 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHmTVYDNM 98
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFGLKLRKyskedidKRVQEAAEILGLKEF------LDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRV 172
Cdd:PRK10247 102 IFPWQIRN-------QQPDPAIFLDDLERFalpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 881073645 173 SMRAEIAKIHRRIGATTIYVTHDQTEaMTLADRIVIMSA 211
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQP 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-236 |
2.67e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.63 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 5 NLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEdITE------GECSIDGTV--VNNVAPKD 76
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISEtgqtivGDYAIPANLkkIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 RDIAMVFQ--NYALYPHmTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK13645 90 KEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHE----------GKVISIGSPFEI 238
|
...
gi 881073645 234 YKN 236
Cdd:PRK13645 239 FSN 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-235 |
3.01e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.98 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVApKDRDI-------AMVFQnyalYPHM--- 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-KNKDIkqirkkvGLVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 93 --TVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKE-FLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 170 LRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:PRK13649 180 GRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEK----------GKLVLSGKPKDIFQ 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-246 |
5.39e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 5.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEgECSIDGTVVNN----VAPKD------RDIAMVFQNYALY 89
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYNghniYSPRTdtvdlrKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 90 PhMTVYDNMAFGLKLRK-YSKEDIDKRVQEA---AEILG-LKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK14239 99 P-MSIYENVVYGLRLKGiKDKQVLDEAVEKSlkgASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 165 NLDAKlrVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAG 244
Cdd:PRK14239 178 ALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLD----------GDLIEYNDTKQMFMNPKHKETED 245
|
..
gi 881073645 245 FI 246
Cdd:PRK14239 246 YI 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-245 |
5.39e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.43 E-value: 5.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVE---DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnNVAPKDRD-- 78
Cdd:PRK10535 5 LELKDIRRSYPSGEE-QVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ---DVATLDADal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 -------IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:PRK10535 81 aqlrrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDAKLRVSMRAeIAKIHRRIGATTIYVTHDQTEAMTlADRIVIMSATKNPAGTGTIGRVEQIGSPQ 231
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGTE 238
|
250
....*....|....*.
gi 881073645 232 EVYKNP--VNKFVAGF 245
Cdd:PRK10535 239 PVVNTAsgWRQFVSGF 254
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
22-232 |
6.30e-26 |
|
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: 109.28 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN--NVAPKDRDIAMVFQNYALYPHmTVYDNMA 99
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFENIA 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 100 FGLKLrkySKEDidkrVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:TIGR03797 549 GGAPL---TLDE----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEATSALDN 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 169 KLRVSMRAEIAkihrRIGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:TIGR03797 622 RTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDA----------GRVVQQGTYDE 670
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-237 |
9.52e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.79 E-value: 9.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYP---------NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVA- 73
Cdd:PRK10261 314 LQVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 74 ----PKDRDIAMVFQN-YA-LYPHMTVYDNMAFGLKLRKY-SKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVA 145
Cdd:PRK10261 394 gklqALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRIC 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 146 MGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAK----IHRRIGATTIYVTHDQTEAMTLADRIVIMSatknpagtgtI 221
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALD----VSIRGQIINllldLQRDFGIAYLFISHDMAVVERISHRVAVMY----------L 539
|
250
....*....|....*.
gi 881073645 222 GRVEQIGSPQEVYKNP 237
Cdd:PRK10261 540 GQIVEIGPRRAVFENP 555
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-246 |
1.41e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN--------NVAPKDRDIAMVFQNYALYPHM 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 93 TVYDNMAFGLKLRKYS-KEDIDKRVQEAAEILGL-KEFLDR--KPAD-LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRlnSPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 168 AKLRVSMRAEIAKIHRRIgaTTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFI 246
Cdd:PRK14246 186 IVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYN----------GELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-211 |
1.65e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVF 83
Cdd:PRK13647 7 VEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNyalyPH-----MTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK13647 86 QD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 159 MDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSA 211
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-249 |
1.88e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.69 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvNNVAPKDRD--------IAMVFQNYALYPHMT 93
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPAMSRSrlytvrkrMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAFglKLRKYSK---EDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL 170
Cdd:PRK11831 101 VFDNVAY--PLREHTQlpaPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 171 RVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSATKnpagtgtigrVEQIGSPQEVYKNP---VNKFVAGFIG 247
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKK----------IVAHGSAQALQANPdprVRQFLDGIAD 248
|
..
gi 881073645 248 SP 249
Cdd:PRK11831 249 GP 250
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-243 |
1.96e-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: 102.60 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIA 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILglKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAklrvSMRAEIAKIHRRI----GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:TIGR03410 157 EPTEGIQP----SIIKDIGRVIRRLraegGMAILLVEQYLDFARELADRYYVMER----------GRVVASGAGDELDED 222
|
....*..
gi 881073645 237 PVNKFVA 243
Cdd:TIGR03410 223 KVRRYLA 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-209 |
2.24e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 102.23 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNS--------------------EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECS 63
Cdd:cd03220 1 IELENVSKSYPTYkggssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 64 IDGTVVnnvapkdrdiAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQR 143
Cdd:cd03220 81 VRGRVS----------SLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 144 VAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-210 |
4.71e-25 |
|
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: 100.70 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNI--YKKYPNSEHYS--VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ITEGECSIDGTVVNNVAP 74
Cdd:cd03213 1 GVTLSFRNLtvTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 75 KDRdIAMVFQNYALYPHMTVYDNMAFGLKLRKyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDA 154
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 155 KVFLMDEPLSNLDAklrvSMRAEIAKIHRRI---GATTIYVTHD-QTEAMTLADRIVIMS 210
Cdd:cd03213 131 SLLFLDEPTSGLDS----SSALQVMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLS 186
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-235 |
1.14e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.93 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 17 EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnVAPkdRDIAMVFQnyalyPHMTVYD 96
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---SAL--LELGAGFH-----PELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 97 NMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRvsMRA 176
Cdd:COG1134 108 NIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ--KKC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 881073645 177 EiAKIHRRI--GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:COG1134 186 L-ARIRELResGRTVIFVSHSMGAVRRLCDRAIWLEK----------GRLVMDGDPEEVIA 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
1.22e-24 |
|
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: 105.14 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 2 VELNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDI 79
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNyalyPHM---TVYDNMAFGlklrkySKEDIDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVA 145
Cdd:TIGR02868 412 SVCAQD----AHLfdtTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 146 MGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHD 195
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
23-207 |
1.90e-24 |
|
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: 100.54 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGEcSID-------GTVVNNVAPKdrdIAMV---FQNYaLYPHM 92
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-DVRlfgerrgGEDVWELRKR---IGLVspaLQLR-FPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 93 TVYDNMA------FGLkLRKYSKEDIDkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:COG1119 96 TVLDVVLsgffdsIGL-YREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 167 DAKLRVSMRAEIAKIHRRIGATTIYVTHDQ-------TEAMTLAD-RIV 207
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVeeippgiTHVLLLKDgRVV 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-237 |
1.98e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.22 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVA--PKDRDI-A 80
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQN-YALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDqTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP 237
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDR----------GKIVLEGEPENVLSDV 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-235 |
2.25e-24 |
|
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: 104.44 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:COG4618 330 RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHmTVYDNMA-FGlklrkyskEDIDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGR 148
Cdd:COG4618 410 YLPQDVELFDG-TIAENIArFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 149 AIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTeAMTLADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRD----------GRVQAFG 548
|
....*..
gi 881073645 229 SPQEVYK 235
Cdd:COG4618 549 PRDEVLA 555
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-232 |
3.36e-24 |
|
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: 99.61 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYpHMTVYDNMAF 100
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVLF-NDTIGYNIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 GlklrKYSKEDIDkrVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:cd03253 98 G----RPDATDEE--VIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 170 LRVSMRAEIAKIHRriGATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:cd03253 172 TEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKD----------GRIVERGTHEE 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-238 |
3.41e-24 |
|
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: 99.15 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIA 80
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDAKLRVSMRAEIAKIHRR-IGattIYVT-HDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYE----------GKVLAEGTPEEIAANEL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-233 |
4.05e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 99.10 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK--DRDIAMVF 83
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNYALYpHMTVYDNMAFGlklrkysKEDID-KRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAIV 151
Cdd:cd03252 83 QENVLF-NRSIRDNIALA-------DPGMSmERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDAKlrvSMRAEIAKIHRRI-GATTIYVTHDQTEAMTlADRIVIMSAtknpagtgtiGRVEQIGSP 230
Cdd:cd03252 155 HNPRILIFDEATSALDYE---SEHAIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEK----------GRIVEQGSH 220
|
...
gi 881073645 231 QEV 233
Cdd:cd03252 221 DEL 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
7.90e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.56 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNSEhySVEDFNLDIKDKEfIV-FVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVA------ 73
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 74 ------PKDrdiAMVFQNyalyphMTVYDN-MAFgLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAM 146
Cdd:COG1137 78 lgigylPQE---ASIFRK------LTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 147 GRAIVRDAKVFLMDEPLSNLDAkLRVsmrAEIAKI-----HRRIGattIYVT-HDQTEAMTLADRIVIMSAtknpagtgt 220
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDP-IAV---ADIQKIirhlkERGIG---VLITdHNVRETLGICDRAYIISE--------- 211
|
250
....*....|....*..
gi 881073645 221 iGRVEQIGSPQEVYKNP 237
Cdd:COG1137 212 -GKVLAEGTPEEILNNP 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-287 |
1.00e-23 |
|
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: 103.55 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGT-VVNNVAPKDRDIAMVFQ 84
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 85 NYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 165 NLDAKLRVSMRAEIAKIhrRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYknpvNKFVAG 244
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQ----------GRLYCSGTPLFLK----NCFGTG 1154
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 881073645 245 FIGSPAMNFINVKLEGG------YIVTNGLNLKVPEGALKVLKEKGYDG 287
Cdd:TIGR01257 1155 FYLTLVRKMKNIQSQRGgcegtcSCTSKGFSTRCPARVDEITPEQVLDG 1203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-209 |
1.14e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.62 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 25 NLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDItEGECSIDGTVVNNVAPKD--RDIAMVFQNYALyPHMTVYDNMAFGl 102
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 103 klrkysKEDI-DKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK- 169
Cdd:PRK11174 447 ------NPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHs 520
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 881073645 170 -LRVsMRAeIAKIHRriGATTIYVTH--DQTEAMtlaDRIVIM 209
Cdd:PRK11174 521 eQLV-MQA-LNAASR--RQTTLMVTHqlEDLAQW---DQIWVM 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-167 |
1.36e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.40 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYpHMTVYDNMAFGLKlRKYSKEDIDKrvqeAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRA 149
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-EQYSREQIEE----AARMAYAMDFINKMDngldtvigengVLLSGGQRQRIAIARA 494
|
170
....*....|....*...
