|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-350 |
0e+00 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 587.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSKVFKKGK--VVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPP 79
Cdd:NF040933 1 VTVRVENVTKIFKKGKkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGKIIVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVAS 239
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 240 LIGEINELEGKVTNEG-VVIGSLRFPVSVSS---DRAIIGIRPEDVKLSK-DVIKDDSWILVGKGKVKVIGYQGGLFRIT 314
Cdd:NF040933 241 LIGDINLLEGKVEEEGlVDGNDLKIPLPNPKleaGEVIIGIRPEDIDISEsDMRLPPGFVEVGKGRVKVSSYAGGVFRVV 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 499226461 315 ITPLDSEE-EIFTYSDHPIHSGEEVLVYVRKDKIKVF 350
Cdd:NF040933 321 VSPIDDDSiEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-353 |
1.24e-148 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 422.94 E-value: 1.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPE 80
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----LPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL 240
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 241 IGE--INELEGKVTNEGVVIGSLRFPVSV-----SSDRAIIGIRPEDVKLSKDvikDDSWIlvgKGKVKVIGYQGGLFRI 313
Cdd:COG3839 234 IGSppMNLLPGTVEGGGVRLGGVRLPLPAalaaaAGGEVTLGIRPEHLRLADE---GDGGL---EATVEVVEPLGSETLV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 499226461 314 TITPLDSEEEIFTYSDHPIHSGEEVLVYVRKDKIKVFEKN 353
Cdd:COG3839 308 HVRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-352 |
1.13e-133 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 384.84 E-value: 1.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPE 80
Cdd:COG3842 3 MPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL 240
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 241 IGEINELEGKVT---NEGVVIGSLRFPVSVSS-----DRAIIGIRPEDVKLSKDviKDDSWIlvgKGKVKVIGYQGGLFR 312
Cdd:COG3842 236 IGEANLLPGTVLgdeGGGVRTGGRTLEVPADAglaagGPVTVAIRPEDIRLSPE--GPENGL---PGTVEDVVFLGSHVR 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499226461 313 ITITpLDSEEEIFTYSDH----PIHSGEEVLVYVRKDKIKVFEK 352
Cdd:COG3842 311 YRVR-LGDGQELVVRVPNraalPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-347 |
5.38e-114 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 334.81 E-value: 5.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgkliVPPEDRK 83
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN----LPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGE 243
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 244 INELEGKVTNEGVVIGSLRFPVS--VSSDRAIIGIRPEDVKLSKDVIKDDSWilvgKGKVKVIGYQGGLFRITITPLDSE 321
Cdd:COG1118 237 VNVLRGRVIGGQLEADGLTLPVAepLPDGPAVAGVRPHDIEVSREPEGENTF----PATVARVSELGPEVRVELKLEDGE 312
|
330 340 350
....*....|....*....|....*....|...
gi 499226461 322 EEIF-------TYSDHPIHSGEEVLVYVRKDKI 347
Cdd:COG1118 313 GQPLeaevtkeAWAELGLAPGDPVYLRPRPARV 345
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-223 |
4.06e-111 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 322.55 E-value: 4.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-223 |
6.43e-98 |
|
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: 288.77 E-value: 6.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD-----LPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-351 |
1.50e-97 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 293.10 E-value: 1.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYfddrlvaSNGKLI--VP 78
Cdd:TIGR03265 2 SPYLSIDNIRKRF--GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIY-------QGGRDItrLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:TIGR03265 73 PQKRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVA 238
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 239 SLIGEINELEGKV-TNEGVVIGSLRF----PVSVSSDRAIIGIRPEDVKLSKDVIKDDSWilvgKGKVKVIGYQGGLFRI 313
Cdd:TIGR03265 233 DFVGEVNWLPGTRgGGSRARVGGLTLacapGLAQPGASVRLAVRPEDIRVSPAGNAANLL----LARVEDMEFLGAFYRL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499226461 314 TITPLDSEEEI----FTYSD---HPIHSGEEVLVYVRKDKIKVFE 351
Cdd:TIGR03265 309 RLRLEGLPGQAlvadVSASEverLGIRAGQPIWIELPAERLRAFA 353
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-242 |
9.80e-91 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 271.42 E-value: 9.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIG 242
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-286 |
1.32e-87 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 267.86 E-value: 1.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVasNGkliVPPE 80
Cdd:PRK11650 1 MAGLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NE---LEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL 240
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 241 IGE--INELEGKVTNEGVVI---GSLRFPVSVSSD-----RAIIGIRPEDVKLSKD 286
Cdd:PRK11650 235 IGSpaMNLLDGRVSADGAAFelaGGIALPLGGGYRqyagrKLTLGIRPEHIALSSA 290
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-286 |
3.79e-85 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 261.58 E-value: 3.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKlivppEDRK 83
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI-----QQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGE 243
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499226461 244 INELEGKVTNEGVVIGSLRFPV------SVSSDRAIIGIRPEDVKLSKD 286
Cdd:PRK11432 240 ANIFPATLSGDYVDIYGYRLPRpaafafNLPDGECTVGVRPEAITLSEQ 288
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
5.30e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 246.49 E-value: 5.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRII-VKNVSKVFKKG--KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsngKLiv 77
Cdd:COG1136 1 MSPLLeLRNLTKSYGTGegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS---SL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 78 pPED-------RKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVA 150
Cdd:COG1136 76 -SERelarlrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPaDIFAIADRVGVLVKGKLV 220
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-243 |
1.02e-80 |
|
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: 246.10 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-----VPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPL----TNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVAS 239
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235
|
....
gi 499226461 240 LIGE 243
Cdd:cd03296 236 FLGE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-298 |
2.77e-80 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 249.86 E-value: 2.77e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH-----VPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGE 243
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 244 INELEGKVT---NEGVVIGSL---------RFPVSVsSDRAIIGIRPEDVKLSKDVIKDDSWILVGK 298
Cdd:PRK09452 248 INIFDATVIerlDEQRVRANVegrecniyvNFAVEP-GQKLHVLLRPEDLRVEEINDDEHAEGLIGY 313
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-242 |
3.85e-80 |
|
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: 244.55 E-value: 3.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFddrlvasNGKLI--VPPEDRKIGMVFQTW 91
Cdd:cd03299 8 KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL-------NGKDItnLPPEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 ALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNL 171
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 172 DARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIG 242
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-287 |
5.30e-80 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 248.79 E-value: 5.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPE 80
Cdd:PRK11000 1 MASVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND-----VPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL 240
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 241 IG--EINELEGKVT---NEGVVI---GSLRFPVSVSS------DRAIIGIRPE--------DVKLSKDV 287
Cdd:PRK11000 234 IGspKMNFLPVKVTataIEQVQVelpNRQQVWLPVEGrgvqvgANMSLGIRPEhllpsdiaDVTLEGEV 302
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-214 |
1.98e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 243.46 E-value: 1.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDdrlvasnGKLIVP 78
Cdd:COG1116 5 APALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-------GKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PeDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:COG1116 78 P-GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-218 |
1.66e-78 |
|
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: 238.24 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKlIVPPEDRK 83
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED-ELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPltnmkmskeeirkrveevakildihhvlnhfpreLSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-233 |
1.48e-76 |
|
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: 235.26 E-value: 1.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDR-LVASNGKLIVPPEdR 82
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYELR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNLTAFENIAFPLT-NMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 162 LLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLY--DNPV 233
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDPW 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-310 |
5.62e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 238.58 E-value: 5.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKkGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRKIG 85
Cdd:PRK11607 22 IRNLTKSFD-GQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-----VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLD 165
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 166 EPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEIN 245
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 246 ELEGKVT---NEGVVIGS--LRFPVSVSSDRAI-------IGIRPEDVKLSKDVIKDDSWILVgkGKVKVIGYQGGL 310
Cdd:PRK11607 255 VFEGVLKerqEDGLVIDSpgLVHPLKVDADASVvdnvpvhVALRPEKIMLCEEPPADGCNFAV--GEVIHIAYLGDL 329
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-219 |
1.42e-75 |
|
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: 232.00 E-value: 1.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG--KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--SNGKLIvpp 79
Cdd:cd03255 1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklSEKELA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDR--KIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVK 157
Cdd:cd03255 78 AFRrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 158 DPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPaDIFAIADRVGVLVKGKL 219
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-315 |
2.94e-75 |
|
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: 235.08 E-value: 2.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 36 ILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKE 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN-----VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 116 EIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLL 195
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 196 VVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEINELEGKVTNEG----VVIGSLRFPVSVSSDR 271
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKseqvVLAGVEGRRCDIYTDV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499226461 272 AIIG-------IRPEDVKLSKdvIKDDSWILVGKGKVKVIGYQGGLFRITI 315
Cdd:TIGR01187 236 PVEKdqplhvvLRPEKIVIEE--EDEANSSNAIIGHVIDITYLGMTLEVHV 284
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-228 |
4.63e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.79 E-value: 4.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRK 83
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-285 |
2.52e-73 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 231.13 E-value: 2.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:PRK10851 3 IEIANIKKSFGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-----LHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNM----KMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLTVLprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVAS 239
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLE 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499226461 240 LIGEINELEGKVTNEGVVIGSLRFPVSVSS---DRAIIGIRPEDVKLSK 285
Cdd:PRK10851 236 FMGEVNRLQGTIRGGQFHVGAHRWPLGYTPayqGPVDLFLRPWEVDISR 284
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
4.08e-73 |
|
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: 225.81 E-value: 4.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDdrlvasnGKLIVPPeD 81
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD-------GEPVTGP-G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499226461 162 LLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-232 |
2.06e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 228.04 E-value: 2.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--SNGKLIvpP 79
Cdd:COG1135 2 IELENLSKTFptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERELR--A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-232 |
6.91e-71 |
|
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: 220.92 E-value: 6.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK--KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPED 81
Cdd:cd03258 2 IELKNVSKVFGdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 162 LLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-232 |
1.85e-70 |
|
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: 219.51 E-value: 1.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDR-LVASNGKLIVppedR 82
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKdITKKNLRELR----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQtwalYP-----NLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVK 157
Cdd:COG1122 76 KVGLVFQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 158 DPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-232 |
5.16e-70 |
|
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: 227.09 E-value: 5.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVF---KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDR 82
Cdd:COG1123 263 VRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQ--TWALYPNLTAFENIAFPLTNMK-MSKEEIRKRVEEVAKI--LDIHHvLNHFPRELSGGQQQRVALARALVK 157
Cdd:COG1123 343 RVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERvgLPPDL-ADRYPHELSGGQRQRVAIARALAL 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 158 DPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:COG1123 422 EPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
8.12e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 217.61 E-value: 8.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIivKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE 80
Cdd:COG2884 1 MIRF--ENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-243 |
9.45e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 217.70 E-value: 9.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 25 NINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRKIGMVFQTWALYPNLTAFENIA 104
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-----LPPAERPVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 105 FPLT-NMKMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALV 183
Cdd:COG3840 94 LGLRpGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 184 KEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGE 243
Cdd:COG3840 173 DELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-232 |
4.23e-68 |
|
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: 213.52 E-value: 4.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKkGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFD--DRLVASNGKLIvpPED 81
Cdd:cd03261 1 IELRGLTKSFG-GRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELY--RLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPL-TNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLY--DNP 232
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDP 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-223 |
6.71e-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: 212.54 E-value: 6.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIE---NGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDR-LVASNGKLIVPPEDRKIGMVFQTWALYPN 96
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 97 LTAFENIAFPLTnmKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMR 176
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499226461 177 DSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-218 |
1.95e-67 |
|
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: 211.17 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPpedRKIG 85
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---RKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQtwalYP-----NLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:cd03225 79 LVFQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQsRLGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-243 |
3.08e-66 |
|
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: 209.08 E-value: 3.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED-- 81
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-----QDPVElr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKI--LDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVAS 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 499226461 240 LIGE 243
Cdd:cd03295 235 FVGA 238
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-243 |
2.16e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 209.18 E-value: 2.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED-- 81
Cdd:COG1125 2 IEFENVTKRYPDGTV-AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD-----LDPVElr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKI--LDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVAS 239
Cdd:COG1125 156 PILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAD 235
|
....