gi 881073645 150 IVRDAKVFLMDEPLSNLD 167
Cdd:PRK11176 495 LLRDSPILILDEATSALD 512
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-233 |
1.47e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.69 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYAL---------- 88
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfefdvrqvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 ----YPHMTVYDNMAfglklrkyskEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK09536 99 emgrTPHRSRFDTWT----------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 165 NLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLAD----------GRVRAAGPPADV 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-208 |
2.83e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.62 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnvaP-KDR-----DIAMVF-QNYALYPHMT 93
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PfKRRkefarRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNmaFGLkLRK-Y--SKEDIDKRVQEAAEILGLKEFLD---RKpadLSGGQRQR--VAMgrAIVRDAKVFLMDEPLSN 165
Cdd:COG4586 113 AIDS--FRL-LKAiYriPDAEYKKRLDELVELLDLGELLDtpvRQ---LSLGQRMRceLAA--ALLHRPKILFLDEPTIG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 881073645 166 LD--AKLRVsmRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVI 208
Cdd:COG4586 185 LDvvSKEAI--REFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-209 |
3.98e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.07 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD-IAMV 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYpHMTVYDNmafglklrkyskedidkrvqeaaeiLGLKefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:cd03247 81 NQRPYLF-DTTLRNN-------------------------LGRR---------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 163 LSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDQTeAMTLADRIVIM 209
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFL 169
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
4.14e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN--NVAPKDRD 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQN---YALYPhmTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK13652 80 VGLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDK----------GRIVAYGTVEEIFL 227
|
..
gi 881073645 236 NP 237
Cdd:PRK13652 228 QP 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-208 |
4.84e-23 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 96.71 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 11 KKYPNSEHYSVEDFnlDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDgtvVNNVAPKDRDIAMVFQnyalyp 90
Cdd:cd03237 7 KKTLGEFTLEVEGG--SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE---LDTVSYKPQYIKADYE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 hMTVYDnMAFGLKLRKYSKEDIDkrvQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDakl 170
Cdd:cd03237 76 -GTVRD-LLSSITKDFYTHPYFK---TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 881073645 171 rVSMRAEIAKIHRRIG----ATTIYVTHDQTEAMTLADRIVI 208
Cdd:cd03237 148 -VEQRLMASKVIRRFAenneKTAFVVEHDIIMIDYLADRLIV 188
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
6-235 |
4.87e-23 |
|
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: 100.79 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVaPKDR---DIAMV 82
Cdd:TIGR03796 480 LRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYpHMTVYDNMAfgLKLRKYSKEDIDKRVQEAA---EILGLKEFLDRK----PADLSGGQRQRVAMGRAIVRDAK 155
Cdd:TIGR03796 559 DQDIFLF-EGTVRDNLT--LWDPTIPDADLVRACKDAAihdVITSRPGGYDAElaegGANLSGGQRQRLEIARALVRNPS 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIakihRRIGATTIYVTHdQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYK 235
Cdd:TIGR03796 636 ILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAH-RLSTIRDCDEIIVLER----------GKVVQRGTHEELWA 700
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-194 |
4.94e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvnnvapKDRDIAMVF--------QNyALYPHMT 93
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--------GDIDDPDVAeachylghRN-AMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAFGLKLRKYSKEDIDkrvqEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlRVS 173
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVA 164
|
170 180
....*....|....*....|.
gi 881073645 174 MRAEIAKIHRRIGATTIYVTH 194
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-233 |
5.06e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.98 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNMA 99
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 100 FGLK-----LRKYSKEDIDKrVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK10253 104 RGRYphqplFTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 175 RAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK10253 183 LELLSELNREKGYTLAAVLHDLNQACRYASHLIALRE----------GKIVAQGAPKEI 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-209 |
5.08e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.01 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 17 EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL---EDITEGECSIDGTVVNNVAPKDRDI-------AMVFQNY 86
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrksrantGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 87 ALYPHMTVYDNMAFGLK---------LRKYSKEDiDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK09984 96 NLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 158 LMDEPLSNLDAK-LRVSMRAeIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK09984 175 LADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-211 |
6.02e-23 |
|
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: 95.96 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSI--DGTVVNNVAPKDRDIAMVFQNYALY--------P 90
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrviP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 HMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFL-DRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:COG4778 107 RVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 881073645 170 LRVSMRAEIAKIHRRiGATTIYVTHDqTEAM-TLADRIVIMSA 211
Cdd:COG4778 187 NRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTP 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-209 |
1.21e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 94.46 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 9 IYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnnvapkdrdIAMVFQNyAL 88
Cdd:cd03250 9 TWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 YPHMTVYDNMAFGLKLRKyskedidKRVQEAAEILGLKEFLDRKPA-D----------LSGGQRQRVAMGRAIVRDAKVF 157
Cdd:cd03250 77 IQNGTIRENILFGKPFDE-------ERYEKVIKACALEPDLEILPDgDlteigekginLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 158 LMDEPLSNLDAklRVSmraeiAKI-------HRRIGATTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03250 150 LLDDPLSAVDA--HVG-----RHIfencilgLLLNNKTRILVTH-QLQLLPHADQIVVL 200
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-233 |
1.82e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNM 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIV-------RDAKVFLMDEPLSNLDAK-- 169
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAhq 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 170 LRVsMRaeIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:COG4559 177 HAV-LR--LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQ----------GRLVAQGTPEEV 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-209 |
1.92e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 99.05 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK--DRDIAM 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 VFQNYALYPHmTVYDNMAFGlklrkySKEDIDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRAI 150
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALC------NPGAPFEHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARAL 608
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 151 VRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHdQTEAMTLADRIVIM 209
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVL 664
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-210 |
2.27e-22 |
|
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: 94.32 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEHYSVE---DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGtvvnNVAPKDRD---- 78
Cdd:cd03267 19 LIGSLKSLFKRKYREVEalkGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKkflr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 -IAMVF-QNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:cd03267 95 rIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-237 |
4.27e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.37 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN-------NVAPKd 76
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 rdIAMVFQN-----YAlyPhmTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:PRK13639 80 --VGIVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQ 231
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSD----------GKIIKEGTPK 222
|
....*.
gi 881073645 232 EVYKNP 237
Cdd:PRK13639 223 EVFSDI 228
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
3-233 |
5.75e-22 |
|
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: 97.27 E-value: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:TIGR01192 334 AVEFRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESlrKSIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYpHMTVYDNMAFGlklrkysKED-IDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGR 148
Cdd:TIGR01192 413 TVFQDAGLF-NRSIRENIRLG-------REGaTDEEVYEAAKAAAAHDFILKRSngydtlvgergNRLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 149 AIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIhrRIGATTIYVTHdQTEAMTLADRIVIMSAtknpagtgtiGRVEQIG 228
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDAL--RKNRTTFIIAH-RLSTVRNADLVLFLDQ----------GRLIEKG 551
|
....*
gi 881073645 229 SPQEV 233
Cdd:TIGR01192 552 SFQEL 556
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-237 |
6.05e-22 |
|
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: 97.06 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTT----LRMIAGLEDITEGECSIDGTVVNNVAPKD------RDIAMVFQN--YAL 88
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmTSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 YPHMTVYDNMAFGLKL-RKYSKEDIDKRVQEAAEILGLKE---FLDRKPADLSGGQRQRV--AMgrAIVRDAKVFLMDEP 162
Cdd:COG4172 106 NPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVmiAM--ALANEPDLLIADEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 163 LSNLDaklrVSMRAEI----AKIHRRIGATTIYVTHDqteaMTL----ADRIVIMSAtknpagtGTIgrVEQiGSPQEVY 234
Cdd:COG4172 184 TTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQ-------GEI--VEQ-GPTAELF 245
|
...
gi 881073645 235 KNP 237
Cdd:COG4172 246 AAP 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-232 |
7.58e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.50 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvaPKDRDIAM----VFQNYALYPHMTVYD 96
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRRrvgyMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 97 NMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRA 176
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 177 EIAKIHRRIGaTTIYV-THDQTEAMtLADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:NF033858 439 LLIELSREDG-VTIFIsTHFMNEAE-RCDRISLMHA----------GRVLASDTPAA 483
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-237 |
7.84e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.53 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 5 NLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL----------EDITEGECSIDGTVVNNVAP 74
Cdd:PRK13631 26 NLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 75 KD--------RDIAMVFQ--NYALYPHmTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKE-FLDRKPADLSGGQRQR 143
Cdd:PRK13631 106 KKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 144 VAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMrAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGR 223
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK----------GK 253
|
250
....*....|....
gi 881073645 224 VEQIGSPQEVYKNP 237
Cdd:PRK13631 254 ILKTGTPYEIFTDQ 267
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-195 |
8.91e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 17 EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTT----LRMIAglediTEGECSIDGTVVNNVAPKD-----RDIAMVFQ--N 85
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 86 YALYPHMTVYDNMAFGLKL--RKYSKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190
....*....|....*....|....*....|...
gi 881073645 163 LSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHD 195
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-168 |
9.44e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIdgtvvnnvaPKDRDIAMVFQNYALYPHMTVYDNMAFG 101
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPPLDDDLTVLDTVLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 102 LK-----LRKY---------SKEDIDK--RVQE-------------AAEIL-GLK---EFLDRKPADLSGGQRQRVAMGR 148
Cdd:COG0488 86 DAelralEAELeeleaklaePDEDLERlaELQEefealggweaearAEEILsGLGfpeEDLDRPVSELSGGWRRRVALAR 165
|
170 180
....*....|....*....|
gi 881073645 149 AIVRDAKVFLMDEPLSNLDA 168
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLDL 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-210 |
1.27e-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: 91.95 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYS--VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED---ITEGECSIDGTVVNNVAPKDRd 78
Cdd:cd03234 4 LPWWDVGLKAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDiDKRVQEAAEILGLKEFLDRKPAD-----LSGGQRQRVAMGRAIVRD 153
Cdd:cd03234 83 VAYVRQDDILLPGLTVRETLTYTAILRLPRKSS-DAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 154 AKVFLMDEPLSNLD---AKLRVSMRAEIAKIHRrigatTIYVTHDQ--TEAMTLADRIVIMS 210
Cdd:cd03234 162 PKVLILDEPTSGLDsftALNLVSTLSQLARRNR-----IVILTIHQprSDLFRLFDRILLLS 218
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-233 |
1.63e-21 |
|
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: 91.84 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 32 EFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnNVAPKDRDIAMVFQNYAL---YP---HMTVYDNMAFGLKLR 105
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPisvAHTVMSGRTGHIGWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 106 KYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD---AKLRVSMRAEIAKih 182
Cdd:TIGR03771 84 RRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFIELAG-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 183 rrIGATTIYVTHDQTEAMTLADRIVIMSatknpagtgtiGRVEQIGSPQEV 233
Cdd:TIGR03771 162 --AGTAILMTTHDLAQAMATCDRVVLLN-----------GRVIADGTPQQL 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-233 |
2.10e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD-IAMV 82
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMA-----FGLklrkySKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLvfgryFGL-----SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEE----------GRKIAEGAPHAL 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-232 |
2.33e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.41 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 12 KYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALY 89
Cdd:PRK13657 343 SYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 90 pHMTVYDNMAFGlklrkysKED-IDKRVQEAAEILGLKEFLDRKPA-----------DLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK13657 422 -NRSIEDNIRVG-------RPDaTDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 158 LMDEPLSNLDAKLRVSMRAEIAKIhrRIGATTIYVTHDQTeamTL--ADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS---TVrnADRILVFDN----------GRVVESGSFDE 555
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
32-194 |
2.52e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.50 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 32 EFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK-DRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKE 110
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFWAAIHGGAQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 111 DIDkrvqEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGATTI 190
Cdd:TIGR01189 107 TIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLARGGIVL 181
|
....
gi 881073645 191 YVTH 194
Cdd:TIGR01189 182 LTTH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-209 |
3.79e-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: 90.99 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 13 YPNSEHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK--DRDIAMVFQNYALY 89
Cdd:cd03248 21 YPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 90 PHmTVYDNMAFGLKlrkySKEDidKRVQEAAEILGLKEFL-----------DRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:cd03248 101 AR-SLQDNIAYGLQ----SCSF--ECVKEAAQKAHAHSFIselasgydtevGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 159 MDEPLSNLDAKLRVSMRAEIAKIHRRigaTTIYVTHDQTEAMTLADRIVIM 209
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-208 |
7.06e-21 |
|
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: 94.08 E-value: 7.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 8 NIYKKYPnsehysveDFNLD-----IKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGEcsIDGTVvnNVAPK------D 76
Cdd:COG1245 346 DLTKSYG--------GFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDL--KISYKpqyispD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 RDiamvfqnyalyphMTVYDNmafglkLRKYSKEDIDKRV--QEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:COG1245 414 YD-------------GTVEEF------LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 155 KVFLMDEPLSNLDaklrVSMRAEIAKIHRRI----GATTIYVTHDQTEAMTLADRIVI 208
Cdd:COG1245 475 DLYLLDEPSAHLD----VEQRLAVAKAIRRFaenrGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-236 |
7.86e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.34 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYpnSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNV---APKDR 77
Cdd:PRK10895 1 MATLTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 DIAMVFQNYALYPHMTVYDNMAFGLKLRK-YSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQ----------GHLIAHGTPTEILQD 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-230 |
8.42e-21 |
|
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: 89.48 E-value: 8.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 7 KNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTT----LRMIagleDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHmTVYDNMAFglkLRKYSkediDKRVQEAAEILGLKEFLDRKP-----------ADLSGGQRQRVAMGRA 149
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLDP---FGEYS----DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLD----AKLRVSMRAEIAkihrriGATTIYVTHdQTEAMTLADRIVIMSAtknpagtgtiGRVE 225
Cdd:cd03244 154 LLRKSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDK----------GRVV 216
|
....*
gi 881073645 226 QIGSP 230
Cdd:cd03244 217 EFDSP 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
37-238 |
9.30e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.62 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNMAFGL-----KLRKYSK 109
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELVAIGRypwhgALGRFGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 110 EDiDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATT 189
Cdd:PRK10575 123 AD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTV 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 190 IYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:PRK10575 202 IAVLHDINMAARYCDYLVALRG----------GEMIAQGTPAELMRGET 240
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-213 |
1.38e-20 |
|
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: 93.65 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVapkDRDIAMVFQNY-ALYPHM---TVYD 96
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 97 NMAFGLKlRKYSKEDIDKRVqEAAEI--------LGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:TIGR01193 567 NLLLGAK-ENVSQDEIWAAC-EIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 881073645 169 KLRVSMRAEIAKIHRRigaTTIYVTHDQTEAmTLADRIVIMSATK 213
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGK 685
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-233 |
1.49e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.83 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYAL-YPhMTVYDN 97
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-FTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVR------DAKVFLMDEPLSNLDakLR 171
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD--LA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 172 ---VSMRaeIAK--IHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:PRK13548 175 hqhHVLR--LARqlAHER-GLAVIVVLHDLNLAARYADRIVLLHQ----------GRLVADGTPAEV 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-295 |
1.68e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 5 NLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN----NVAPKD--RD 78
Cdd:PRK13641 7 NVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKlrKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQnyalYPHM-----TVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKE-FLDRKPADLSGGQRQRVAMGRAIVR 152
Cdd:PRK13641 87 VSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 153 DAKVFLMDEPLSNLDAKLRVSMrAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEH----------GKLIKHASPKE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 233 VYKNPvNKFVAGFIGSPAMNFINVKLEGGyivtnglNLKVPEGALKVlkekgydgKELIFGIR 295
Cdd:PRK13641 232 IFSDK-EWLKKHYLDEPATSRFASKLEKG-------GFKFSEMPLTI--------DELVDGIK 278
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-209 |
1.76e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR---DIA 80
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFG-LKLRKYSKEDI------DKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGrHLTKKVCGVNIidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 154 AKVFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK09700 164 AKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-234 |
2.65e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIYKKYPNSehYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR-DI 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYPHMTVYDNMA-----FGLKLRkyskeDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLvfgryFGMSTR-----EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 155 KVFLMDEPLSNLDAKLR----VSMRAEIAKihrriGATTIYVTHDQTEAMTLADRIVIMSATKNPAGTGTIGRV-EQIGS 229
Cdd:PRK13536 192 QLLILDEPTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIdEHIGC 266
|
....*.
gi 881073645 230 PQ-EVY 234
Cdd:PRK13536 267 QViEIY 272
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-209 |
2.91e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 2 VELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD-RD-I 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYPHmTVYDNMAFGlklrkySKEDIDKRVQEAAEILGLKEFLD-RKPAD---------LSGGQRQRVAMGRA 149
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGLEKLLEdDKGLNawlgeggrqLSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRriGATTIYVTHDQTeAMTLADRIVIM 209
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVM 546
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-210 |
3.07e-20 |
|
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: 87.10 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 18 HYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD---IAMV---FQNYALYPH 91
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 92 MTVYDNMAFglklrkyskedidkrvqeaaeilglkefldrkPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklr 171
Cdd:cd03215 93 LSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD---- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 881073645 172 VSMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:cd03215 137 VGAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMY 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-208 |
2.04e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV---NNVAPKDRDIA 80
Cdd:PRK11288 5 LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGL---KLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 158 LMDEPLSNLDAKlrvsmraEIAKIHRRI------GATTIYVTHDQTEAMTLADRIVI 208
Cdd:PRK11288 163 AFDEPTSSLSAR-------EIEQLFRVIrelraeGRVILYVSHRMEEIFALCDAITV 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-208 |
3.80e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 89.10 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 8 NIYKKYPnsehysveDFNLD-----IKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGEcsIDGTVvnnvapkdrDIAMV 82
Cdd:PRK13409 345 DLTKKLG--------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPEL---------KISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNmafglkLRK--------YSKEDIDKRvqeaaeiLGLKEFLDRKPADLSGGQRQRVAMGRAIVRDA 154
Cdd:PRK13409 406 PQYIKPDYDGTVEDL------LRSitddlgssYYKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 155 KVFLMDEPLSNLDaklrVSMRAEIAKIHRRI----GATTIYVTHDQTEAMTLADRIVI 208
Cdd:PRK13409 473 DLYLLDEPSAHLD----VEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLMV 526
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
4.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK----DRDI 79
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQ--NYALYPhMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVY 234
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE----------GRVILQGNPKEVF 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-237 |
7.36e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.04 E-value: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVV-----NNVAPKDrdIAMVFQNYALYPHMTVY 95
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpgHQIARMG--VVRTFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 96 DNMAF------------GL----KLRKYSKEDIDkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK11300 99 ENLLVaqhqqlktglfsGLlktpAFRRAESEALD-RAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSATKnPAGTGTigrveqigsPQEVYKNP 237
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT-PLANGT---------PEEIRNNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-210 |
1.15e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEfIV-FVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---RDIAMVFQN---YALYPHMT 93
Cdd:COG1129 268 VRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAFGLkLRKYSKEDIDKRVQEAAEILGLKEFLDRKPAD-------LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:COG1129 347 IRENITLAS-LDRLSRGGLLDRRRERALAEEYIKRLRIKTPSpeqpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 167 DaklrVSMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:COG1129 426 D----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMR 468
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-248 |
1.48e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN--NVAPKDRDIAMVFQN--YALYPHMTVY 95
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 96 DNMAFGLKLR-KYSKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVS 173
Cdd:PRK15112 108 QILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD----MS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 174 MRAEIA----KIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAGFIGS 248
Cdd:PRK15112 184 MRSQLInlmlELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ----------GEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-226 |
1.85e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.78 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIdgtvvnnvaPKDRDIAMVFQNyalyPHM---TVYDN 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQR----PYLplgTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 98 MAFGLKLRKYSkediDKRVQEAAEILGLKEFLDR--KPAD----LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:COG4178 446 LLYPATAEAFS----DAELREALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 172 VSMRAEIakIHRRIGATTIYVTHdQTEAMTLADRIVIMSatknPAGTGTIGRVEQ 226
Cdd:COG4178 522 AALYQLL--REELPGTTVISVGH-RSTLAAFHDRVLELT----GDGSWQLLPAEA 569
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-235 |
2.32e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 9 IYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNN------VAPKDRDIAMV 82
Cdd:PRK13646 11 TYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQnyalYPHMTVYDN-----MAFGLKLRKYSKEDIDKRVQEAAEILGL-KEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK13646 91 FQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 157 FLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSatknpagTGTIgrVEQiGSPQEVYK 235
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMK-------EGSI--VSQ-TSPKELFK 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-226 |
3.63e-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: 86.03 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYpHMTVYDNMAFGlklrkysKEDIDK 114
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYG-------RPDASE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 115 R-VQEAAEILGLKEFLDRKPaD------------LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKI 181
Cdd:COG5265 462 EeVEAAARAAQIHDFIESLP-DgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 182 HRriGATTIYVTH------DqteamtlADRIVIMSAtknpagtGTIgrVEQ 226
Cdd:COG5265 541 AR--GRTTLVIAHrlstivD-------ADEILVLEA-------GRI--VER 573
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-248 |
8.57e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL---EDITEGECSIDGTVVNNVAPKD------RDIAMVFQN--YAL 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 YPHMTVYDNMAFGLKLRK-YSK-----EDIdkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKgMSKaeafeESV--RMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 163 LSNLDaklrVSMRAEIA----KIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:PRK09473 189 TTALD----VTVQAQIMtllnELKREFNTAIIMITHDLGVVAGICDKVLVMYA----------GRTMEYGNARDVFYQPS 254
|
250
....*....|
gi 881073645 239 NKFVAGFIGS 248
Cdd:PRK09473 255 HPYSIGLLNA 264
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-277 |
2.38e-17 |
|
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: 84.29 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDG-TVVNNvapkdrdIAMV 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGkSILTN-------ISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFG-------LKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIM-----------SATKNPAGTGTIGRV 224
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMvkgafqclgtiQHLKSKFGDGYIVTM 2169
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 225 eQIGSPQEVY---KNPVNKFVAG-FIGSpamnfinVKLEGGYivtNGLNLKVPEGAL 277
Cdd:TIGR01257 2170 -KIKSPKDDLlpdLNPVEQFFQGnFPGS-------VQRERHY---NMLQFQVSSSSL 2215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-194 |
2.39e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.46 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 32 EFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK-DRDIAMVFQNYALYPHMTVYDNMAFglklrkYSKE 110
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRF------WHAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 111 DIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaKLRVSMRAEIAKIHRRIGATTI 190
Cdd:cd03231 101 HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVARFAEAMAGHCARGGMVV 179
|
....