gi 499226461 240 LIGE 243
Cdd:COG1125 236 FVGA 239
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
3.12e-65 |
|
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: 206.58 E-value: 3.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG--KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDdrlvasnGKLIVPPED 81
Cdd:COG1124 2 LEVRNLSVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD-------GRPVTRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 ----RKIGMVFQ--TWALYPNLTAFENIAFPLTNMKMSkeEIRKRVEEVAKILDIH-HVLNHFPRELSGGQQQRVALARA 154
Cdd:COG1124 75 kafrRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-232 |
3.21e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 206.38 E-value: 3.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvpPEDR- 82
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDI--NKLRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNLTAFENIAF-PLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 162 LLLDEPFSNLDARMrdsaralVKEVQS------RLGVTLLVVSHDPAdiFA--IADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:COG1126 158 MLFDEPTSALDPEL-------VGEVLDvmrdlaKEGMTMVVVTHEMG--FAreVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-223 |
1.28e-64 |
|
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: 204.66 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRK 83
Cdd:cd03257 4 VKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQ--TWALYPNLTAFENIAFPLT-NMKMSKEEIRKRV--EEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:cd03257 84 IQMVFQdpMSSLNPRMTIGEQIAEPLRiHGKLSKKEARKEAvlLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-241 |
3.45e-62 |
|
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: 199.79 E-value: 3.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF----------------------KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGE 61
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 62 LYFDDRLVAS-NGKLIVPPEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRE 140
Cdd:cd03294 81 VLIDGQDIAAmSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 141 LSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|.
gi 499226461 221 QVGKPEDLYDNPVSIQVASLI 241
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFF 261
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-232 |
4.06e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 196.56 E-value: 4.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIivKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDR-LVA-SNGKLI 76
Cdd:PRK11153 1 MIEL--KNISKVFpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdLTAlSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 VppEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV 156
Cdd:PRK11153 79 K--ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-231 |
6.33e-60 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 192.77 E-value: 6.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRK 83
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA----RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARmrdSARALVKEVQS--RLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:COG4555 156 LDEPTNGLDVM---ARRLLREILRAlkKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-232 |
9.40e-59 |
|
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: 191.13 E-value: 9.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQtwalYPN-----LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDI-HHVLNHFPRELSGGQQQRVALARA 154
Cdd:TIGR04521 81 RKKVGLVFQ----FPEhqlfeETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-232 |
1.35e-58 |
|
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: 189.86 E-value: 1.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDR-KI 84
Cdd:COG0411 7 VRGLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG-----LPPHRIaRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 GMV--FQTWALYPNLTAFENIA---------------FPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQ 147
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*
gi 499226461 228 LYDNP 232
Cdd:COG0411 240 VRADP 244
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-232 |
3.07e-58 |
|
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: 188.41 E-value: 3.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK-- 83
Cdd:cd03219 3 VRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-----LPPHEIArl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 -IGMVFQTWALYPNLTAFENI----------AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALA 152
Cdd:cd03219 76 gIGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-252 |
8.34e-57 |
|
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: 188.39 E-value: 8.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDnVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLI-VPPEDRKIGMVFQTWALYPNLT 98
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIfLPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFpltNMKMSKEEIRK-RVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRD 177
Cdd:COG4148 94 VRGNLLY---GRKRAPRAERRiSFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 178 SARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEINELEGKVT 252
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVA 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-258 |
8.40e-57 |
|
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: 192.43 E-value: 8.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPS----TGELYFDDR-LVASNGKLIvp 78
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHggriSGEVLLDGRdLLELSEALR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 peDRKIGMVFQ--TWALYPnLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV 156
Cdd:COG1123 82 --GRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQ 236
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
250 260
....*....|....*....|..
gi 499226461 237 VASLIGEINELEGKVTNEGVVI 258
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPL 260
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-218 |
2.10e-56 |
|
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: 182.83 E-value: 2.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIvkNVSKVFKKGkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE 80
Cdd:TIGR02673 1 MIEFH--NVSKAYPGG-VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:TIGR02673 78 RRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-219 |
2.84e-56 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 181.06 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVppedRK 83
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK----RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIafpltnmkmskeeirkrveevakildihhvlnhfprELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
5.77e-56 |
|
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: 182.25 E-value: 5.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK--KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGElyfddrlVASNGKLIVP-PE 80
Cdd:COG4181 9 IELRGLTKTVGtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-------VRLAGQDLFAlDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 D-------RKIGMVFQTWALYPNLTAFENIAFP--LTNMKMSKEEIRKRVEEVAkiLDihHVLNHFPRELSGGQQQRVAL 151
Cdd:COG4181 82 DararlraRHVGFVFQSFQLLPTLTALENVMLPleLAGRRDARARARALLERVG--LG--HRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 152 ARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQ 221
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-234 |
2.65e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 181.06 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrLVASNGKLIVPPEDRKIGM 86
Cdd:PRK09493 5 KNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-LKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 87 VFQTWALYPNLTAFENIAF-PLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLD 165
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 166 EPFSNLDARMRDSA----RALVKEvqsrlGVTLLVVSHDPAdiFA--IADRVGVLVKGKLVQVGKPEDLYDNPVS 234
Cdd:PRK09493 162 EPTSALDPELRHEVlkvmQDLAEE-----GMTMVIVTHEIG--FAekVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-211 |
4.51e-55 |
|
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: 179.26 E-value: 4.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvPPEDRK 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI-NELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNM-KMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLL 162
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 163 LLDEPFSNLDARMrdsaralVKEVQ------SRLGVTLLVVSHDPADIFAIADRV 211
Cdd:cd03262 158 LFDEPTSALDPEL-------VGEVLdvmkdlAEEGMTMVVVTHEMGFAREVADRV 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-228 |
7.18e-54 |
|
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: 176.54 E-value: 7.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRK 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA----RQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFpLTNMK-MSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLL 162
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRF-YARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 163 LLDEPFSNLDARMRDSARALVKEVQSrlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-219 |
1.92e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.00 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED--RK 83
Cdd:COG4619 3 LEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA-----MPPPEwrRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNlTAFENIAFPLT--NMKMSKEEIRKRVEEVAkiLDiHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:COG4619 76 VAYVPQEPALWGG-TVRDNLPFPFQlrERKFDRERALELLERLG--LP-PDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 162 LLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-232 |
2.10e-53 |
|
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: 178.71 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVP---STGELYFDDRLVASngkliVPPE 80
Cdd:COG0444 4 VRNLKVYFptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK-----LSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 D------RKIGMVFQ---TwALYPNLTAFENIAFPL-TNMKMSKEEIRKRVEEVAK---ILDIHHVLNHFPRELSGGQQQ 147
Cdd:COG0444 79 ElrkirgREIQMIFQdpmT-SLNPVMTVGDQIAEPLrIHGGLSKAEARERAIELLErvgLPDPERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*
gi 499226461 228 LYDNP 232
Cdd:COG0444 238 LFENP 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-219 |
6.52e-53 |
|
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: 173.75 E-value: 6.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRK 83
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 164 LDEPFSNLDArmrDSARALVKEVQS--RLGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:cd03292 160 ADEPTGNLDP---DTTWEIMNLLKKinKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-228 |
8.52e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.86 E-value: 8.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRK 83
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENI---AFPLTN------MKMSKEEIRkRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGRTStwrsllGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 155 LVKDPSLLLLDEPFSNLDARmrdSAR---ALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG3638 161 LVQEPKLILADEPVASLDPK---TARqvmDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-224 |
2.34e-51 |
|
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: 170.04 E-value: 2.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 25 NINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVasngkLIVPPEDRKIGMVFQTWALYPNLTAFENIA 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-----TGLAPYQRPVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 105 FPLT-NMKMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALV 183
Cdd:TIGR01277 93 LGLHpGLKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499226461 184 KEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-228 |
2.85e-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: 170.05 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGL-----DVPSTGELYFDDRLVASNGKLIVPPE 80
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 dRKIGMVFQTWALYPnLTAFENIAFPLTNMKM-SKEEIRKRVEEVAKILDIH-HVLNH-FPRELSGGQQQRVALARALVK 157
Cdd:cd03260 81 -RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdEVKDRlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 158 DPSLLLLDEPFSNLDARmrdSARA---LVKEVQSRlgVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:cd03260 159 EPEVLLLDEPTSALDPI---STAKieeLIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
2.94e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 171.20 E-value: 2.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKKGK--VVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklivP 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRkiGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:COG4525 75 GADR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHD 200
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-223 |
9.90e-51 |
|
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: 168.06 E-value: 9.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 28 IENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRKIGMVFQTWALYPNLTAFENIAFPL 107
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-----APPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 108 T-NMKMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEV 186
Cdd:cd03298 96 SpGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 499226461 187 QSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-242 |
1.04e-50 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 168.99 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 25 NINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFddrlvasNGK--LIVPPEDRKIGMVFQTWALYPNLTAFEN 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL-------NGQdhTTTPPSRRPVSMLFQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 103 IAFPLT-NMKMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARA 181
Cdd:PRK10771 92 IGLGLNpGLKLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 182 LVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNpvSIQVASLIG 242
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSG--KASASALLG 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-228 |
1.31e-50 |
|
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: 169.07 E-value: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED- 81
Cdd:COG1120 1 MLEAENLS--VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS-----LSRREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 -RKIGMVFQTWALYPNLTAFENIA---FPLTNM--KMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARAL 155
Cdd:COG1120 74 aRRIAYVPQEPPAPFGLTVRELVAlgrYPHLGLfgRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 156 VKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-233 |
1.67e-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: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDnVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGK-LIVPPEDRKIGMVFQTWALYPNLT 98
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFPLTnmKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDS 178
Cdd:TIGR02142 92 VRGNLRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 179 ARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPV 233
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-211 |
6.44e-50 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 166.12 E-value: 6.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGL---DVPSTGELYFDDRLVASngkliVPPEDRKIGMVFQTWALYPNL 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTA-----LPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 98 TAFENIAFPLTNmKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRD 177
Cdd:COG4136 92 SVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|....
gi 499226461 178 SARALVKEVQSRLGVTLLVVSHDPADIFAiADRV 211
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRV 203
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
4-247 |
2.72e-49 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 169.57 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKK----------------------GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGE 61
Cdd:TIGR03415 1 IRFKNVDIVFGDqpdealalldqgktreeildrtGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 62 LyfddrLVASNGKLIVP-----PEDRK-----IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIH 131
Cdd:TIGR03415 81 V-----LVKDGDGSVDVancdaATLRRlrthrVSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 132 HVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRV 211
Cdd:TIGR03415 156 QWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRI 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 499226461 212 GVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEINEL 247
Cdd:TIGR03415 236 AIMEGGRIIQHGTPEEIVLNPANDYVADFVAHTNPL 271
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-228 |
4.10e-49 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 175.02 E-value: 4.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED- 81
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ-----IDPASl 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 -RKIGMVFQTWALYpNLTAFENIAfpLTNMKMSKEEIRkrveEVAKILDIHHVLNHFP-----------RELSGGQQQRV 149
Cdd:COG2274 548 rRQIGVVLQDVFLF-SGTIRENIT--LGDPDATDEEII----EAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDARmrdSARALVKEVQSRL-GVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAE---TEAIILENLRRLLkGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-232 |
9.20e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 166.83 E-value: 9.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF---------KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGK 74
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 75 LIVPPEDRKIGMVFQ--TWALYPNLTAFENIAFPLTNMKM-SKEEIRKRVEEV-AKI-LDIHHvLNHFPRELSGGQQQRV 149
Cdd:COG4608 88 RELRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELlELVgLRPEH-ADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDArmrdSARA----LVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKP 225
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDV----SIQAqvlnLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
....*..