gi 881073645 191 YVTH 194
Cdd:cd03231 180 LTTH 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-234 |
2.92e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 24 FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVN----NVAPKDRDIAMVFQNyalyPHMTVY---- 95
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIFytdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 96 -DNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK13638 96 dSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 175 RAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVY 234
Cdd:PRK13638 176 IAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQ----------GQILTHGAPGEVF 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-167 |
3.06e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPnsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnNVA--PKDRDiam 81
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV--KIGyfDQHQE--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 82 vfqnyALYPHMTVYDNMafglklRKYSKediDKRVQEAAEILGLkeFL------DRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:COG0488 389 -----ELDPDKTVLDEL------RDGAP---GGTEQEVRGYLGR--FLfsgddaFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170
....*....|..
gi 881073645 156 VFLMDEPLSNLD 167
Cdd:COG0488 453 VLLLDEPTNHLD 464
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-237 |
6.87e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTlrmIAGLEDI-------TEGECSIDGTVVNNVAPKDRDIAMVFQN--YALYPH 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLT---CAAALGIlpagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 92 MTVYDNMAFGLKLRkySKEDIDKRVQEAAEILGLKE---FLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:PRK10418 96 HTMHTHARETCLAL--GKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 169 KLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP 237
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH----------GRIVEQGDVETLFNAP 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-196 |
9.12e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 17 EHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDgtvvnnvapkdrdiamvFQNYALYPHMTVYD 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 97 NMafglklrkYSKEDIDkrvqEAAEIL---GLKE--FLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:COG2401 105 AI--------GRKGDFK----DAVELLnavGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....*
gi 881073645 172 VSMRAEIAKIHRRIGATTIYVTHDQ 196
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-212 |
1.65e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 18 HYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNvAPKDRDIAMVFQNYAL---YP---- 90
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYVPQSEEVdwsFPvlve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 ---HMTVYDNMAFglkLRKYSKEDiDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK15056 99 dvvMMGRYGHMGW---LRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 881073645 168 AKLRVSMRAEIAKIhRRIGATTIYVTHDQTEAMTLADRIVIMSAT 212
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGT 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-237 |
1.82e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK----------------DRDIAMVF 83
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQvielseqsaaqmrhvrGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QN--YALYPHMTVYDNMAFGLKLRK-YSKEDI---DKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQgASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 158 LMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP 237
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ----------GEAVETGSVEQIFHAP 260
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-209 |
1.89e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSVEDFNLdiKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAP---KDRDIA 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTL--HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKlrkySKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 161 EPLSNLDAklrvsmrAEIAKIHRRI------GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK15439 166 EPTASLTP-------AETERLFSRIrellaqGVGIVFISHKLPEIRQLADRISVM 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-208 |
1.97e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 5 NLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGE--------------CSIDGTVVN 70
Cdd:PRK13651 7 NIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktKEKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 71 NVAPKD------------RDIAMVFQ--NYALYpHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKE-FLDRKPAD 135
Cdd:PRK13651 87 LVIQKTrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 136 LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVI 208
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIF 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-168 |
2.43e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 13 YPNSEHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK--DRDIAMVFQNYALY 89
Cdd:TIGR00958 488 YPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 90 PHmTVYDNMAFGLklRKYSKEDIDKRVQEAAEILGLKEF-------LDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEP 162
Cdd:TIGR00958 568 SG-SVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFpngydteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
....*.
gi 881073645 163 LSNLDA 168
Cdd:TIGR00958 645 TSALDA 650
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-233 |
3.07e-16 |
|
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: 80.76 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 25 NLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnvapkdrdiAMVFQNyALYPHMTVYDNMAFGLKL 104
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 105 rkysKEDIDKRVQEAAEILGLKEFL---DR-----KPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL-RVSMR 175
Cdd:TIGR00957 726 ----NEKYYQQVLEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 176 AEIAKIHRRIGATTIYVTHDQTeAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:TIGR00957 802 HVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSG----------GKISEMGSYQEL 848
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-232 |
4.01e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 32 EFIVFVGPSGCGKSTTLRMIAGLediTEGECSIDGTVVNNVAPKDRDI-----AMVFQNYALYPHMTVYDNMAFGLKLR- 105
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGMPIDAKEmraisAYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 106 --KYSKEDIDKRVQEAAEILGLkefldRKPAD-----------LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklrv 172
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLQALGL-----RKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS---- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 173 SMRAEIAKIHRRI---GATTIYVTHDQT-EAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQE 232
Cdd:TIGR00955 200 FMAYSVVQVLKGLaqkGKTIICTIHQPSsELFELFDKIILMAE----------GRVAYLGSPDQ 253
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-233 |
8.18e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 24 FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiTEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNMAFG 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 102 LKlRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVR-------DAKVFLMDEPLSNLDAKLRVSM 174
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 175 RAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:COG4138 173 DRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQ----------GKLVASGETAEV 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-169 |
8.69e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvapKDRDiamVFQNYALY--------PHMT 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 94 VYDNMAFGLKLRKYSKEDidkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-275 |
1.01e-15 |
|
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: 78.31 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDI--TEG----------EC------SID 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGriiyhvalceKCgyverpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 66 GTVV----NNVAPKDRD---------------IAMVFQ-NYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGL 125
Cdd:TIGR03269 79 GEPCpvcgGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 126 KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD---AKLRVSMRAEIAKIHRrigaTTIYVTHDQTEAMT- 201
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAVKASG----ISMVLTSHWPEVIEd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 202 LADRIVIMSAtknpagtgtiGRVEQIGSPQEVyknpVNKFVAGF----------IGSPAMNFINVK-----LEGGYI-VT 265
Cdd:TIGR03269 235 LSDKAIWLEN----------GEIKEEGTPDEV----VAVFMEGVsevekeceveVGEPIIKVRNVSkryisVDRGVVkAV 300
|
330
....*....|
gi 881073645 266 NGLNLKVPEG 275
Cdd:TIGR03269 301 DNVSLEVKEG 310
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-247 |
1.47e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 36 FVGPSGCGKSTTLRMIAGLEDITEG-----ECSIDGTVVNN---VAPKDRDIAMVFQNYALYPhMTVYDNMAFGLKL--- 104
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNyrdVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAhkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 105 --RKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIH 182
Cdd:PRK14271 131 vpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 183 RRIgaTTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNP----VNKFVAGFIG 247
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFD----------GRLVEEGPTEQLFSSPkhaeTARYVAGLSG 267
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
247-299 |
1.56e-15 |
|
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: 69.92 E-value: 1.56e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 881073645 247 GSPAMNFINVKLEGGYIVTNGLNLKVPEGALKVLKEKGYDGKELIFGIRPEDV 299
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGGVTLPLPEGQVLALKLYVGKEVILGIRPEHI 53
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-208 |
2.52e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL--EDITEGECSIDGTVVnnVAPKDRD--- 78
Cdd:PRK13549 6 LEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEEL--QASNIRDter 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 --IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEIL-GLKefLDRKPA----DLSGGQRQRVAMGRAIV 151
Cdd:PRK13549 82 agIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaQLK--LDINPAtpvgNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 152 RDAKVFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRI-VI 208
Cdd:PRK13549 160 KQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTIcVI 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-196 |
2.59e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.72 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIykkypnseHYSVED------FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ITEGECSIDGTVVNNVAPK 75
Cdd:COG0396 1 LEIKNL--------HVSVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 76 DR---DIAMVFQNYALYPHMTVYD--NMAFGLKLRK-YSKEDIDKRVQEAAEILGL-KEFLDRkPAD--LSGGQRQRVAM 146
Cdd:COG0396 73 ERaraGIFLAFQYPVEIPGVSVSNflRTALNARRGEeLSAREFLKLLKEKMKELGLdEDFLDR-YVNegFSGGEKKRNEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 881073645 147 GRAIVRDAKVFLMDEPLSNLDA-KLRVsMRAEIAKIHRRiGATTIYVTHDQ 196
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQ 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-209 |
2.95e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.08 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK---DRDIAMV 82
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 FQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEI---LGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-210 |
5.18e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDikDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNvAPKDRDIAMVFQNYALYPHMTVYDNMAFGL 102
Cdd:PRK13543 31 DFHVD--AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSRFMAYLGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 103 KLRKYSKEDIDKrvqEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlRVSMRAEIAKIH 182
Cdd:PRK13543 108 GLHGRRAKQMPG---SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAH 183
|
170 180
....*....|....*....|....*...
gi 881073645 183 RRIGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK13543 184 LRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-205 |
5.25e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNIykkypnSEHY----SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNvAPKD 76
Cdd:PRK11614 3 KVMLSFDKV------SAHYgkiqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 R----DIAMVFQNYALYPHMTVYDNMAFGLKLRkySKEDIDKRVQEAAEILG-LKEFLDRKPADLSGGQRQRVAMGRAIV 151
Cdd:PRK11614 76 KimreAVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 152 RDAKVFLMDEPLSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHDQTEAMTLADR 205
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADR 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-253 |
6.60e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 73.94 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAG--------LEDITEGECSID---GTVVNN----VAPKDRDIAMVFQNYALYPhmtvydNMAFG 101
Cdd:cd03236 32 VGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDefrGSELQNyftkLLEGDVKVIVKPQYVDLIP------KAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 102 LKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMraeiAKI 181
Cdd:cd03236 106 KVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA----ARL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 182 HRRI---GATTIYVTHDQTEAMTLADRIVIMSATknPAGTGTigrveqIGSPQEVyKNPVNKFVAGFIGSPAMNF 253
Cdd:cd03236 182 IRELaedDNYVLVVEHDLAVLDYLSDYIHCLYGE--PGAYGV------VTLPKSV-REGINEFLDGYLPTENMRF 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-238 |
8.38e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.22 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 60 GECSIDGTVVNNVAPKD-RDIAMVFQNYALYPHMTVYDNMAFGlklrkysKEDIDKR-VQEAAEILGLKEFLDRKP---- 133
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATREdVKRACKFAAIDEFIESLPnkyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 134 -------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHdQTEAMTLADRI 206
Cdd:PTZ00265 1350 tnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKI 1428
|
170 180 190
....*....|....*....|....*....|....*..