gi 499226461 226 EDLYDNP 232
Cdd:COG4608 243 DELYARP 249
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-243 |
1.01e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 164.91 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFD--DRLVASNGKLIvppeD 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDglDTLDEENLWEI----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQtwalypN-------LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:TIGR04520 77 KKVGMVFQ------NpdnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDLY----- 229
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFsqvel 229
|
250 260
....*....|....*....|
gi 499226461 230 ------DNPVSIQVASLIGE 243
Cdd:TIGR04520 230 lkeiglDVPFITELAKALKK 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-230 |
2.24e-48 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 163.12 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRK 83
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMK---------MSKEEIRKRVEEVAKiLDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEKQRALAALER-VGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-200 |
9.01e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 161.14 E-value: 9.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 8 NVSKVFKKGKVVA--LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV-----ASNGKLivppE 80
Cdd:PRK11629 10 NLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAKAEL----R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHD 200
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-204 |
1.50e-47 |
|
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: 159.57 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivPPEDR 82
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR----EDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNLTAFENIAF--PLTNMKMSKEEIrkrvEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFwaALYGLRADREAI----DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADI 204
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-223 |
2.20e-47 |
|
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: 159.67 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKvvALDNVNINIENGeRFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRK 83
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL----RRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSrlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
2.42e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 160.64 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLI--VP 78
Cdd:COG1121 4 MPAIELENLT--VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIgyVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 pedrkigmvfQTWALYPN--LTAFENIAFPLTN----MKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALA 152
Cdd:COG1121 82 ----------QRAEVDWDfpITVRDVVLMGRYGrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVgVLVKGKLVQVGKPED 227
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-218 |
2.83e-47 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 157.41 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsngKLIVPPEDRKIG 85
Cdd:cd00267 2 IENLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---KLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQtwalypnltafeniafpltnmkmskeeirkrveevakildihhvlnhfpreLSGGQQQRVALARALVKDPSLLLLD 165
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499226461 166 EPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-223 |
1.33e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 158.64 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEL-----YFD--DRLVASNGKLI 76
Cdd:COG4161 3 IQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghQFDfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 vppeDRKIGMVFQTWALYPNLTAFEN-IAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARAL 155
Cdd:COG4161 81 ----RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 156 VKDPSLLLLDEPFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPAdiFA--IADRVGVLVKGKLVQVG 223
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVE--FArkVASQVVYMEKGRIIEQG 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-223 |
3.14e-46 |
|
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: 156.76 E-value: 3.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK--KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgklivPPE- 80
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKE-----PAEa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEvQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-231 |
1.07e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 157.52 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlVASNGKLIVPPE 80
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRK-IGMVFQtwalYPNLTAFE-----NIAFPLTNMKMSKEEIRKRVEEVAKI--LDIHHVLNHFPRELSGGQQQRVALA 152
Cdd:PRK13637 81 IRKkVGLVFQ----YPEYQLFEetiekDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-258 |
1.84e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 157.19 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASN-----GKLivpPE 80
Cdd:COG4152 4 LKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdrrriGYL---PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRkigmvfqtwALYPNLTAFENIAFpLTNMK-MSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:COG4152 79 ER---------GLYPKMKVGEQLVY-LARLKgLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 160 SLLLLDEPFSNLDA----RMRDSARALVKEvqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYD----N 231
Cdd:COG4152 149 ELLILDEPFSGLDPvnveLLKDVIRELAAK-----GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRqfgrN 223
|
250 260 270
....*....|....*....|....*....|.
gi 499226461 232 PVSIQVASLIGEINELEG----KVTNEGVVI 258
Cdd:COG4152 224 TLRLEADGDAGWLRALPGvtvvEEDGDGAEL 254
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-211 |
1.99e-45 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 154.31 E-value: 1.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKvfKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS-NGKLIVPPEDRKI 84
Cdd:TIGR03608 1 LKNISK--KFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 GMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLL 164
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499226461 165 DEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPAdIFAIADRV 211
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPE-VAKQADRV 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-223 |
2.04e-45 |
|
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: 154.61 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklivppEDRKIG 85
Cdd:cd03235 2 VEDLT--VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--------ERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQT----WAlYPnLTAFENIAFPLTN-----MKMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV 156
Cdd:cd03235 72 YVPQRrsidRD-FP-ISVRDVVLMGLYGhkglfRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQsRLGVTLLVVSHDPADIFAIADRVgVLVKGKLVQVG 223
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
2.28e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 152.03 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlvaSNGKLIVPPEDRKIGMVFQTWALYPNLTAF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ---DLTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 101 ENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNH----FPRELSGGQQQRVALARALVKDPSLLLLDEPFS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-230 |
1.43e-44 |
|
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: 153.22 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRK 83
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMK---------MSKEEIRKRVEEVAKiLDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgrFSEEDKERALSALER-VGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
5.24e-44 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 159.15 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSkVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED 81
Cdd:COG4988 335 PSIELEDVS-FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD-----LDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 --RKIGMVFQTWALyPNLTAFENIAfpLTNMKMSKEEIrkrvEEVAKILDIHHVLNHFP-----------RELSGGQQQR 148
Cdd:COG4988 409 wrRQIAWVPQNPYL-FAGTIRENLR--LGRPDASDEEL----EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRL-GVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDA---ETEAEILQALRRLAkGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
....
gi 499226461 228 LYDN 231
Cdd:COG4988 558 LLAK 561
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-228 |
6.78e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 159.17 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSkvFK-KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED 81
Cdd:COG1132 339 EIEFENVS--FSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD-----LTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 --RKIGMVFQTWALYpNLTAFENIAFpltnmkmSKEEI-RKRVEEVAKILDIHHVLNHFP-----------RELSGGQQQ 147
Cdd:COG1132 412 lrRQIGVVPQDTFLF-SGTIRENIRY-------GRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKevqsrlGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVG 223
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDteteALIQEALERLMK------GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
....*
gi 499226461 224 KPEDL 228
Cdd:COG1132 557 THEEL 561
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-223 |
1.06e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 150.93 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEL-----YFDdrlvasngkLIVP 78
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFD---------FSKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PED-------RKIGMVFQTWALYPNLTAFEN-IAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVA 150
Cdd:PRK11124 72 PSDkairelrRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQsRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-223 |
1.46e-43 |
|
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: 149.74 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKlivppedRKIG 85
Cdd:cd03269 3 VENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR-------NRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTWALYPNLTAFENIAFpLTNMK-MSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLL 164
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVY-LAQLKgLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 165 DEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-228 |
4.61e-43 |
|
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: 148.67 E-value: 4.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYfddrlVASNGKLIVPPEDRK 83
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDVVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 -IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLL 162
Cdd:cd03265 74 rIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 163 LLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-233 |
9.17e-43 |
|
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: 148.07 E-value: 9.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK 83
Cdd:cd03218 1 LRAENLSKRYGKRKVV--NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-----LPMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 ---IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:cd03218 74 rlgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPV 233
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-219 |
9.30e-43 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 147.56 E-value: 9.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS---NGKLIVp 78
Cdd:NF038007 2 LNMQNAEKCYitKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsySQKIIL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 pEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:NF038007 81 -RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 159 PSLLLLDEPFSNLDARmrdSARALVKEVQ--SRLGVTLLVVSH-DPADIFaiADRVGVLVKGKL 219
Cdd:NF038007 160 PALLLADEPTGNLDSK---NARAVLQQLKyiNQKGTTIIMVTHsDEASTY--GNRIINMKDGKL 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-232 |
1.73e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 148.76 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRKIG 85
Cdd:PRK11831 10 MRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTWALYPNLTAFENIAFPL-TNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLL 164
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 165 DEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-241 |
2.65e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 148.06 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSK-------VFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgklivp 78
Cdd:COG4167 7 VRNLSKtfkyrtgLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 peDRK-----IGMVFQ--TWALYPNLTAFENIAFPLT-NMKMSKEEIRKRVEEVAK---ILDIHhvLNHFPRELSGGQQQ 147
Cdd:COG4167 81 --DYKyrckhIRMIFQdpNTSLNPRLNIGQILEEPLRlNTDLTAEEREERIFATLRlvgLLPEH--ANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....
gi 499226461 228 LYDNPVSIQVASLI 241
Cdd:COG4167 237 VFANPQHEVTKRLI 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-232 |
5.21e-42 |
|
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: 153.30 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVF---------KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPSTGELYFDDRLVASNGKLI 76
Cdd:COG4172 278 ARDLKVWFpikrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 VPPEDRKIGMVFQT--WALYPNLTAFENIAFPLT--NMKMSKEEIRKRV----EEVAkiLDiHHVLNHFPRELSGGQQQR 148
Cdd:COG4172 357 LRPLRRRMQVVFQDpfGSLSPRMTVGQIIAEGLRvhGPGLSAAERRARVaealEEVG--LD-PAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDArmrdSARA----LVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDV----SVQAqildLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
....*...
gi 499226461 225 PEDLYDNP 232
Cdd:COG4172 510 TEQVFDAP 517
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-231 |
6.88e-42 |
|
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: 145.65 E-value: 6.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDR---KIGMVFQTWA 92
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-----LPPHERaraGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 LYPNLTAFENI---AFPLTnmkmsKEEIRKRVEEvakildihhVLNHFPR----------ELSGGQQQRVALARALVKDP 159
Cdd:cd03224 86 IFPELTVEENLllgAYARR-----RAKRKARLER---------VYELFPRlkerrkqlagTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 160 SLLLLDEPFSNLdarmrdsARALVKEVQS------RLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:cd03224 152 KLLLLDEPSEGL-------APKIVEEIFEairelrDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-232 |
7.39e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 146.72 E-value: 7.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMR-------IIAGLDVpsTGELYFDDRLVASNGk 74
Cdd:COG1117 10 PKIEVRNLN--VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDPD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 75 liVPPED--RKIGMVFQTwalyPN---LTAFENIAFPL-TNMKMSKEEIRKRVEEV---AKILD-IHHVLNHFPRELSGG 144
Cdd:COG1117 85 --VDVVElrRRVGMVFQK----PNpfpKSIYDNVAYGLrLHGIKSKSELDEIVEESlrkAALWDeVKDRLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 145 QQQRVALARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKEvqsrlgVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILELKKD------YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250
....*....|..
gi 499226461 221 QVGKPEDLYDNP 232
Cdd:COG1117 233 EFGPTEQIFTNP 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-224 |
9.54e-42 |
|
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: 145.69 E-value: 9.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklivPPEDRKIgmVFQTWALYPNLTAF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE------PGPDRMV--VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 101 ENIAFPL--TNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDS 178
Cdd:TIGR01184 73 ENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499226461 179 ARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-228 |
4.65e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.17 E-value: 4.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivpP---EDR 82
Cdd:COG1129 7 MRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS-----PrdaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNLTAFENIAF---PLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 160 SLLLLDEPFSNLDArmRDSAR--ALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG1129 160 RVLILDEPTASLTE--REVERlfRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-223 |
5.90e-41 |
|
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: 141.80 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklivppedrkig 85
Cdd:cd03214 2 VENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 mvfqtwalypnltafeniafpltnmkMSKEEIRKR---VEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLL 162
Cdd:cd03214 66 --------------------------LSPKELARKiayVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 163 LLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-221 |
9.56e-41 |
|
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: 143.79 E-value: 9.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVF-------KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVP 78
Cdd:TIGR02769 5 VRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ-----LD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRK-----IGMVFQTW--ALYPNLTAFENIAFPLTNM-KMSKEEIRKRVEEVAKILDIH-HVLNHFPRELSGGQQQRV 149
Cdd:TIGR02769 80 RKQRRafrrdVQLVFQDSpsAVNPRMTVRQIIGEPLRHLtSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQ 221
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-227 |
1.28e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.02 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivpPE 80
Cdd:COG3845 3 PPALELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS-----PR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 D---RKIGMVFQTWALYPNLTAFENIAF---PLTNMKMSKEEIRKRVEEVAKI--LDIHhvLNHFPRELSGGQQQRVALA 152
Cdd:COG3845 76 DaiaLGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERygLDVD--PDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 153 RALVKDPSLLLLDEPFSNLD----ARMRDSARALVKEvqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG3845 154 KALYRGARILILDEPTAVLTpqeaDELFEILRRLAAE-----GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-218 |
1.30e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 140.60 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED-- 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD-----LDLESlr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYpNLTAFENIafpltnmkmskeeirkrveevakildihhvlnhfpreLSGGQQQRVALARALVKDPSL 161
Cdd:cd03228 76 KNIAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 162 LLLDEPFSNLDArmrDSARALVKEVQSRL-GVTLLVVSHDPADIfAIADRVGVLVKGK 218
Cdd:cd03228 118 LILDEATSALDP---ETEALILEALRALAkGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-234 |
2.22e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 142.63 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA----SNGKLIvpP 79
Cdd:COG4598 9 LEVRDLHKSF--GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdRDGELV--P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRK--------IGMVFQTWALYPNLTAFEN-IAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVA 150
Cdd:COG4598 85 ADRRqlqrirtrLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARmrdsaraLVKEVqsrLGV---------TLLVVSHDPAdiFA--IADRVGVLVKGKL 219
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPE-------LVGEV---LKVmrdlaeegrTMLVVTHEMG--FArdVSSHVVFLHQGRI 232
|
250
....*....|....*
gi 499226461 220 VQVGKPEDLYDNPVS 234
Cdd:COG4598 233 EEQGPPAEVFGNPKS 247
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-232 |
2.56e-40 |
|
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: 141.66 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDR---KIGMVFQTWA 92
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-----LPPHRIarlGIGYVPEGRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 LYPNLTAFENI---AFPLTnmkmSKEEIRKRVEEvakildihhVLNHFPR----------ELSGGQQQRVALARALVKDP 159
Cdd:COG0410 89 IFPSLTVEENLllgAYARR----DRAEVRADLER---------VYELFPRlkerrrqragTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-240 |
3.08e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.82 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV-ASNGKLIvppeDR 82
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEI----RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTwalyPN-----LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVK 157
Cdd:PRK13632 84 KIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 158 DPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFaIADRVGVLVKGKLVQVGKPEDLYDNPVSIQV 237
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEK 238
|
...
gi 499226461 238 ASL 240
Cdd:PRK13632 239 AKI 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-220 |
3.35e-40 |
|
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: 140.82 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlvaSNGKLIVPPedRK 83
Cdd:cd03268 1 LKTNDLTKTYGKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIEAL--RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKeeirKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 164 LDEPFSNLD----ARMRDSARALVKEvqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:cd03268 150 LDEPTNGLDpdgiKELRELILSLRDQ-----GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-232 |
8.11e-40 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 143.31 E-value: 8.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPST-GElyfddrlVASNGKLIVPPEDRK-------IG 85
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGL-VKATdGE-------VAWLGKDLLGMKDDEwravrsdIQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQT--WALYPNLTAFENIAFPLTNM--KMSKEEIRKRVEEV-AKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK15079 102 MIFQDplASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-220 |
1.10e-39 |
|
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: 137.95 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivpPED---R 82
Cdd:cd03216 3 LRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS-----PRDarrA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQtwalypnltafeniafpltnmkmskeeirkrveevakildihhvlnhfpreLSGGQQQRVALARALVKDPSLL 162
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 163 LLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-227 |
1.44e-39 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 140.22 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK--------------------KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEly 63
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 64 fddrlVASNGKlIVPPEDrkIGMVFQtwalyPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHfP-RELS 142
Cdd:COG1134 83 -----VEVNGR-VSALLE--LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 143 GGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQV 222
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*
gi 499226461 223 GKPED 227
Cdd:COG1134 228 GDPEE 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-236 |
1.66e-39 |
|
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: 140.22 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSkVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTG-ELY-FDDRLvasnGKlivppED 81
Cdd:COG1119 4 LELRNVT-VRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGERR----GG-----ED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 -----RKIGMV--FQTWALYPNLTAFENIAFPLTNM----KMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVA 150
Cdd:COG1119 73 vwelrKRIGLVspALQLRFPRDETVLDVVLSGFFDSiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED--- 227
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEvlt 232
|
250
....*....|....*
gi 499226461 228 ------LYDNPVSIQ 236
Cdd:COG1119 233 senlseAFGLPVEVE 247
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-200 |
1.99e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.22 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklivPPEDRkiGMVFQTWALYPNLTA 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------PGAER--GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 100 FENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSA 179
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|.
gi 499226461 180 RALVKEVQSRLGVTLLVVSHD 200
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-220 |
2.46e-39 |
|
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: 139.39 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF-------------------KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGElyf 64
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 65 ddrlVASNGklIVPPEDRK-----IGMVF-QTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFP 138
Cdd:cd03267 78 ----VRVAG--LVPWKRRKkflrrIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 139 RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
..
gi 499226461 219 LV 220
Cdd:cd03267 232 LL 233
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-232 |
6.18e-39 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 138.58 E-value: 6.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLD--VPS---TGELYFDDRLVASNgKLIVP 78
Cdd:TIGR00972 2 IEIENLNLFY--GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlVPGvriEGKVLFDGQDIYDK-KIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRKIGMVFQTWALYPnLTAFENIAF-PLTNMKMSKEEIRKRVEEV---AKILD-IHHVLNHFPRELSGGQQQRVALAR 153
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFP-MSIYDNIAYgPRLHGIKDKKELDEIVEESlkkAALWDeVKDRLHDSALGLSGGQQQRLCIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLgvTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNP 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
6.29e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 138.08 E-value: 6.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIivKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE 80
Cdd:PRK10908 1 MIRF--EHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
1.66e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 144.14 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED 81
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD-----LDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 --RKIGMVFQTWALYpNLTAFENIAfpLTNMKMSKEEIRkrveEVAKILDIHHVLNHFP-----------RELSGGQQQR 148
Cdd:COG4987 407 lrRRIAVVPQRPHLF-DTTLRENLR--LARPDATDEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRL-GVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDA---ATEQALLADLLEALaGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE 555
|
....*
gi 499226461 228 LYDNP 232
Cdd:COG4987 556 LLAQN 560
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-220 |
2.35e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 139.07 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK------------KG-------KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYF 64
Cdd:COG4586 2 IEVENLSKTYRvyekepglkgalKGlfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 65 DDRlvasngkliVPPEDRK-----IGMVF-QTWALYPNLTAFENiaFPLtNMKM---SKEEIRKRVEEVAKILDIHHVLN 135
Cdd:COG4586 82 LGY---------VPFKRRKefarrIGVVFgQRSQLWWDLPAIDS--FRL-LKAIyriPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 136 HFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLV 215
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVID 229
|
....*
gi 499226461 216 KGKLV 220
Cdd:COG4586 230 HGRII 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-220 |
2.72e-38 |
|
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: 136.18 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlvaSNGKLIVPPEDR 82
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG----TDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 K-IGMVFQTWALYpNLTAFENIAFPLTNmkmSKEEirkRVEEVAKILDIHHVLNHFP-----------RELSGGQQQRVA 150
Cdd:cd03245 78 RnIGYVPQDVTLF-YGTLRDNITLGAPL---ADDE---RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARmrdSARALVKEVQSRL-GVTLLVVSHDPAdIFAIADRVGVLVKGKLV 220
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMN---SEERLKERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-228 |
5.95e-38 |
|
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: 142.25 E-value: 5.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF---KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYF---DDRL-VASNGKLI 76
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEWVdMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 VPPEDRKIGMVFQTWALYPNLTAFEN------IAFPLTNMKMSKEEIRKRV---EEVAKildihHVLNHFPRELSGGQQQ 147
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITLKMVgfdEEKAE-----EILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
.
gi 499226461 228 L 228
Cdd:TIGR03269 515 I 515
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
1.23e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.77 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKKGKVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV--------ASN 72
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVV--KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 73 GklivppedrkIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALA 152
Cdd:COG1137 79 G----------IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 153 RALVKDPSLLLLDEPFSNLD----ARMRDsaraLVKEVQSR-LGVtlLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDpiavADIQK----IIRHLKERgIGV--LITDHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
250
....*....|
gi 499226461 228 LYDNPVSIQV 237
Cdd:COG1137 223 ILNNPLVRKV 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
1.24e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 135.26 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKkGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTG-----ELYFDDRLVASNGKL 75
Cdd:PRK11264 1 MSAIEVKNLVKKFH-GQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 76 IVPPEDRKIGMVFQTWALYPNLTAFEN-IAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 155 LVKDPSLLLLDEPFSNLDARM----RDSARALVKEVQsrlgvTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELvgevLNTIRQLAQEKR-----TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
..
gi 499226461 231 NP 232
Cdd:PRK11264 234 DP 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
7.29e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 133.66 E-value: 7.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKKGKVVA-------LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNG 73
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 74 KLIVPPEDRKIGMVFQ--TWALYPNLTAFENIAFPLTNM-KMSKEEIRKRVEEVAKILDIH-HVLNHFPRELSGGQQQRV 149
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQdsISAVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQ 221
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-234 |
1.03e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 136.70 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--SNGKLiVPPEDRKIGMVFQTW 91
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAEL-REVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 ALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNL 171
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 172 DARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVS 234
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-227 |
1.47e-36 |
|
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: 138.73 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgklivPPED- 81
Cdd:COG4618 330 RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-----DREEl 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 -RKIGMVFQTWALYPNlTAFENIA-FPltnmkmskEEIRKRVEEVAKILDIHHVLNHFP-----------RELSGGQQQR 148
Cdd:COG4618 405 gRHIGYLPQDVELFDG-TIAENIArFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPAdIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
2.72e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 131.96 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGL-----DVPSTGELYFDDRLVAsngKL 75
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF---KM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 76 IVPPEDRKIGMVFQTWALYPNLTAFENIAF--PLTNMKMSKEEIRKRVE---EVAKILD-IHHVLNHFPRELSGGQQQRV 149
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPIPNLSIFENVALglKLNRLVKSKKELQERVRwalEKAQLWDeVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLgvTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLY 229
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
...
gi 499226461 230 DNP 232
Cdd:PRK14247 234 TNP 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
5.80e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 130.95 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELyfddrlVASNGKLIVPPEDrk 83
Cdd:PRK11247 13 LLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEARED-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLtnmkmsKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-257 |
7.80e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.03 E-value: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKlivpPEDRK 83
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF----EKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 -IGMVFQTwalyP------NLTAFEnIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV 156
Cdd:PRK13648 84 hIGIVFQN----PdnqfvgSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDLY------- 229
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFdhaeelt 237
|
250 260 270
....*....|....*....|....*....|..
gi 499226461 230 ----DNPVSIQVASLIGEINELegkVTNEGVV 257
Cdd:PRK13648 238 riglDLPFPIKINQMLGHQTSF---LTYEGLV 266
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-223 |
1.33e-35 |
|
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: 129.19 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVF--------------------KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEly 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 64 fddrlVASNGKLIVPPEdrkIGMVFQtwalyPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSG 143
Cdd:cd03220 79 -----VTVRGRVSSLLG---LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 144 GQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-232 |
2.29e-35 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 128.93 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDR 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVV--NDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH-----LPMHER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 K---IGMVFQTWALYPNLTAFENIAFPL-TNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:TIGR04406 74 ArlgIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-233 |
2.67e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.92 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 36 ILGPSGAGKTTFMRIIAGLDVPSTGELYFDDR-LVASNGKLIVPPEDRKIGMVFQTWALYPNLTAFENIAFPLtnmkmsK 114
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM------A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 115 EEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDA-RMRD---SARALVKEVQsrl 190
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKREllpYLERLAREIN--- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499226461 191 gVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPV 233
Cdd:PRK11144 180 -IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-257 |
5.73e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.98 E-value: 5.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgklIVPPEDRK 83
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE---TVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTwalyPN-----LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:PRK13635 83 VGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLY--------- 229
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHD-LDEAAQADRVIVMNKGEILEEGTPEEIFksghmlqei 237
|
250 260 270
....*....|....*....|....*....|..
gi 499226461 230 --DNPVSIQVASLI--GEINELEGKVTNEGVV 257
Cdd:PRK13635 238 glDVPFSVKLKELLkrNGILLPNTYLTMESLV 269
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-219 |
7.75e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 127.20 E-value: 7.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYF-DDRLVASNGKLIVPPEDRKIGMVFQTWALYPNLTA 99
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 100 FENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSA 179
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499226461 180 RALVKEVQSRLGVTLLVVSHDPaDIFAIADRVGVLVKGKL 219
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-211 |
9.90e-35 |
|
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: 126.78 E-value: 9.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK----KGK-VVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELyfddrLVASNGKLI-- 76
Cdd:COG4778 5 LEVENLSKTFTlhlqGGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-----LVRHDGGWVdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 --VPPED----RK--IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNH-FPRELSGGQQQ 147
Cdd:COG4778 80 aqASPREilalRRrtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRV 211
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
1.06e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.60 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS---NGKLiv 77
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkkNKKL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 78 PPEDRKIGMVFQtwalYPNLTAFE-----NIAFPLTNMKMSKEEIRKRVEEVAKILDI-HHVLNHFPRELSGGQQQRVAL 151
Cdd:PRK13634 81 KPLRKKVGIVFQ----FPEHQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 152 ARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
.
gi 499226461 232 P 232
Cdd:PRK13634 237 P 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-229 |
1.26e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 128.32 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVV---ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGK-LIVPP 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRKIGMVFQtwalYPNLTAFE-----NIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVL-NHFPRELSGGQQQRVALAR 153
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQsRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLY 229
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-200 |
1.43e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 132.50 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGElyfddrlvasngklIVPPEDRKIG 85
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE--------------VSIPKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTWALYPNLTAFENI--AF-PLTNMKMSKEEIRKRV----EEVAKILDIHHVLNH------------------FP-- 138
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTVldGDaELRALEAELEELEAKLaepdEDLERLAELQEEFEAlggweaearaeeilsglgFPee 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 139 ------RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRLGvTLLVVSHD 200
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPG-TVLVVSHD 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-227 |
1.95e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.15 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSkvFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED-- 81
Cdd:COG4559 2 LEAENLS--VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA-----WSPWEla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV----- 156
Cdd:COG4559 75 RRRAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 157 --KDPSLLLLDEPFSNLD-----ARMRdSARALVKEvqsrlGVTLLVVSHDP--ADIFaiADRVGVLVKGKLVQVGKPED 227
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDlahqhAVLR-LARQLARR-----GGGVVAVLHDLnlAAQY--ADRILLLHQGRLVAQGTPEE 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-232 |
3.43e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 126.32 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDvpstgELYfdDRLVASNGKLIVPPED----------RKIGMVFQT 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI-----EIY--DSKIKVDGKVLYFGKDifqidaiklrKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 91 WALYPNLTAFENIAFPLTNMKMS-KEEIRKRVEEVAKIL----DIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLD 165
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 166 EPFSNLDARMRDSARALVKEVQSRlgVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-228 |
4.30e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 131.46 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKkGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDV--PSTGELYFDDRLVASNGKLIVPPED 81
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEV-LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHVALCEKCGYVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 ------------------------------RKIGMVFQ-TWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDI 130
Cdd:TIGR03269 79 gepcpvcggtlepeevdfwnlsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 131 HHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADR 210
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....*...