gi 881073645 207 VIMSatkNPAGTGTI----GRVEQIGSPQE-VYKNPV 238
Cdd:PTZ00265 1429 VVFN---NPDRTGSFvqahGTHEELLSVQDgVYKKYV 1462
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-210 |
1.16e-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: 71.91 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 1 MVELNLKNI--YKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGledITEGECSIDGTVV-NNVAPKD- 76
Cdd:cd03233 1 ASTLSWRNIsfTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHyNGIPYKEf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 77 -----RDIAMVFQNYALYPHMTVYDNMAFGLKLRKyskedidkrvqeaaeilglKEFLdRKpadLSGGQRQRVAMGRAIV 151
Cdd:cd03233 78 aekypGEIIYVSEEDVHFPTLTVRETLDFALRCKG-------------------NEFV-RG---ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 152 RDAKVFLMDEPLSNLDaklrvSMRA-EIAKIHR---RIGATTIYVTHDQT--EAMTLADRIVIMS 210
Cdd:cd03233 135 SRASVLCWDNSTRGLD-----SSTAlEILKCIRtmaDVLKTTTFVSLYQAsdEIYDLFDKVLVLY 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-228 |
1.85e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEfIVFV-GPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRDIAMVF------QNYALYPHMT 93
Cdd:COG3845 274 LKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAfglkLRKYSKED------ID-KRVQEAAEILgLKEFlDRKPAD-------LSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:COG3845 353 VAENLI----LGRYRRPPfsrggfLDrKAIRAFAEEL-IEEF-DVRTPGpdtparsLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 160 DEPLSNLDAklrvsmrAEIAKIHRRI------GATTIYVTHDQTEAMTLADRIVIM-----SATKNPAGTgtigRVEQIG 228
Cdd:COG3845 427 AQPTRGLDV-------GAIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMyegriVGEVPAAEA----TREEIG 495
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-237 |
2.09e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.24 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 19 YSVEDfnldikdKEFIVFVGPSGCGKSTTLRMIAGLED----ITEGECSIDGTVVNNVAPKDR------DIAMVFQN--Y 86
Cdd:PRK11022 28 YSVKQ-------GEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 87 ALYPHMTVYDNMAFGLKLRKYSKEDidKRVQEAAEILGL------KEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMD 160
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGGNKK--TRRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 161 EPLSNLDaklrVSMRAEIA----KIHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:PRK11022 179 EPTTALD----VTIQAQIIelllELQQKENMALVLITHDLALVAEAAHKIIVMYA----------GQVVETGKAHDIFRA 244
|
.
gi 881073645 237 P 237
Cdd:PRK11022 245 P 245
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-194 |
3.39e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 70.67 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 15 NSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKdrDIAMVFQNYALYPHMTV 94
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFGLKLrkYSKEDIdkrVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSM 174
Cdd:PRK13541 88 FENLKFWSEI--YNSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|
gi 881073645 175 RAEIAkIHRRIGATTIYVTH 194
Cdd:PRK13541 163 NNLIV-MKANSGGIVLLSSH 181
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-237 |
3.41e-14 |
|
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: 71.79 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSveDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSI---DGTVVN--NVAPKDR- 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCR--DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELElyQLSEAERr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 78 -----DIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEF----LDRKPADLSGGQRQRVAMGR 148
Cdd:TIGR02323 82 rlmrtEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdptrIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 149 AIVRDAKVFLMDEPLSNLDaklrVSMRAEIAKIHRRI----GATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRV 224
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLD----VSVQARLLDLLRGLvrdlGLAVIIVTHDLGVARLLAQRLLVMQQ----------GRV 227
|
250
....*....|...
gi 881073645 225 EQIGSPQEVYKNP 237
Cdd:TIGR02323 228 VESGLTDQVLDDP 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
3.48e-14 |
|
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: 69.01 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNseHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnvapkdrdiamvf 83
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 qNYALYPHmtvydnmafglklrkyskedidkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:cd03221 64 -KIGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRrigaTTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
38-194 |
4.11e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 38 GPSGCGKSTTLRMIAGLEDITEGECSIDG-TVVNNVAPKDRDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEdidkrV 116
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERqSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVG-----I 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 117 QEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKlrvSMRAEIAKI--HRRIGATTIYVTH 194
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL---SLLTIITKIqeHRAKGGAVLLTSH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-209 |
4.63e-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: 73.28 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAG-----LEDItEGECSIDgtvvnnvapkdrDIAMVFQNYALYPHMT-VYDNmafGLK------- 103
Cdd:COG1245 105 LGPNGIGKSTALKILSGelkpnLGDY-DEEPSWD------------EVLKRFRGTELQDYFKkLANG---EIKvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 104 ---LRKYSK-------EDIDKR--VQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:COG1245 169 vdlIPKVFKgtvrellEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 881073645 172 VSMraeiAKIHRRI---GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:COG1245 249 LNV----ARLIRELaeeGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-210 |
5.08e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 14 PNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLR-MIAGLEDITEGECSIDGTVvnnvapkdrdiAMVFQNYALYpHM 92
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 93 TVYDNMAFGLKLRKyskedidKRVQEAAEILGLKEFLDRKPA-----------DLSGGQRQRVAMGRAIVRDAKVFLMDE 161
Cdd:PLN03130 694 TVRDNILFGSPFDP-------ERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 162 PLSNLDAklRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PLN03130 767 PLSALDA--HVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVH 813
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-210 |
5.76e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---RDIAMVFQNY---ALYPHMTV 94
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFG--LKLRKY-------SKEDIDKRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK09700 359 AQNMAISrsLKDGGYkgamglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 165 NLDaklrVSMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK09700 439 GID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFC 483
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-230 |
5.91e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.13 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKY-PNSEHySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDI 79
Cdd:cd03369 6 EIEVENLSVRYaPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYPHmTVYDNM-AFGlklrKYSKEDIDK--RVQEAAEilglkefldrkpaDLSGGQRQRVAMGRAIVRDAKV 156
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLdPFD----EYSDEEIYGalRVSEGGL-------------NLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 157 FLMDEPLSNLDaklrVSMRAEIAK-IHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSP 230
Cdd:cd03369 147 LVLDEATASID----YATDALIQKtIREEFTNSTILTIAHRLRTIIDYDKILVMDA----------GEVKEYDHP 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-209 |
6.61e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPK--DRDIAMVFQNYALYPHmTVYDNMA 99
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 100 FGlklRKYSKEdidkRVQEAAEILGLKEFLDRKPA-----------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:PRK10790 437 LG---RDISEE----QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 881073645 169 KLRVSMRAEIAKIHRRigaTTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10790 510 GTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVL 547
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-209 |
7.19e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.82 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 13 YPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYP 90
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 91 HmTVYDNMAFGLKlrKYSKEDIDKRVQEAA---EILGLKEFLDRKPAD----LSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:PRK10789 403 D-TVANNIALGRP--DATQQEIEHVARLASvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 164 SNLDAKlrvsMRAEIAKIHRRIGAT-TIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10789 480 SAVDGR----TEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVM 522
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-267 |
8.28e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSV-EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSI-DGTVVNNVAPK--DRD 78
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHmTVYDNMAFGL-------KLRKYSKED-------IDKRVQEAAEILG-------------------- 124
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdleALSNYYNEDgndsqenKNKRNSCRAKCAGdlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 125 -----------------LKEFLDRKP-----------ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRA 176
Cdd:PTZ00265 541 yqtikdsevvdvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 177 EIAKIHRRIGATTIYVTHdQTEAMTLADRIVIMSATKNPAGTGTIGRVEQIGSPQEVYKNPVNKFVAGFIGSPAMNFINV 256
Cdd:PTZ00265 621 TINNLKGNENRITIIIAH-RLSTIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINN 699
|
330
....*....|.