gi 499226461 211 VGVLVKGKLVQVGKPEDL 228
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV 256
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-220 |
6.09e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.29 E-value: 6.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlVASNGKLIvppedRKIG 85
Cdd:cd03226 2 IENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK-PIKAKERR-----KSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTwalyPNLTAFENIAFP---LTNMKMSKEEirKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLL 162
Cdd:cd03226 75 YVMQD----VDYQLFTDSVREellLGLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 163 LLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-229 |
7.97e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 126.43 E-value: 7.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGK-LIVPP 79
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRKIGMVFQtwalYPNLTAFEN-----IAFPLTNMKMSKEEIRKRVEEVakILDI---HHVLNHFPRELSGGQQQRVAL 151
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRL--LMDLgfsRDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 152 ARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLY 229
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-247 |
1.40e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 125.35 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVppEDRK-IGMVFQTwalyPN-- 96
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM--KLREsVGMVFQD----PDnq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 97 ---LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDA 173
Cdd:PRK13636 95 lfsASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 174 RMRDSARALVKEVQSRLGVTLLVVSHDpADIFAI-ADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL----IGEINEL 247
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHD-IDIVPLyCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLrlprIGHLMEI 252
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-228 |
1.68e-33 |
|
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: 123.88 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsngKLIVPPEDRK 83
Cdd:cd03253 1 IEFENVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR---EVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYpNLTAFENIAFplTNMKMSKEEirkrVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVALA 152
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIRY--GRPDATDEE----VIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARM-RDSARALVKEVQSRlgvTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTeREIQAALRDVSKGR---TTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-220 |
1.79e-33 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 130.76 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlvaSNGKLIvPPED--RKI 84
Cdd:TIGR03375 467 RNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG----VDIRQI-DPADlrRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 GMVFQTWALYpNLTAFENIAF--PLTnmkmSKEEIRkrveEVAKILDIHHVLNHFP-----------RELSGGQQQRVAL 151
Cdd:TIGR03375 542 GYVPQDPRLF-YGTLRDNIALgaPYA----DDEEIL----RAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVAL 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 152 ARALVKDPSLLLLDEPFSNLDARmrdSARALVKEVQSRL-GVTLLVVSHDPAdIFAIADRVGVLVKGKLV 220
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNR---SEERFKDRLKRWLaGKTLVLVTHRTS-LLDLVDRIIVMDNGRIV 678
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
3.87e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.07 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRII-VKNVSKVFKKGKV-VALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFD-DRLVASNgkliV 77
Cdd:PRK13650 1 MSNIIeVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgDLLTEEN----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 78 PPEDRKIGMVFQTwalyPN-----LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALA 152
Cdd:PRK13650 77 WDIRHKIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLY 229
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-232 |
3.92e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.46 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRKIGMVFQT--W 91
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 ALYPNLTAFENIAFPLT-NMKMSKEEIRKRVEEV-AKI-LDIHHVlNHFPRELSGGQQQRVALARALVKDPSLLLLDEPF 168
Cdd:PRK11308 104 SLNPRKKVGQILEEPLLiNTSLSAAERREKALAMmAKVgLRPEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 169 SNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-262 |
6.77e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.65 E-value: 6.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEdRKIG 85
Cdd:PRK13639 4 TRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVR-KTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTwalyPNLTAF-----ENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK13639 82 IVFQN----PDDQLFaptveEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQ---- 236
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRkanl 236
|
250 260 270
....*....|....*....|....*....|
gi 499226461 237 ----VASLIGEINELEGKVTNEGVVIGSLR 262
Cdd:PRK13639 237 rlprVAHLIEILNKEDNLPIKMGYTIGEAR 266
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-274 |
6.98e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.31 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRII-VKNVSKVFKKGkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV-ASNGKLIvp 78
Cdd:PRK13647 1 MDNIIeVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 peDRKIGMVFQTwalyPN-----LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALAR 153
Cdd:PRK13647 78 --RSKVGLVFQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN-- 231
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEdi 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499226461 232 --------PVSIQVASLIGEinelegkvtnegvvIGSLRFPVSVSSDRAII 274
Cdd:PRK13647 231 veqaglrlPLVAQIFEDLPE--------------LGQSKLPLTVKEAVQII 267
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-232 |
1.07e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 122.26 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDvpstgELYFDDRL---VASNGKLIVPPE------DRKIGMVFQTW 91
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLL-----ELNEEARVegeVRLFGRNIYSPDvdpievRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 ALYPNLTAFENIAF--PLTNMKMSKEEIRKRVEEVAKIL----DIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLD 165
Cdd:PRK14267 95 NPFPHLTIYDNVAIgvKLNGLVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 166 EPFSNLDARMRDSARALVKEVQSRLgvTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-230 |
1.12e-32 |
|
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: 121.82 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsngklIVPPE--D 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-----LADPAwlR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYpNLTAFENIAfpLTNMKMSKEeirkRVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVA 150
Cdd:cd03252 76 RQVGVVLQENVLF-NRSIRDNIA--LADPGMSME----RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRL-GVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDLY 229
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDY---ESEHAIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
.
gi 499226461 230 D 230
Cdd:cd03252 225 A 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-214 |
1.15e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 127.40 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlvasngKLIVPPED- 81
Cdd:TIGR02857 321 SLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV------PLADADADs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 --RKIGMVFQTWALYPNlTAFENIAFPLTNMkmSKEEIRKRVEEVAkiLD---------IHHVLNHFPRELSGGQQQRVA 150
Cdd:TIGR02857 394 wrDQIAWVPQHPFLFAG-TIAENIRLARPDA--SDAEIREALERAG--LDefvaalpqgLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 151 LARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKevqsrlGVTLLVVSHDPADIfAIADRVGVL 214
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDaeteAEVLEALRALAQ------GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-228 |
1.83e-32 |
|
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: 121.18 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlvasNGKLIVPPEDR 82
Cdd:cd03254 2 EIEFENVNFSYDEKKPV-LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 K-IGMVFQTWALYPNlTAFENIafpltnmKMSKEEIR-KRVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRV 149
Cdd:cd03254 77 SmIGVVLQDTFLFSG-TIMENI-------RLGRPNATdEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDARMrdsaRALVKEVQSRL--GVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPED 227
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTET----EKLIQEALEKLmkGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDE 223
|
.
gi 499226461 228 L 228
Cdd:cd03254 224 L 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-219 |
2.02e-32 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 119.24 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivPPEDRK 83
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD----PNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 -IGMVFQTWALYPNLTAfENIafpltnmkmskeeirkrveevakildihhvlnhfpreLSGGQQQRVALARALVKDPSLL 162
Cdd:cd03246 77 hVGYLPQDDELFSGSIA-ENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 163 LLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIfAIADRVGVLVKGKL 219
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-260 |
2.34e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 122.12 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGK----VVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrLVASNGKLIVPP 79
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-LDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EdRKIGMVFQTwalyPN--LTAF---ENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:PRK13633 84 R-NKAGMVFQN----PDnqIVATiveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSH--DPAdifAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHymEEA---VEADRIIVMDSGKVVMEGTPKEIFKEV 235
|
250 260
....*....|....*....|....*....
gi 499226461 233 VSIQVASL-IGEINELEGKVTNEGVVIGS 260
Cdd:PRK13633 236 EMMKKIGLdVPQVTELAYELKKEGVDIPS 264
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-234 |
2.71e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 121.61 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 8 NVSKVFKK-GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA----SNGKLIVPPEDR 82
Cdd:PRK10619 7 NVIDLHKRyGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKVADKNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 ------KIGMVFQTWALYPNLTAFENI-AFPLTNMKMSKEEIRKR-VEEVAKILDIHHVLNHFPRELSGGQQQRVALARA 154
Cdd:PRK10619 87 lrllrtRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVS 234
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
3.20e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.50 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGE---LYFDDRLVASNGKLI 76
Cdd:PRK13651 2 QIKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 VPPED------------------RKIGMVFQtWALYP--NLTAFENIAFPLTNMKMSKEEIRKRVEEVAKI--LDIHHvL 134
Cdd:PRK13651 82 KVLEKlviqktrfkkikkikeirRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELvgLDESY-L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 135 NHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*...
gi 499226461 215 VKGKLVQVGKPED-LYDN 231
Cdd:PRK13651 239 KDGKIIKDGDTYDiLSDN 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-223 |
4.59e-32 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 118.81 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAG-LDVPST-GElyfddrlVASNGKLIVPPED 81
Cdd:cd03213 9 LTVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGE-------VLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RK-IGMVFQTWALYPNLTAFENIAFpltnmkmskeeirkrveeVAKIldihhvlnhfpRELSGGQQQRVALARALVKDPS 160
Cdd:cd03213 81 RKiIGYVPQDDILHPTLTVRETLMF------------------AAKL-----------RGLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 161 LLLLDEPFSNLDARM-RDSARALVKEVQSrlGVTLLVVSHDP-ADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03213 132 LLFLDEPTSGLDSSSaLQVMSLLRRLADT--GRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-220 |
1.20e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.61 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFKKGK--VVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS-NGKLIVPPEDRK 83
Cdd:PRK10535 8 KDIRRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPaDIFAIADRVGVLVKGKLV 220
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDP-QVAAQAERVIEIRDGEIV 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-242 |
1.38e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.48 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKkGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLivppE 80
Cdd:PRK13536 39 TVAIDLAGVSKSYG-DKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL----A 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 161 LLLLDEPFSNLDARmrdsARALVKE-VQSRL--GVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQV 237
Cdd:PRK13536 193 LLILDEPTTGLDPH----ARHLIWErLRSLLarGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQV 268
|
....*
gi 499226461 238 ASLIG 242
Cdd:PRK13536 269 IEIYG 273
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-232 |
1.64e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.93 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASN-GKLIVPP 79
Cdd:PRK13641 3 IKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRKIGMVFQtwalYPNLTAFEN-----IAFPLTNMKMSKEEIR-KRVEEVAKILDIHHVLNHFPRELSGGQQQRVALAR 153
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAKeKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQsRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-258 |
1.67e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 119.71 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIivKNVSKVFKKGkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLivpPE 80
Cdd:PRK13644 1 MIRL--ENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKL---QG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKI-GMVFQT-WALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:PRK13644 75 IRKLvGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 159 PSLLLLDEPFSNLDArmrDSARALVKEVQS--RLGVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDLYDNP---- 232
Cdd:PRK13644 155 PECLIFDEVTSMLDP---DSGIAVLERIKKlhEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVslqt 230
|
250 260
....*....|....*....|....*.
gi 499226461 233 VSIQVASLIgeinELEGKVTNEGVVI 258
Cdd:PRK13644 231 LGLTPPSLI----ELAENLKMHGVVI 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-230 |
1.95e-31 |
|
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: 118.49 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkLIVPPEDRK 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD---YTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYpNLTAFENIAFPLTNmkmskeEIRKRVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVALA 152
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAYGRPG------ATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARmrdSARaLVKEVQSRL--GVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:cd03251 151 RALLKDPPILILDEATSALDTE---SER-LVQAALERLmkNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEELLA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-232 |
2.76e-31 |
|
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: 123.64 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGK--VVALDNVNINIENGERFGILGPSGAGKT----TFMRIIAGLDVPSTGELYFDDRLVasngkLIVPP 79
Cdd:COG4172 9 VEDLSVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL-----LGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 ED------RKIGMVFQ---TwALYPNLTAFENIAFPLT-NMKMSKEEIRKRV----EEVaKILDIHHVLNHFPRELSGGQ 145
Cdd:COG4172 84 RElrrirgNRIAMIFQepmT-SLNPLHTIGKQIAEVLRlHRGLSGAAARARAlellERV-GIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 146 QQRVALARALVKDPSLLLLDEPFSNLD----ARMRDsaraLVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQ 221
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDvtvqAQILD----LLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
250
....*....|.
gi 499226461 222 VGKPEDLYDNP 232
Cdd:COG4172 238 QGPTAELFAAP 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-231 |
6.99e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 118.57 E-value: 6.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKG---KVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE 80
Cdd:PRK13645 7 IILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 D--RKIGMVFQtwalYPNLTAFE-----NIAFPLTNMKMSKEEIRKRVEEVAKILDI-HHVLNHFPRELSGGQQQRVALA 152
Cdd:PRK13645 87 RlrKEIGLVFQ----FPEYQLFQetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-229 |
9.14e-31 |
|
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: 116.87 E-value: 9.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSkvF---KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlvaSNGKLIVPPE 80
Cdd:cd03249 1 IEFKNVS--FrypSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DR-KIGMVFQTWALYPNlTAFENIAFPLTNMKMskEEirkrVEEVAKILDIHHVLNHFPR-----------ELSGGQQQR 148
Cdd:cd03249 75 LRsQIGLVSQEPVLFDG-TIAENIRYGKPDATD--EE----VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDARmrdsARALVKE--VQSRLGVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPE 226
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAE----SEKLVQEalDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHD 222
|
...
gi 499226461 227 DLY 229
Cdd:cd03249 223 ELM 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-223 |
1.51e-30 |
|
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: 115.83 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 10 SKVFKKGKVV-ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPSTGELYFDdrlVASNGKLIVPPEDRK-IGMV 87
Cdd:cd03234 11 LKAKNWNKYArILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTSGQ---ILFNGQPRKPDQFQKcVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 88 FQTWALYPNLTAFENIAF--PLTNMKMSKEEIRKRVEEVAKILDIHH--VLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03234 87 RQDDILLPGLTVRETLTYtaILRLPRKSSDAIRKKRVEDVLLRDLALtrIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 164 LDEPFSNLDARmrdSARALVKEVQ--SRLGVTLLVVSHDP-ADIFAIADRVGVLVKGKLVQVG 223
Cdd:cd03234 167 LDEPTSGLDSF---TALNLVSTLSqlARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-231 |
1.99e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.15 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFKKGKVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsngklIVPPE 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVV--EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS-----LLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRK---IGMVFQTWALYPNLTAFENIAFPLTNMK-MSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV 156
Cdd:PRK10895 74 ARArrgIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-227 |
2.15e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSkVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED 81
Cdd:PRK13548 1 AMLEARNLS-VRLGGRTL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD-----WSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 --RKIGMVFQTWAL-YPnLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV-- 156
Cdd:PRK13548 74 laRRRAVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 157 ----KDPSLLLLDEPFSNLDAR-----MRdsaraLVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAhqhhvLR-----LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-236 |
9.22e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.41 E-value: 9.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED-- 81
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-----TPSREla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAF---PLTNMKMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKD 158
Cdd:COG4604 75 KRLAILRQENHINSRLTVRELVAFgrfPYSKGRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 159 PSLLLLDEPFSNLDarMRDSA------RALVKEvqsrLGVTLLVVSHdpaDI-FAI--ADRVGVLVKGKLVQVGKPE--- 226
Cdd:COG4604 154 TDYVLLDEPLNNLD--MKHSVqmmkllRRLADE----LGKTVVIVLH---DInFAScyADHIVAMKDGRVVAQGTPEeii 224
|
250
....*....|....*.
gi 499226461 227 ------DLYDNPVSIQ 236
Cdd:COG4604 225 tpevlsDIYDTDIEVE 240
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-228 |
1.00e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 119.37 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDdrlvasnGKLI--VPPE 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD-------GADLkqWDRE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 D--RKIGMVFQTWALYPNLTAfENIAfpltnmKMSKEEIRKRVEEVAKILDIHHVLNHFPR-----------ELSGGQQQ 147
Cdd:TIGR01842 389 TfgKHIGYLPQDVELFPGTVA-ENIA------RFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPAdIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:TIGR01842 462 RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDE 539
|
.
gi 499226461 228 L 228
Cdd:TIGR01842 540 V 540
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-232 |
2.28e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.13 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 15 KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGE-LYFDDRLVASNGKlivppEDRK-IGMVFQTwa 92
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvLIRGEPITKENIR-----EVRKfVGLVFQN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 lyPNLTAF-----ENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEP 167
Cdd:PRK13652 87 --PDDQIFsptveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 168 FSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-242 |
5.45e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivPPEDRK 83
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARmrdsARALVKE-VQSRL--GVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL 240
Cdd:PRK13537 162 LDEPTTGLDPQ----ARHLMWErLRSLLarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEI 237
|
..
gi 499226461 241 IG 242
Cdd:PRK13537 238 YG 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-236 |
5.98e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 112.39 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS-NGKLIVppedRKi 84
Cdd:PRK11300 8 VSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQIA----RM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 GMV--FQTWALYPNLTAFENIAFP------------LTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRE---LSGGQQQ 147
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVAqhqqlktglfsgLLKTPAFRRAESEALDRAATWLERVGLLEHANRQagnLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*....
gi 499226461 228 LYDNPVSIQ 236
Cdd:PRK11300 241 IRNNPDVIK 249
|
|
| GlcV_C_terminal |
pfam17847 |
Glucose ABC transporter C-terminal domain; This is the C-terminal domain found at the ATPase ... |
291-351 |
8.26e-29 |
|
Glucose ABC transporter C-terminal domain; This is the C-terminal domain found at the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus. Overall, the C-terminal domain (residues 243-353) contains only beta-strands, which form an elongated barrel-shaped structure composed of two parts. This entry represents the upper part which includes a three-stranded anti-parallel beta-sheets and two small anti-parallel beta-strands. The overall structure of this domain is very similar to that of the C-terminal domain of MalK from T. litoralis however, the function of the C-terminal domain in GlcV is not clear.
Pssm-ID: 375378 Cd Length: 61 Bit Score: 106.01 E-value: 8.26e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 291 DSWILVGKGKVKVIGYQGGLFRITITPLDSEEEIFTYSDHPIHSGEEVLVYVRKDKIKVFE 351
Cdd:pfam17847 1 DKYINVGKVKVKVVSYQAGIFKITVSPINSEEEISVNSEHPIKTGEEVLLYVRKNKIKIFD 61
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-258 |
2.80e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPstgelyfDDrlvASNGKLIVPPED-- 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLP-------DD---NPNSKITVDGITlt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 --------RKIGMVFQTwalyPN-----LTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQR 148
Cdd:PRK13640 76 aktvwdirEKVGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEI 230
|
250 260 270
....*....|....*....|....*....|.
gi 499226461 229 YDNPVSIQVASL-IGEINELEGKVTNEGVVI 258
Cdd:PRK13640 231 FSKVEMLKEIGLdIPFVYKLKNKLKEKGISV 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-232 |
3.91e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.80 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 19 VALDNVNINIENGERFGILGPSGAGKTT----FMRIIAgldvpSTGELYFDDRLVASNGKLIVPPEDRKIGMVFQ--TWA 92
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 LYPNLTAFENIA------FPLTNMKMSKEEIRKRVEEVAKILDIHHvlnHFPRELSGGQQQRVALARALVKDPSLLLLDE 166
Cdd:PRK15134 375 LNPRLNVLQIIEeglrvhQPTLSAAQREQQVIAVMEEVGLDPETRH---RYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 167 PFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-229 |
8.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.21 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLI-VPPEDRKIGMVFQtwalYPNLT 98
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFE-----NIAFPLTNMKMSKEEIRKRVEEVAKILDI-HHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLD 172
Cdd:PRK13643 97 LFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 173 ARMRDSARALVKEVQsRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLY 229
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-228 |
1.85e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 113.22 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSKVFKKGKVVAldnvniniengerfgILGPSGAGKTTFMRIIAGLDvpSTGELYFDDRLVasNGKLIVPPED 81
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLA---------------VMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLL--NGMPIDAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKI-GMVFQTWALYPNLTAFENIAFpLTNMKM----SKEEIRKRVEEVAK---ILDIHHVLNHFP---RELSGGQQQRVA 150
Cdd:TIGR00955 98 RAIsAYVQQDDLFIPTLTVREHLMF-QAHLRMprrvTKKEKRERVDEVLQalgLRKCANTRIGVPgrvKGLSGGERKRLA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDP-ADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-233 |
2.15e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.94 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGKvvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGL-----DVPSTGELYFddrlvasNGKLIVPP- 79
Cdd:PRK14239 8 VSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVY-------NGHNIYSPr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 ----EDRK-IGMVFQTWALYPnLTAFENIAFPL-TNMKMSKEEIRKRVEEV---AKILD-IHHVLNHFPRELSGGQQQRV 149
Cdd:PRK14239 79 tdtvDLRKeIGMVFQQPNPFP-MSIYENVVYGLrLKGIKDKQVLDEAVEKSlkgASIWDeVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKEvqsrlgVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKP 225
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDpisaGKIEETLLGLKDD------YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
....*...
gi 499226461 226 EDLYDNPV 233
Cdd:PRK14239 232 KQMFMNPK 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-246 |
2.98e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 108.26 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsnGKLIVPPED-----RKIGMVFQT 90
Cdd:PRK14271 33 GKTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG--GRSIFNYRDvlefrRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 91 WALYPnLTAFENI-----AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLD 165
Cdd:PRK14271 110 PNPFP-MSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 166 EPFSNLDARMRDSARALVKEVQSRLgvTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQ----VASLI 241
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAEtaryVAGLS 266
|
....*
gi 499226461 242 GEINE 246
Cdd:PRK14271 267 GDVKD 271
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-218 |
7.09e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.79 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPS---TGELYFD-DRLVASNgklIVPPEDR 82
Cdd:PRK13549 9 KNITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEgEELQASN---IRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNLTAFENI---AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
9-229 |
1.06e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 9 VSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFD-DRLVASNgkliVPPEDRKIGMV 87
Cdd:PRK13642 11 VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgELLTAEN----VWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 88 FQTW-ALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDE 166
Cdd:PRK13642 87 FQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 167 PFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLY 229
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHD-LDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-211 |
1.35e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKkGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEL---------YFD---DRLvas 71
Cdd:COG0488 316 LELEGLSKSYG-DKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigYFDqhqEEL--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 72 ngklivPPEDRkigmVFQT-WALYPNLTAFENIAFpLTNMKMSKEEIRKRVeevakildihhvlnhfpRELSGGQQQRVA 150
Cdd:COG0488 391 ------DPDKT----VLDElRDGAPGGTEQEVRGY-LGRFLFSGDDAFKPV-----------------GVLSGGEKARLA 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARMRDsarALVKEVQSRLGvTLLVVSHDPADIFAIADRV 211
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLE---ALEEALDDFPG-TVLLVSHDRYFLDRVATRI 499
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-232 |
3.06e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 105.26 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFK-------KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvp 78
Cdd:PRK15112 7 VRNLSKTFRyrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 pEDRKIGMVFQ--TWALYPNLTAFENIAFPLT-NMKMSKEEIRKRVEEVAKILDI--HHVlNHFPRELSGGQQQRVALAR 153
Cdd:PRK15112 85 -RSQRIRMIFQdpSTSLNPRQRISQILDFPLRlNTDLEPEQREKQIIETLRQVGLlpDHA-SYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-232 |
4.53e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.43 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDD-RLVASNGKLIvppeDRKIGMVFQTWALYpNLTA 99
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvPLVQYDHHYL----HRQVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 100 FENIAFPLTNMKMskEEIRKrveeVAKILDIHHVLNHFPR-----------ELSGGQQQRVALARALVKDPSLLLLDEPF 168
Cdd:TIGR00958 572 RENIAYGLTDTPD--EEIMA----AAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 169 SNLDARmrdsARALVKEVQSRLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:TIGR00958 646 SALDAE----CEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-211 |
5.00e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdvPSTGElyfddrlvasnGKLIVPPEDR 82
Cdd:COG4178 362 ALALEDLTLRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--WPYGS-----------GRIARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 kigMVFQTWALY-PNLTAFENIAFPLTNMKMSKEEIRKRVEEV--AKILDIHHVLNHFPRELSGGQQQRVALARALVKDP 159
Cdd:COG4178 428 ---VLFLPQRPYlPLGTLREALLYPATAEAFSDAELREALEAVglGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499226461 160 SLLLLDEPFSNLDArmrDSARALVKEVQSRL-GVTLLVVSHDPAdIFAIADRV 211
Cdd:COG4178 505 DWLFLDEATSALDE---ENEAALYQLLREELpGTTVISVGHRST-LAAFHDRV 553
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-225 |
6.20e-26 |
|
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: 109.33 E-value: 6.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRK 83
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV----RQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 164 LDEPFSNLDARMRDSARALVkeVQSRLGVTLLVVSH--DPADIfaIADRVGVLVKGKLVQVGKP 225
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHhmDEADL--LGDRIAIISQGRLYCSGTP 1144
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-230 |
6.67e-26 |
|
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: 108.65 E-value: 6.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlvasngkliVPPED- 81
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG----------HDLADy 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 ------RKIGMVFQTWALYpNLTAFENIAFPLTnmkmsKEEIRKRVEEVAKILDIHHVLNHFPR-----------ELSGG 144
Cdd:TIGR02203 400 tlaslrRQVALVSQDVVLF-NDTIANNIAYGRT-----EQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 145 QQQRVALARALVKDPSLLLLDEPFSNLDArmrDSARaLVKEVQSRL--GVTLLVVSHDPADIfAIADRVGVLVKGKLVQV 222
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDN---ESER-LVQAALERLmqGRTTLVIAHRLSTI-EKADRIVVMDDGRIVER 548
|
....*...