gi 881073645 257 klEGGYIVTNG 267
Cdd:PTZ00265 700 --AGSYIIEQG 708
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-244 |
1.85e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSidgtvvnnvapKDRDIAMVFQNyALYPHMTVYDNMAFgl 102
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF-- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 103 klrkYSKEDiDKRVQEAAEIL-----------GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKL- 170
Cdd:PTZ00243 744 ----FDEED-AARLADAVRVSqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 171 -RVSMRAEIAKIHrriGATTIYVTHdQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKFVAG 244
Cdd:PTZ00243 819 eRVVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGD----------GRVEFSGSSADFMRTSLYATLAA 879
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-215 |
2.44e-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: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIdgtvvnnvaPKDRDIAMVFQNyalyPHMTvydnmaf 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 glklrkyskedidkrvqeaaeiLG-LKEFLdRKPAD--LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAE 177
Cdd:cd03223 77 ----------------------LGtLREQL-IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 881073645 178 IAKIHRRIGATTIYVTHdQTEAMTLADRIVIMSATKNP 215
Cdd:cd03223 130 LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEGGW 166
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-245 |
2.62e-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: 67.60 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 27 DIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvapkdrdiamvfqnyalyphmtvydnmafglklrk 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 107 YSKEDIDkrvqeaaeilglkefldrkpadLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRIG 186
Cdd:cd03222 65 YKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 187 ATTIYVTHDQTEAMTLADRIVIMSATKNPAGTgtigrveqiGSPQEVYKNPVNKFVAGF 245
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEGEPGVYGI---------ASQPKGTREGINRFLRGY 172
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-236 |
3.24e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLR-MIAGLEDITEGECSIDGTVVnnVAPKdrdIAMVFqnyalypHMTVYDNM 98
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVA--YVPQ---VSWIF-------NATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFGlklRKYSKEdidkRVQEAAEILGLKEFLDRKPA-----------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PLN03232 700 LFG---SDFESE----RYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 168 AKLRVSMRAEIAKiHRRIGATTIYVThDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:PLN03232 773 AHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSE----------GMIKEEGTFAELSKS 829
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-209 |
4.59e-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: 67.74 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 20 SVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD------IAMVFQNYALYpHMT 93
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 VYDNMAFGLKLRKYS-KEDIDK-RVQEAAEIL--GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK 169
Cdd:cd03290 95 VEENITFGSPFNKQRyKAVTDAcSLQPDIDLLpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 881073645 170 LRVS-MRAEIAKIHRRIGATTIYVTHdQTEAMTLADRIVIM 209
Cdd:cd03290 175 LSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAM 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-209 |
5.52e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSI---DGTVVNNVA---PKDR-----DIAMVFQNYA--L 88
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlseAERRrllrtEWGFVHQHPRdgL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 89 YPHMTVYDN-----MAFGLklRKYSkeDIdkRvQEAAEILGLKEF----LDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK11701 103 RMQVSAGGNigerlMAVGA--RHYG--DI--R-ATAGDWLERVEIdaarIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 160 DEPLSNLDaklrVSMRAEIAKIHRRI----GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK11701 176 DEPTGGLD----VSVQARLLDLLRGLvrelGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-209 |
5.65e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAG-----LEDiTEGECSIDgTVVnnvapkDRdiamvFQNYALYPHMT-VYDNmafGLK------- 103
Cdd:PRK13409 105 LGPNGIGKTTAVKILSGelipnLGD-YEEEPSWD-EVL------KR-----FRGTELQNYFKkLYNG---EIKvvhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 104 ---LRKYSK-------EDIDKR--VQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLR 171
Cdd:PRK13409 169 vdlIPKVFKgkvrellKKVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 881073645 172 VSMraeiAKIHRRI--GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK13409 249 LNV----ARLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-211 |
6.75e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 28 IKDKEFIVFVGPSGCGKSTTLRMIAGLED----ITEGECSIDGTVVNNVAPKDR-DIAMVFQNYALYPHMTVYDNMAFGL 102
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 103 KLRK-------YSKEDIDKRVQE-AAEILGLKEFLDRKPAD-----LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAk 169
Cdd:TIGR00956 164 RCKTpqnrpdgVSREEYAKHIADvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS- 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 881073645 170 lrvSMRAEIAKIHR---RIGATTIYVTHDQT--EAMTLADRIVIMSA 211
Cdd:TIGR00956 243 ---ATALEFIRALKtsaNILDTTPLVAIYQCsqDAYELFDKVIVLYE 286
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-209 |
1.22e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.57 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnnvapkdrdIAMVFQNYALYPHmTVYDNMAF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 GLKLRKYSKEDIDKRVQEAAEILGLKE----FLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRA 176
Cdd:cd03291 121 GVSYDEYRYKSVVKACQLEEDITKFPEkdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD----VFTEK 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 881073645 177 EIAK---IHRRIGATTIYVThDQTEAMTLADRIVIM 209
Cdd:cd03291 197 EIFEscvCKLMANKTRILVT-SKMEHLKKADKILIL 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-210 |
1.35e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 22 EDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---RDIAMVFQNY---ALYPHMTVY 95
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 96 DNMA---------FGLKL-RKYSKEDIDKRVQEaaeiLGLKE-FLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK11288 350 DNINisarrhhlrAGCLInNRWEAENADRFIRS----LNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 881073645 165 NLDaklrVSMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK11288 426 GID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMR 470
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-238 |
2.22e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 24 FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiTEGECSIDGTVV-----------------NNVAPkdrdIAM-VFQN 85
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawsaaelarhraylsqQQTPP----FAMpVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 86 YALYPHmtvydnmafglklRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVR-------DAKVFL 158
Cdd:PRK03695 90 LTLHQP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 159 MDEPLSNLDAKLRVSMRAEIAKIHRRiGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPV 238
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQ----------GKLLASGRRDEVLTPEN 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-207 |
1.04e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 26 LDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAmvfqnyalyphMTVYDNMAFGLK 103
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNVE-----------GTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 104 -----LRKYS---------------------KEDID--------KRVQEAAEILGLKEflDRKPADLSGGQRQRVAMGRA 149
Cdd:PRK11147 93 eqaeyLKRYHdishlvetdpseknlnelaklQEQLDhhnlwqleNRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073645 150 IVRDAKVFLMDEPLSNLDaklrvsmraeIAKIH------RRIGATTIYVTHDQTEAMTLADRIV 207
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLD----------IETIEwlegflKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-211 |
1.11e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNsEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:PRK10522 322 TLELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMtvydnmafglkLRKYSKEDIDKRVQEAAEILGLK---EFLDRKPAD--LSGGQRQRVAMGRAIVRDAK 155
Cdd:PRK10522 401 AVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 156 VFLMDEPLSNLDAKLRVSMRAEIAKIHRRIGATTIYVTHDQtEAMTLADRIVIMSA 211
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRN 524
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-168 |
1.19e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 32 EFIVFVGPSGCGKSTTLRMIAGLediTEGECSIDGTVVNNVAPKD---RDIAMVFQNYALYPHMTVYDNMAFG--LKLRK 106
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 107 YSKEDIDKRVQEA--AEiLGLKEFLDRKPAD-----LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDA 168
Cdd:PLN03211 172 SLTKQEKILVAESviSE-LGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-209 |
1.29e-11 |
|
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: 66.47 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTvvnnvapkdrdIAMVFQNYALYPHmTVYDNMAF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 GLKLRKYSKEDIDKRVQEAAEILGLKEfLDRKP-----ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMR 175
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQLEEDIALFPE-KDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VVTE 584
|
170 180 190
....*....|....*....|....*....|....*..
gi 881073645 176 AEIAK---IHRRIGATTIYVThDQTEAMTLADRIVIM 209
Cdd:TIGR01271 585 KEIFEsclCKLMSNKTRILVT-SKLEHLKKADKILLL 620
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-209 |
2.73e-11 |
|
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: 64.85 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL--EDITEGECSIDGT--VVNNVAPKDRD- 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSplKASNIRDTERAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFG----LKLRKYSKEDIDKRVQEAAEILGLKEFLDRKP-ADLSGGQRQRVAMGRAIVRD 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 154 AKVFLMDEPLSNLDAKlRVSMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-209 |
2.76e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD---RDIAMVFQNY---ALYPHMTV 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 95 YDNMAFgLKLRKYSKEDIdkRVQEAAEILGLKEFLD----RKPA------DLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK10762 348 KENMSL-TALRYFSRAGG--SLKHADEQQAVSDFIRlfniKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 881073645 165 NLDaklrVSMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10762 425 GVD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-196 |
2.79e-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: 62.16 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 18 HYSVED------FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ITEGECSIDGTVVNNVAPKDRDIAMVFqnyaly 89
Cdd:cd03217 7 HVSVGGkeilkgVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIF------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 90 phmtvydnMAFglklrkyskedidkrvQEAAEILGLK--EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:cd03217 81 --------LAF----------------QYPPEIPGVKnaDFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190
....*....|....*....|....*....|.
gi 881073645 168 AklrVSMR--AEIAKIHRRIGATTIYVTHDQ 196
Cdd:cd03217 137 I---DALRlvAEVINKLREEGKSVLIITHYQ 164
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-167 |
1.49e-10 |
|
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: 62.65 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnvapkdrDIAMVFQNY-ALYPHMTVYDNMAFGLKLRKYSKEDIDKR 115
Cdd:TIGR03719 354 IGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSR 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 116 VqeaaeILGLKEFL----DRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:TIGR03719 425 A-----YVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-209 |
3.32e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTT----LRMIAGLEDI-TEGECSIDG-TVVNNVAPKDR-----DIAMVFQN--YA 87
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGeSLLHASEQTLRgvrgnKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 88 LYPHMTVYDNMAFGLKLRKYSKedidkrvQEAA--EILGLkefLDRK------------PADLSGGQRQRVAMGRAIVRD 153
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSLHRGMR-------REAArgEILNC---LDRVgirqaakrltdyPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 154 AKVFLMDEPLSNLDaklrVSMRAEI----AKIHRRIGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK15134 175 PELLIADEPTTALD----VSVQAQIlqllRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-207 |
5.93e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGecsidgTVVNNVAPKdrdIAMVFQNYALYPHM--TVYDNMAF 100
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------VIKRNGKLR---IGYVPQKLYLDTTLplTVNRFLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 101 --GLKlrkysKEDID---KRVQEAaeilglkEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 175
Cdd:PRK09544 93 rpGTK-----KEDILpalKRVQAG-------HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190
....*....|....*....|....*....|..
gi 881073645 176 AEIAKIHRRIGATTIYVTHDQTEAMTLADRIV 207
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-167 |
8.31e-10 |
|
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: 60.69 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiTEGECSIDGTVVNNVAPKDRDIAmv 82
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 fqnYALYPHMTVYDNMAFGLKLRKYSKEDiDKRVQEAAEILGLKEFLDRKPADL-----------SGGQRQRVAMGRAIV 151
Cdd:TIGR01271 1294 ---FGVIPQKVFIFSGTFRKNLDPYEQWS-DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369
|
170
....*....|....*.
gi 881073645 152 RDAKVFLMDEPLSNLD 167
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLD 1385
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-213 |
1.03e-09 |
|
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: 58.71 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDiTEGECSIDGTVVNNVAPKDRDIAmv 82
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 83 fqnYALYPHMTVYDNMAFGLKLRKYSKEDiDKRVQEAAEILGLKEFLDRKPADL-----------SGGQRQRVAMGRAIV 151
Cdd:cd03289 79 ---FGVIPQKVFIFSGTFRKNLDPYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 881073645 152 RDAKVFLMDEPLSNLDAklrVSMRAeIAKIHRRIGAT-TIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:cd03289 155 SKAKILLLDEPSAHLDP---ITYQV-IRKTLKQAFADcTVILSEHRIEAMLECQRFLVIEENK 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
37-241 |
1.07e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHMTVYDNMAFglklrkysKEDIDK 114
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGTVRFNIDPF--------SEHNDA 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 115 RVQEAAEILGLKEFLDRKPADL-----------SGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAK-IH 182
Cdd:PLN03232 1340 DLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQRtIR 1415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 183 RRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKF 241
Cdd:PLN03232 1416 EEFKSCTMLVIAHRLNTIIDCDKILVLSS----------GQVLEYDSPQELLSRDTSAF 1464
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-233 |
1.38e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKD--RDIA 80
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGlklrKYSKEDidkrVQEAAEILGLKEFLDRKPA-----------DLSGGQRQRVAMGRA 149
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDPFS----QYSDEE----VWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 150 IVRDAKVFLMDEPLSNLDAKLRVSMRAeiakihrrigatTIYVTHDQTEAMTLADRI-VIMSATKnpAGTGTIGRVEQIG 228
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQS------------TIRTQFEDCTVLTIAHRLnTIMDYTR--VIVLDKGEVAEFG 1501
|
....*
gi 881073645 229 SPQEV 233
Cdd:TIGR00957 1502 APSNL 1506
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-211 |
1.52e-09 |
|
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: 59.43 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPN---SEHYSVEDFNLDIKDKEfIVF-VGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNnvaPKDRD 78
Cdd:COG4615 327 TLELRGVTYRYPGedgDEGFTLGPIDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 -----IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKE-DIDKRVQEAAEilglkEFLDRkpaDLSGGQRQRVAMGRAIVR 152
Cdd:COG4615 403 ayrqlFSAVFSDFHLFDRLLGLDGEADPARARELLERlELDHKVSVEDG-----RFSTT---DLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 153 DAKVFLMDE------P----------LSNLdaklrvsmraeiakihRRIGATTIYVTHDQTeAMTLADRIVIMSA 211
Cdd:COG4615 475 DRPILVFDEwaadqdPefrrvfytelLPEL----------------KARGKTVIAISHDDR-YFDLADRVLKMDY 532
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-209 |
3.07e-09 |
|
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: 56.10 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLED--ITEGECSIDGTvvnnvaPKD----RDIAMVFQNYALYPHMTVYDNMAFGLKLRkyske 110
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTagVITGEILINGR------PLDknfqRSTGYVEQQDVHSPNLTVREALRFSALLR----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 111 didkrvqeaaeilglkefldrkpaDLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAklrvSMRAEIAKIHRRIGAT-- 188
Cdd:cd03232 108 ------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVRFLKKLADSgq 159
|
170 180
....*....|....*....|...
gi 881073645 189 TIYVTHDQTEAMTLA--DRIVIM 209
Cdd:cd03232 160 AILCTIHQPSASIFEkfDRLLLL 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-195 |
3.90e-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: 58.02 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 34 IVFVGPSGCGKSTTLRMIAGLEDITEGECsidgtvvnnVAPKDRDIAMVFQNYALYPHMTVYDNMAFGLK---------- 103
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAeikdaldrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 104 --LRKYSKED------------------------IDKRVQEAAEILGLKEFlDRKPADLSGGQRQRVAMGRAIVRDAKVF 157
Cdd:TIGR03719 105 eiSAKYAEPDadfdklaaeqaelqeiidaadawdLDSQLEIAMDALRCPPW-DADVTKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 881073645 158 LMDEPLSNLDAKlrvSMrAEIAKIHRRIGATTIYVTHD 195
Cdd:TIGR03719 184 LLDEPTNHLDAE---SV-AWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-209 |
6.12e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDRD---IA 80
Cdd:PRK10762 5 LQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 81 MVFQNYALYPHMTVYDNMAFGLKLR-KYSKEDIDKRVQEAAEIL---GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKV 156
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKLLarlNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 157 FLMDEPLSNL-----DAKLRV--SMRAEiakihrriGATTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK10762 163 IIMDEPTDALtdtetESLFRVirELKSQ--------GRGIVYISHRLKEIFEICDDVTVF 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-209 |
8.71e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYS-VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGL-EDITEGECSIDGTVVNNVAPKD---RD 78
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQN---YALYPHMTVYDNMAFGLkLRKYSKEdidKRVQEAAEI---------LGLKEFLDRKP-ADLSGGQRQRVA 145
Cdd:TIGR02633 338 IAMVPEDrkrHGIVPILGVGKNITLSV-LKSFCFK---MRIDAAAELqiigsaiqrLKVKTASPFLPiGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 146 MGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAKIHRRI---GATTIYVTHDQTEAMTLADRIVIM 209
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVD----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-167 |
8.92e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 34 IVFV-GPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnvapkdrDIAMVFQNY-ALYPHMTVYDNMAFGLKLRKYSKED 111
Cdd:PRK11819 352 IVGIiGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNRE 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 881073645 112 IDKRVQEAAeiLGLKEFLDRKPA-DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK11819 423 IPSRAYVGR--FNFKGGDQQKKVgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-167 |
9.63e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIdGTVVnnvapkdrDIAMvFQNY--ALYPHMTVYDNM 98
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL--------EVAY-FDQHraELDPEKTVMDNL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFGlklrkysKEDID----KRvqeaaEILG-LKEFL-----DRKPAD-LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK11147 405 AEG-------KQEVMvngrPR-----HVLGyLQDFLfhpkrAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-194 |
1.46e-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: 56.30 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIdgtvvnnvaPKDRDIAMVFQNyalyPHMT------- 93
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTlgtlrdq 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 -VYDNMAFGLKLRKYSKEDIDKRVQEaaeiLGLKEFLDRKP-----AD----LSGGQRQRVAMGRAIVRDAKVFLMDEPL 163
Cdd:TIGR00954 535 iIYPDSSEDMKRRGLSDKDLEQILDN----VQLTHILEREGgwsavQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 881073645 164 SnldaKLRVSMRAEIAKIHRRIGATTIYVTH 194
Cdd:TIGR00954 611 S----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-233 |
1.68e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 36 FVGPSGCGKSTTLRMIAGLEDITEGECSI------DGTVVNNVAPKdrdIAMVFQ----NyaLYPHMTVYDNMAFGLKLR 105
Cdd:NF033858 32 LIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRRAVCPR---IAYMPQglgkN--LYPTLSVFENLDFFGRLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 106 KYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDE------PLSnldaklrvsmRAE-- 177
Cdd:NF033858 107 GQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEpttgvdPLS----------RRQfw 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 881073645 178 --IAKI-HRRIGATTIYVTHDQTEAMTLaDRIVIMSAtknpagtgtiGRVEQIGSPQEV 233
Cdd:NF033858 177 elIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDA----------GRVLATGTPAEL 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-167 |
2.53e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 21 VEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLE--DITEGECSIDGTVVNNVAPKDRD---IAMVFQNYALYPHMTVY 95
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 96 D--NMAFGLKLRKYSKEDID-----KRVQEAAEILGLKE-FLDRKPAD-LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNL 166
Cdd:CHL00131 103 DflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
.
gi 881073645 167 D 167
Cdd:CHL00131 183 D 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-209 |
1.14e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 23 DFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDR-DIAMVF-----QNYALYPHMT--- 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPlaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 94 -----VYDNMAFGLKLRKYSKedidkRVQEAAEILGLK-EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK15439 361 nvcalTHNRRGFWIKPARENA-----VLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 881073645 168 aklrVSMRAEIAKIHRRIGA---TTIYVTHDQTEAMTLADRIVIM 209
Cdd:PRK15439 436 ----VSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
1.38e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEHYSveDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGleDITEGECSIDGTVVNNVAPKDRDIAMVF 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFK--NLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEPDSGTVKWSENANIGYYAQDHAYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 84 QNyalypHMTVYDNMAfglklrKYSKEDIDKRVQEAaeILGLKEF----LDRKPADLSGGQRQRVAMGRAIVRDAKVFLM 159
Cdd:PRK15064 396 EN-----DLTLFDWMS------QWRQEGDDEQAVRG--TLGRLLFsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 160 DEPLSNLDAKLRVSMRAEIAKIHrrigATTIYVTHDQTEAMTLADRIVIMSATK 213
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKYE----GTLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-208 |
1.58e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 4 LNLKNIYKKYPNSEhySVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDIT--EGECSIDGTVVNNVAPKD---RD 78
Cdd:NF040905 2 LEMRGITKTFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDseaLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 79 IAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEIL---GLKEFLDRKPADLSGGQRQRVAMGRAIVRDAK 155
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLakvGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 156 VFLMDEPLSNLDAK-------LRVSMRAEiakihrriGATTIYVTHDQTEAMTLADRIVI 208
Cdd:NF040905 160 LLILDEPTAALNEEdsaalldLLLELKAQ--------GITSIIISHKLNEIRRVADSITV 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-206 |
1.63e-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: 50.06 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 31 KEFIVFVGPSGCGKSTTLRMIAGLEDITEGEC-SIDGTvvnnvapkdrdiamvfqnyalyphmtvydnmafglklrkysk 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 110 edidkRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEI-----AKIHRR 184
Cdd:smart00382 40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSE 114
|
170 180
....*....|....*....|..
gi 881073645 185 IGATTIYVTHDQTEAMTLADRI 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
59-209 |
1.77e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 59 EGECSIDGTVVNNVAPKD---RDIAMVFQN---YALYPHMTVYDNMAFGLkLRKYSKEdidKRVQEAAEILGLKEFLDR- 131
Cdd:PRK13549 317 EGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITLAA-LDRFTGG---SRIDDAAELKTILESIQRl 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 132 ---------KPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMRAEIAKIHRRI---GATTIYVTHDQTEA 199
Cdd:PRK13549 393 kvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPEV 468
|
170
....*....|
gi 881073645 200 MTLADRIVIM 209
Cdd:PRK13549 469 LGLSDRVLVM 478
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-195 |
1.85e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 2 VELNLKNIYKKY------------------PNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECS 63
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipkhKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 64 IDGtvvnnvapkdrDIAMVFQNYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQR 143
Cdd:PRK13546 83 RNG-----------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 881073645 144 VAMGRAIVRDAKVFLMDEPLSNLDAKLrvsMRAEIAKIH--RRIGATTIYVTHD 195
Cdd:PRK13546 152 LGFSINITVNPDILVIDEALSVGDQTF---AQKCLDKIYefKEQNKTIFFVSHN 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-241 |
2.15e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 28 IKDKEFIVFVGPSGCGKSTTL----RMIagleDITEGECSIDGTVVNNVAPKD--RDIAMVFQNYALYPHmTVYDNM--- 98
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVdpf 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 -------------AFGLKLRKYSK-EDIDKRVQEAAeilglkefldrkpADLSGGQRQRVAMGRAIV-RDAKVFLMDEPL 163
Cdd:PTZ00243 1408 leassaevwaaleLVGLRERVASEsEGIDSRVLEGG-------------SNYSVGQRQLMCMARALLkKGSGFILMDEAT 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 164 SNLDAKLRVSMRAEIAKIHRriGATTIYVTHdqtEAMTLA--DRIVIMSAtknpagtgtiGRVEQIGSPQEVYKNPVNKF 241
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFS--AYTVITIAH---RLHTVAqyDKIIVMDH----------GAVAEMGSPRELVMNRQSIF 1539
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
108-209 |
2.44e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 108 SKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAEIAKIHRRiGA 187
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100
....*....|....*....|..
gi 881073645 188 TTIYVTHDQTEAMTLADRIVIM 209
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVI 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-167 |
7.38e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 18 HYSVED------FNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLED--ITEGECSIDGTVVNNVAPKDR---DIAMVFQny 86
Cdd:PRK09580 8 HVSVEDkailrgLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 87 alYPHMTVYDNMAFGLK-----LRKYskedidkRVQEAAEILGLKEFLDRK------PADL---------SGGQRQRVAM 146
Cdd:PRK09580 86 --YPVEIPGVSNQFFLQtalnaVRSY-------RGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDI 156
|
170 180
....*....|....*....|.