gi 499226461 223 GKPEDLYD 230
Cdd:TIGR02203 549 GTHNELLA 556
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-232 |
6.77e-26 |
|
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: 104.14 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRKI- 84
Cdd:TIGR02323 6 VSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 -----GMVFQTWA--LYPNLTAFENIAFPLT--------NMKMSKEEIRKRVE-EVAKILDIhhvlnhfPRELSGGQQQR 148
Cdd:TIGR02323 84 mrtewGFVHQNPRdgLRMRVSAGANIGERLMaigarhygNIRATAQDWLEEVEiDPTRIDDL-------PRAFSGGMQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKEvqsrLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDvsvqARLLDLLRGLVRD----LGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
....*...
gi 499226461 225 PEDLYDNP 232
Cdd:TIGR02323 233 TDQVLDDP 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-211 |
7.55e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.26 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 13 FKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED--RKIGMVFQT 90
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-----LKPEIyrQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 91 WALYPNlTAFENIAFPLtnmkmskeEIRKRVEEVAKILD-------IHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPW--------QIRNQQPDPAIFLDdlerfalPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499226461 164 LDEPFSNLDarmrDSARALVKEVQSRL----GVTLLVVSHDPADIfAIADRV 211
Cdd:PRK10247 161 LDEITSALD----ESNKHNVNEIIHRYvreqNIAVLWVTHDKDEI-NHADKV 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-214 |
8.06e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 8.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELyfddrLVASNGKLivppedrkigmvfqtwALYP 95
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGGARV----------------AYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 NLTAFENiAFPLT---NMKMSK-----------EEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:NF040873 62 QRSEVPD-SLPLTvrdLVAMGRwarrglwrrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499226461 162 LLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIfAIADRVGVL 214
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-233 |
8.13e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.83 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklIVPPEDRKIG 85
Cdd:PRK15439 14 ARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR----LTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 --MVFQTWALYPNLTAFENIAFPLTNmkmsKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLL 163
Cdd:PRK15439 88 iyLVPQEPLLFPNLSVKENILFGLPK----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSrLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPV 233
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-228 |
1.65e-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: 102.22 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPEDRK---IGMVFQTWA 92
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-----LPPHERAragIAYVPQGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 LYPNLTAFENIafpLTNMKMSKEEIRKRVEEvakILDIHHVLNHF-PR---ELSGGQQQRVALARALVKDPSLLLLDEPF 168
Cdd:TIGR03410 86 IFPRLTVEENL---LTGLAALPRRSRKIPDE---IYELFPVLKEMlGRrggDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 169 SNLDARM-RDSARALvKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:TIGR03410 160 EGIQPSIiKDIGRVI-RRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-240 |
2.93e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.78 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 35 GILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV--ASNGKLIVppeDRKIGMVFQTwalyPNLTAF-----ENIAFPL 107
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLAL---RQQVATVFQD----PEQQIFytdidSDIAFSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 108 TNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQ 187
Cdd:PRK13638 104 RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499226461 188 SRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL 240
Cdd:PRK13638 184 AQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-220 |
3.51e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.87 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivP-----------PEDRKigmvf 88
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS----PrdairagiayvPEDRK----- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 89 qTWALYPNLTAFENIAfpLTNMK-------MSKEEIRKRVEEVAKILDI------HHVlnhfpRELSGGQQQRVALARAL 155
Cdd:COG1129 338 -GEGLVLDLSIRENIT--LASLDrlsrgglLDRRRERALAEEYIKRLRIktpspeQPV-----GNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 156 VKDPSLLLLDEPFSNLD--AR------MRDSARAlvkevqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:COG1129 410 ATDPKVLILDEPTRGIDvgAKaeiyrlIRELAAE---------GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-220 |
5.71e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKV---VALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAsngKLivpPE 80
Cdd:COG1101 2 LELKNLSKTFNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT---KL---PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRK---IGMVFQ-----TwAlyPNLTAFENIA--------FPL---TNMKMsKEEIRKRVEEVAkiLDIHHVLNHFPREL 141
Cdd:COG1101 76 YKRakyIGRVFQdpmmgT-A--PSMTIEENLAlayrrgkrRGLrrgLTKKR-RELFRELLATLG--LGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 142 SGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
6.25e-25 |
|
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: 99.43 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--SNGKLI------VPpEDRKIGmvfqtw 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrSPRDAIragiayVP-EDRKRE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 ALYPNLTAFENIAFPltnmkmskeeirkrveevakildihhvlnhfpRELSGGQQQRVALARALVKDPSLLLLDEPFSNL 171
Cdd:cd03215 88 GLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 172 D--------ARMRDSARAlvkevqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:cd03215 136 DvgakaeiyRLIRELADA---------GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
6.79e-25 |
|
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: 98.29 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLvasngklivppedrK 83
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGmvfqtwalypnltafeniafpltnmkmskeeirkrveevakildihhvlnHFPReLSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03221 65 IG--------------------------------------------------YFEQ-LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSrlgvTLLVVSHDPADIFAIADRV 211
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKI 137
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-247 |
7.98e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.62 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKK---GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV---ASNGKLIVPP 79
Cdd:PRK13631 24 VKNLYCVFDEkqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkKNNHELITNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 EDRKI----------GMVFQtwalYPNLTAFE-----NIAFPLTNMKMSKEEIRKRVEEVAKILDIHH-VLNHFPRELSG 143
Cdd:PRK13631 104 YSKKIknfkelrrrvSMVFQ----FPEYQLFKdtiekDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 144 GQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250 260
....*....|....*....|....*....
gi 499226461 224 KPEDLYDNP-----VSIQVASLIGEINEL 247
Cdd:PRK13631 259 TPYEIFTDQhiinsTSIQVPRVIQVINDL 287
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-223 |
1.88e-24 |
|
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: 98.15 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRK 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL----SSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYpNLTAFENIAfpltnmkmskeeirkrveevakildihhvlnhfpRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSrlGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVG 223
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-220 |
2.76e-24 |
|
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: 103.37 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPST--GELYFDDR-LVASNgklIVPPEDR 82
Cdd:TIGR02633 4 MKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSpLKASN---IRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNLTAFENI----AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFP-RELSGGQQQRVALARALVK 157
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 158 DPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-231 |
2.88e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.09 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKvvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGL---DVPSTGELYFDDRLVASNGKLI--VP 78
Cdd:PRK09984 5 IRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLArdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRKIGMVFQTWALYPNLTAFENI--------AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVA 150
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDArmrDSARAL---VKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDP---ESARIVmdtLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
....
gi 499226461 228 lYDN 231
Cdd:PRK09984 240 -FDN 242
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-233 |
7.20e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.96 E-value: 7.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGL-----DVPSTGELYFDDRLVASNgKLIVP 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKIL--EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYER-RVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRKIGMVFQTWALYPnLTAFENIAFPLTNMKM-SKEEIRKRVEEVAKILD----IHHVLNHFPRELSGGQQQRVALAR 153
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVK-----GKLVQVGKPEDL 228
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
....*
gi 499226461 229 YDNPV 233
Cdd:PRK14258 244 FNSPH 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-232 |
1.20e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.86 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 15 KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV--ASNGKLivPPEDRKIGMVFQT-- 90
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtLSPGKL--QALRRDIQFIFQDpy 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 91 WALYPNLTAFENIAFPL-TNMKMSKEEIRKRVEEVAKILDI--HHVLnHFPRELSGGQQQRVALARALVKDPSLLLLDEP 167
Cdd:PRK10261 412 ASLDPRQTVGDSIMEPLrVHGLLPGKAAAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 168 FSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-232 |
1.38e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 98.07 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlvasNGKL-----IVPPE 80
Cdd:PRK11701 9 VRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR----DGQLrdlyaLSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKI-----GMVFQTWA--LYPNLTAFENIAFPLtnMKMSKE---EIR-------KRVE-EVAKILDihhvlnhFPRELS 142
Cdd:PRK11701 83 RRRLlrtewGFVHQHPRdgLRMQVSAGGNIGERL--MAVGARhygDIRatagdwlERVEiDAARIDD-------LPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 143 GGQQQRVALARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKEvqsrLGVTLLVVSHDPADIFAIADRVGVLVKGK 218
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRE----LGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250
....*....|....
gi 499226461 219 LVQVGKPEDLYDNP 232
Cdd:PRK11701 230 VVESGLTDQVLDDP 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-228 |
2.68e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSkVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV--ASNGKLI------V 77
Cdd:COG3845 260 VENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItgLSPRERRrlgvayI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 78 pPEDRkigmvfQTWALYPNLTAFENIAF------PLTNMK-MSKEEIRKRVEEVAKILDI-HHVLNHFPRELSGGQQQRV 149
Cdd:COG3845 339 -PEDR------LGRGLVPDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLD--------ARMRDSARAlvkevqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQ 221
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDvgaiefihQRLLELRDA---------GAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
....*..
gi 499226461 222 VGKPEDL 228
Cdd:COG3845 483 EVPAAEA 489
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
2.92e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.53 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASN-----GKL 75
Cdd:PRK09536 1 MPMIDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraaSRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 76 IVP-PEDRKIGMVFQTWAL-----YPNLTAFENiafpltnmkmSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRV 149
Cdd:PRK09536 79 VASvPQDTSLSFEFDVRQVvemgrTPHRSRFDT----------WTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLD----ARMRDSARALVKEvqsrlGVTLLVVSHDpADIFA-IADRVGVLVKGKLVQVGK 224
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDinhqVRTLELVRRLVDD-----GKTAVAAIHD-LDLAArYCDELVLLADGRVRAAGP 222
|
....
gi 499226461 225 PEDL 228
Cdd:PRK09536 223 PADV 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
5.33e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSKVFKKGKVVAlDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPSTGELyfddrLVasNG---KLIVP 78
Cdd:PRK11174 348 VTIEAEDLEILSPDGKTLA-GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSL-----KI--NGielRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDRK-IGMVFQTwalyPNL---TAFENIAfpLTNMKMSKEEIRKRVEEvAKILDI----HHVLNHFPRE----LSGGQQ 146
Cdd:PRK11174 419 ESWRKhLSWVGQN----PQLphgTLRDNVL--LGNPDASDEQLQQALEN-AWVSEFlpllPQGLDTPIGDqaagLSVGQA 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 147 QRVALARALVKDPSLLLLDEPFSNLDARmrdSARALVKEVQS-RLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKP 225
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAH---SEQLVMQALNAaSRRQTTLMVTHQLEDL-AQWDQIWVMQDGQIVQQGDY 567
|
...
gi 499226461 226 EDL 228
Cdd:PRK11174 568 AEL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-201 |
1.08e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkLIVPPEDRKIGMVFQTWALYp 95
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS---LDQDEVRRRVSVCAQDAHLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 NLTAFENIAfpLTNMKMSKEEIRKRVEEV--AKILD-----IHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPF 168
Cdd:TIGR02868 422 DTTVRENLR--LARPDATDEELWAALERVglADWLRalpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|....
gi 499226461 169 SNLDArmrDSARALVKEVQSRL-GVTLLVVSHDP 201
Cdd:TIGR02868 500 EHLDA---ETADELLEDLLAALsGRTVVLITHHL 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-228 |
1.55e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.32 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDR--------LVASNGkl 75
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhkLAAQLG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 76 ivppedrkIGMVFQTWALYPNLTAFENI-----------AFPLTNMKmskeEIRKRVEEVAKILDIHHVLNHFPRELSGG 144
Cdd:PRK09700 82 --------IGIIYQELSVIDELTVLENLyigrhltkkvcGVNIIDWR----EMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 145 QQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
....