gi 881073645 147 GRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-168 |
7.79e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLEDITEGEC------SI-----------DGTVVNNV--------APKDR--DIAMvfqNYAly 89
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEGEArpapgiKVgylpqepqldpEKTVRENVeegvaevkAALDRfnEIYA---AYA-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 90 phmtvyDNMAFGLKLRKYSKE-----------DIDKRVQEAAEILGLKEFlDRKPADLSGGQRQRVAMGRAIVRDAKVFL 158
Cdd:PRK11819 114 ------EPDADFDALAAEQGElqeiidaadawDLDSQLEIAMDALRCPPW-DAKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
170
....*....|
gi 881073645 159 MDEPLSNLDA 168
Cdd:PRK11819 187 LDEPTNHLDA 196
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-167 |
1.04e-06 |
|
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: 49.52 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIYKKYPNSEHYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNV---APKDRdI 79
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 80 AMVFQNYALYPhmtvyDNMAFGLKLRKYSKEDidkRVQEAAEILGLKEFLDRKPADL-----------SGGQRQRVAMGR 148
Cdd:cd03288 98 SIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169
|
170
....*....|....*....
gi 881073645 149 AIVRDAKVFLMDEPLSNLD 167
Cdd:cd03288 170 AFVRKSSILIMDEATASID 188
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
3-209 |
1.29e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 3 ELNLKNIykkypnsehysvedfNLDIKDKEFIVFVGPSGCGKST----TL------RMIAGLED-ITEGECSIDGTVVNN 71
Cdd:cd03270 8 EHNLKNV---------------DVDIPRNKLVVITGVSGSGKSSlafdTIyaegqrRYVESLSAyARQFLGQMDKPDVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 72 VAPKDRDIAMVFQNYALYPHMTV------YDnmafglKLRK-YSKEDIDKRVQEAAEIlGLKEF-LDRKPADLSGGQRQR 143
Cdd:cd03270 73 IEGLSPAIAIDQKTTSRNPRSTVgtvteiYD------YLRLlFARVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 144 VAMGRAIVR--DAKVFLMDEPLSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHDQtEAMTLADRIVIM 209
Cdd:cd03270 146 IRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDI 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-236 |
4.47e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 27 DIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVVNNVAPKDrdiamVFQNYALYPHMTVYDNMAFGLKLRK 106
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD-----LRKVLGIIPQAPVLFSGTVRFNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 107 YSkEDIDKRVQEAAEILGLKEFLDRKPADL-----------SGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDaklrVSMR 175
Cdd:PLN03130 1336 FN-EHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD----VRTD 1410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 881073645 176 AEIAK-IHRRIGATTIYVTHDQTEAMTLADRIVIMSAtknpagtgtiGRVEQIGSPQEVYKN 236
Cdd:PLN03130 1411 ALIQKtIREEFKSCTMLIIAHRLNTIIDCDRILVLDA----------GRVVEFDTPENLLSN 1462
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
293-367 |
4.57e-06 |
|
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: 44.15 E-value: 4.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 293 GIRPEDVNTEAAfletfpESVVKATISVSELLGSESHLYCQVGD-NEFIAKVDARDY--LGTGETIELGFDLNKAHFF 367
Cdd:pfam08402 2 AIRPEKIRLAAA------ANGLSGTVTDVEYLGDHTRYHVELAGgEELVVRVPNAHArpPAPGDRVGLGWDPEDAHVL 73
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-209 |
5.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 38 GPSGCGKSTTLRMIAglEDITEGECSiDGTVVNNVAPKD----RDIAMVFQNYALYPHMTVYDNMAFGLKLR---KYSKE 110
Cdd:TIGR00956 796 GASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 111 DIDKRVQEAAEILGLKEFLDR---KPAD-LSGGQRQRVAMGRAIVRDAKVFL-MDEPLSNLDAKLRVSmraeIAKIHRRI 185
Cdd:TIGR00956 873 EKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS----ICKLMRKL 948
|
170 180
....*....|....*....|....*...
gi 881073645 186 GAT--TIYVTHDQTEAMTLA--DRIVIM 209
Cdd:TIGR00956 949 ADHgqAILCTIHQPSAILFEefDRLLLL 976
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-176 |
7.73e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 37 VGPSGCGKSTTLRMIAGLED--ITEGECSIDGTvvnnvaPKDRDI-----AMVFQNYALYPHMTVYDNMAFGLKLR---- 105
Cdd:PLN03140 912 MGVSGAGKTTLMDVLAGRKTggYIEGDIRISGF------PKKQETfarisGYCEQNDIHSPQVTVRESLIYSAFLRlpke 985
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 881073645 106 --KYSKEDIDKRVQEAAEILGLKEFLDRKPA--DLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAK-LRVSMRA 176
Cdd:PLN03140 986 vsKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRT 1061
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
30-218 |
1.82e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 30 DKEFIVFVGPSGCGKSTTLRMIAgleditegecsidgtvvnnvapkdrdiamvfqnYALyphmtvydnmaFGLKLRKYSK 109
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------------------------------LAL-----------GGAQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 110 EDIDKRVQEAAEILGLKEFLDRkpadLSGGQRQRVA----MGRAIVRDAKVFLMDEPLSNLDAKLRVSMrAEIAKIHRRI 185
Cdd:cd03227 56 SGVKAGCIVAAVSAELIFTRLQ----LSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQAL-AEAILEHLVK 130
|
170 180 190
....*....|....*....|....*....|...
gi 881073645 186 GATTIYVTHDQtEAMTLADRIVIMSATKNPAGT 218
Cdd:cd03227 131 GAQVIVITHLP-ELAELADKLIHIKKVITGVYK 162
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
92-237 |
2.57e-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: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 92 MTVYDNMAF--GLKL---RKYSKEDIDKRVQEAAEIL---GLKEF-LDRKPADLSGGQRQRVAM----GRAIVrdAKVFL 158
Cdd:TIGR00630 436 LSIREAHEFfnQLTLtpeEKKIAEEVLKEIRERLGFLidvGLDYLsLSRAAGTLSGGEAQRIRLatqiGSGLT--GVLYV 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 159 MDEPLSNLDAklRVSMR-AEIAKIHRRIGATTIYVTHDQtEAMTLADRIVIMSatknpAGTGTI-GRVEQIGSPQEVYKN 236
Cdd:TIGR00630 514 LDEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDIG-----PGAGEHgGEVVASGTPEEILAN 585
|
.
gi 881073645 237 P 237
Cdd:TIGR00630 586 P 586
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
252-299 |
4.61e-04 |
|
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: 37.42 E-value: 4.61e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 881073645 252 NFINVKLEGGYIVTNGLNLKVPEGAlkvlkekGYDGKELIFGIRPEDV 299
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPELA-------GAEGSEVVAYVRPHDL 41
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-210 |
5.43e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 5.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 881073645 136 LSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD--AKLRV-SMRAEIAKIHRRIgattIYVTHDQTEAMTLADRIVIMS 210
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFEIyQLIAELAKKDKGI----IIISSEMPELLGITDRILVMS 465
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
6-164 |
9.10e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 6 LKNIYKKYPNSE-HYSVEDFNLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGECSIDGTVvnnvapkdrdiAMVFQ 84
Cdd:PRK13545 24 LKDLFFRSKDGEyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 85 NYALYPHMTVYDNMAFGLKLRKYSKEDIDKRVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLS 164
Cdd:PRK13545 93 SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-184 |
1.03e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 25 NLDIKDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGE--CSIDGTVVNNVAPKDRDIAMVFQ---NYALYPhmtvyDNMA 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqSQFSHITRLSFEQLQKLVSDEWQrnnTDMLSP-----GEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 100 FGLKLRKYSKEDIDK--RVQEAAEILGLKEFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVSMRAE 177
Cdd:PRK10938 98 TGRTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
....*..
gi 881073645 178 IAKIHRR 184
Cdd:PRK10938 178 LASLHQS 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-167 |
1.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 14 PNSEHYSVEDFNLDIKDKEFIV-------------FVGPSGCGKSTTLRMIA-----GL---------------EDITEG 60
Cdd:PLN03073 173 PAIKDIHMENFSISVGGRDLIVdasvtlafgrhygLVGRNGTGKTTFLRYMAmhaidGIpkncqilhveqevvgDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 61 ECSIDgTVVNNVAPKDRDIAMVFQNYAL-YPHMTVYDNMAF--GLKLRKYSK--EDIDKRVQ---------EAAEIL-GL 125
Cdd:PLN03073 253 QCVLN-TDIERTQLLEEEAQLVAQQRELeFETETGKGKGANkdGVDKDAVSQrlEEIYKRLElidaytaeaRAASILaGL 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 881073645 126 K---EFLDRKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PLN03073 332 SftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
33-119 |
1.49e-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: 39.77 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 33 FIVFVGPSGCGKSTTLRMIagLEDItegecsidgtvvnnvaPKDRDIAMVFqnyalYPHMTVYD-----NMAFGLKLRKY 107
Cdd:COG3267 45 FVVLTGEVGTGKTTLLRRL--LERL----------------PDDVKVAYIP-----NPQLSPAEllraiADELGLEPKGA 101
|
90
....*....|..
gi 881073645 108 SKEDIDKRVQEA 119
Cdd:COG3267 102 SKADLLRQLQEF 113
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
129-209 |
3.94e-03 |
|
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: 37.69 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 129 LDRKPADLSGGQRQRVAMGRAIVRDAK--VFLMDEPLSNLDAKLRVSMRAEIAKIhRRIGATTIYVTHDQTeAMTLADRI 206
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLD-VLSSADWI 158
|
...
gi 881073645 207 VIM 209
Cdd:cd03238 159 IDF 161
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-207 |
5.08e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.97 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 30 DKEFIVFVGPSGCGKSTTlrmIAGLEDITEGEC---SIDGTVVNNVAPKDRDIAMV---FQN-----YALYPHMTVYDNM 98
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTI---IEALKYALTGELppnSKGGAHDPKLIREGEVRAQVklaFENangkkYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073645 99 AFglklrkYSKEDIDKrvqeaaeilglkeFLDRKPADLSGGQRQ------RVAMGRAIVRDAKVFLMDEPLSNLDA-KLR 171
Cdd:cd03240 98 IF------CHQGESNW-------------PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIE 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 881073645 172 VSMRAEIAKIHRRIGATTIYVTHDQtEAMTLADRIV 207
Cdd:cd03240 159 ESLAEIIEERKSQKNFQLIVITHDE-ELVDAADHIY 193
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
5-46 |
8.87e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 8.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 881073645 5 NLKNIykkypnsehysvedfNLDI-KDKeFIVFVGPSGCGKST 46
Cdd:PRK00349 15 NLKNI---------------DLDIpRDK-LVVFTGLSGSGKSS 41
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
114-167 |
8.90e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.07 E-value: 8.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 881073645 114 KRVQEAAEILGLKEFLDRKP-ADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLD 167
Cdd:PRK10938 379 KLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| |