gi 499226461 225 PEDL 228
Cdd:PRK09700 229 VSDV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-200 |
1.74e-22 |
|
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: 98.47 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGElyfddrlvasngklIVPPEDRKIGM 86
Cdd:TIGR03719 8 NRVSKVVPPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------------ARPQPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 87 VFQTWALYPNLTAFENIA------------FPLTNMKMSKE--EIRKRVEEVAKILDI----------------HHVLNH 136
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEegvaeikdaldrFNEISAKYAEPdaDFDKLAAEQAELQEIidaadawdldsqleiaMDALRC 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 137 FPRE-----LSGGQQQRVALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRLGvTLLVVSHD 200
Cdd:TIGR03719 153 PPWDadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-221 |
2.10e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.06 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 8 NVSKVFKKgkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV--ASNGKLIvppeDRKIG 85
Cdd:PRK11288 9 GIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAAL----AAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQTWALYPNLTAFENI-------AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLnhfpRELSGGQQQRVALARALVKD 158
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPL----KYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 159 PSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQ 221
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-211 |
2.92e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.03 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLvasngklivppedrK 83
Cdd:PRK09544 5 VSLENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL--------------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLtafeniafPLTN---MKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS 160
Cdd:PRK09544 69 IGYVPQKLYLDTTL--------PLTVnrfLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRV 211
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-232 |
3.04e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.56 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFK--KGKVVALDNVNINIENGERFGILGPSGAGK--TTF--MRIIAGLDVpSTGELYFddrlvasNGKLIVP- 78
Cdd:PRK09473 15 VKDLRVTFStpDGDVTAVNDLNFSLRAGETLGIVGESGSGKsqTAFalMGLLAANGR-IGGSATF-------NGREILNl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PEDR-------KIGMVFQ--TWALYPNLTAFENIAFPLTNMK-MSKEEIrkrVEEVAKILDI------HHVLNHFPRELS 142
Cdd:PRK09473 87 PEKElnklraeQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKgMSKAEA---FEESVRMLDAvkmpeaRKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 143 GGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQV 222
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250
....*....|
gi 499226461 223 GKPEDLYDNP 232
Cdd:PRK09473 244 GNARDVFYQP 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-205 |
3.06e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.01 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVfkKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlvasngklivPPEDR 82
Cdd:PRK13539 2 MLEGEDLACV--RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG----------DIDDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTW----ALYPNLTAFENIAFpLTNMKMSKEEirkRVEEVAKILDIHHVLnHFP-RELSGGQQQRVALARALVK 157
Cdd:PRK13539 70 DVAEACHYLghrnAMKPALTVAENLEF-WAAFLGGEEL---DIAAALEAVGLAPLA-HLPfGYLSAGQKRRVALARLLVS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499226461 158 DPSLLLLDEPFSNLDArmrdSARALVKE-VQSRL--GVTLLVVSHDPADIF 205
Cdd:PRK13539 145 NRPIWILDEPTAALDA----AAVALFAElIRAHLaqGGIVIAATHIPLGLP 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-199 |
6.18e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.12 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGE-LYFddrlvasnGKLiVPPED- 81
Cdd:NF033858 267 IEARGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLF--------GQP-VDAGDi 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 ---RKIGMVFQTWALYPNLTAFENIA-----FpltnmKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALAR 153
Cdd:NF033858 336 atrRRVGYMSQAFSLYGELTVRQNLElharlF-----HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSH 199
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-314 |
9.32e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.46 E-value: 9.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFK--KGKVVALDNVNINIENGERFGILGPSGAGKT----TFMRII--AGLDVPSTGELyfddrLVASNGKL 75
Cdd:PRK10261 13 LAVENLNIAFMqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKML-----LRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 76 IVPPEDRK----------IGMVFQ--TWALYPNLTAFENIAFPLT-NMKMSKEEI---RKRVEEVAKILDIHHVLNHFPR 139
Cdd:PRK10261 88 IELSEQSAaqmrhvrgadMAMIFQepMTSLNPVFTVGEQIAESIRlHQGASREEAmveAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 140 ELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 220 VQVGKPEDLYDNPVSIQVASLIGEINELegkvtneGVVIGS---LRFPVsVSSDRAiigiRPEDVKLSKDVIKDDSWILV 296
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVPQL-------GAMKGLdypRRFPL-ISLEHP----AKQEPPIEQDTVVDGEPILQ 315
|
330
....*....|....*....
gi 499226461 297 GKGKVKVIGYQGGLF-RIT 314
Cdd:PRK10261 316 VRNLVTRFPLRSGLLnRVT 334
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-202 |
1.47e-21 |
|
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: 89.91 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPSTgelyfddrlvasNGKLIVPpEDRK 83
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL-WPWG------------SGRIGMP-EGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTwALYPNLTAFENIAFPLTnmkmskeeirkrveevakildihhvlnhfpRELSGGQQQRVALARALVKDPSLLL 163
Cdd:cd03223 66 LLFLPQR-PYLPLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 499226461 164 LDEPFSNLDARMRDSARALVKEvqsrLGVTLLVVSHDPA 202
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE----LGITVISVGHRPS 149
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-244 |
2.60e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALdnvniniengerfgiLGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivppeDR 82
Cdd:PRK11231 15 KRILNDLSLSLPTGKITAL---------------IGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS-------SR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGmvfQTWALYPN-LTAFENIAF---------PLTNM--KMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVA 150
Cdd:PRK11231 73 QLA---RRLALLPQhHLTPEGITVrelvaygrsPWLSLwgRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
250
....*....|....
gi 499226461 231 NPVSIQVASLIGEI 244
Cdd:PRK11231 228 PGLLRTVFDVEAEI 241
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-232 |
3.29e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.66 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 15 KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPS---TGelyfdDRLVASNGKLI-VPPEDRK------I 84
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvTA-----DRFRWNGIDLLkLSPRERRkiigreI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 GMVFQ--TWALYPNLTAFENI--AFP---LTNMKMSKEEIRKR--VEEVAK--ILDIHHVLNHFPRELSGGQQQRVALAR 153
Cdd:COG4170 92 AMIFQepSSCLDPSAKIGDQLieAIPswtFKGKWWQRFKWRKKraIELLHRvgIKDHKDIMNSYPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 154 ALVKDPSLLLLDEPFSNLDARMRDSA-RALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIfRLLARLNQLQ-GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-228 |
3.54e-21 |
|
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: 94.50 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED--RKIGMVFQTWALYpNLT 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD-----VTQASlrAAIGIVPQDTVLF-NDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFPLTNMkmSKEEirkrVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVALARALVKDPSLLLLDEP 167
Cdd:COG5265 448 IAYNIAYGRPDA--SEEE----VEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 168 FSNLDARMRdsaralvKEVQSRL-----GVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:COG5265 522 TSALDSRTE-------RAIQAALrevarGRTTLVIAHRLSTI-VDADEILVLEAGRIVERGTHAEL 579
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-265 |
3.93e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPpedRKIGMVFQTWALYP 95
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 NLTAFENIA---FPLTNMKMS-KEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNL 171
Cdd:PRK10253 95 DITVQELVArgrYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 172 DARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDlydnpvsIQVASLIGEINELEGKV 251
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE-------IVTAELIERIYGLRCMI 247
|
250
....*....|....
gi 499226461 252 TNEGVVIGSLRFPV 265
Cdd:PRK10253 248 IDDPVAGTPLVVPL 261
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
3.99e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 92.50 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVF--KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGL-DVP---STGELYFDDRlvasNGK 74
Cdd:PRK11022 1 MALLNVDKLSVHFgdESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQ----DLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 75 LIVPPEDRKI-----GMVFQ--TWALYPNLTAFENIAFPL-TNMKMSKEEIRKRVEEVAK---ILDIHHVLNHFPRELSG 143
Cdd:PRK11022 77 RISEKERRNLvgaevAMIFQdpMTSLNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNqvgIPDPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 144 GQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVG 223
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*....
gi 499226461 224 KPEDLYDNP 232
Cdd:PRK11022 237 KAHDIFRAP 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-227 |
6.46e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 93.79 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 31 GERFGILGPSGAGKTTFMRIIAGlDVPSTGelyFDDRLVASNGKlIVPPEDRKIGMVFQTWALYPNLTAFENIAF----- 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG-RIQGNN---FTGTILANNRK-PTKQILKRTGFVTQDDILYPHLTVRETLVFcsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 106 -PLTnmkMSKEEIRKRVEEVAKILDIHH-----VLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDArmrDSA 179
Cdd:PLN03211 169 lPKS---LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA---TAA 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499226461 180 RALVKEVQS--RLGVTLLVVSHDPAD-IFAIADRVGVLVKGKLVQVGKPED 227
Cdd:PLN03211 243 YRLVLTLGSlaQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-173 |
8.26e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.09 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 22 DNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFddrlvasNGKLIvppedRKIGMVFQTWALY------- 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW-------QGEPI-----RRQRDEYHQDLLYlghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 95 -PNLTAFENIAFpltNMKMSKEeirkrVEEVAkildIHHVLNHF--------P-RELSGGQQQRVALARALVKDPSLLLL 164
Cdd:PRK13538 86 kTELTALENLRF---YQRLHGP-----GDDEA----LWEALAQVglagfedvPvRQLSAGQQRRVALARLWLTRAPLWIL 153
|
....*....
gi 499226461 165 DEPFSNLDA 173
Cdd:PRK13538 154 DEPFTAIDK 162
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-200 |
1.35e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 88.18 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 15 KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklIVPPEDRKIGMVFQTWALY 94
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDEPHENILYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 95 PNLTAFENIAFPLTNMKMSKEEIRKRVEEVAkILDIHHVLNHFpreLSGGQQQRVALARALVKDPSLLLLDEPFSNLDAR 174
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQRTIEDALAAVG-LTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 499226461 175 MRDSARALVKEVQSRLGVTLLVVSHD 200
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-227 |
1.97e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 28 IENGERFGILGPSGAGKTTFMRIIAGLdVPSTGELYFDDRLVA--SNGKL----------IVPPedrkIGM-VFQTWALY 94
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEawSAAELarhraylsqqQTPP----FAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 95 -PNLTAfeniafpltnmkmsKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVK-DPS------LLLLDE 166
Cdd:PRK03695 94 qPDKTR--------------TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 167 PFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-228 |
2.07e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 92.32 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGlDVPstgelyFDDRLVASNGKLIV------PPEDRKiGMVFQTWA-- 92
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVL------LDDGRIIYEQDLIVarlqqdPPRNVE-GTVYDFVAeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 ---LYPNLTAFENIAFPLTNMKMskEEIRKRVEEVAKILD----------IHHVLNHFP-------RELSGGQQQRVALA 152
Cdd:PRK11147 91 ieeQAEYLKRYHDISHLVETDPS--EKNLNELAKLQEQLDhhnlwqlenrINEVLAQLGldpdaalSSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSrlgvTLLVVSHDPADIFAIADRVGVLVKGKLVQ---------VG 223
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLVSypgnydqylLE 244
|
....*
gi 499226461 224 KPEDL 228
Cdd:PRK11147 245 KEEAL 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-213 |
2.09e-20 |
|
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: 89.00 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 27 NIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDrkiGMVFQTwaLYPNLTAFENIAFP 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYE---GTVRDL--LSSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 107 LTnmkmskeeirkrveEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEV 186
Cdd:cd03237 96 KT--------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180
....*....|....*....|....*..
gi 499226461 187 QSRLGVTLLVVSHDPADIFAIADRVGV 213
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-232 |
2.19e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLD--VPS---TGELYFDDRLVasNGKLIVPPE-DRKIGMVFQ 89
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKNL--YAPDVDPVEvRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 90 TWALYPNlTAFENIAF-PLTN-MKMSKEEIRKRVEEVAKILD-IHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDE 166
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYgARINgYKGDMDELVERSLRQAALWDeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 167 PFSNLDARMRDSARALVKEVQSRLgvTLLVVSHDPADIFAIADRVGVL-VK--------GKLVQVGKPEDLYDNP 232
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnVEltegggryGYLVEFDRTEKIFNSP 250
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-227 |
2.68e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.74 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPSTGELYFDDRLVASngkliVPPED--RKIGMVFQTWALYPNLT 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSD-----WSAAElaRHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFPLTNmKMSKEEIRKRVEEVAKILDI----HHVLNHfpreLSGGQQQRVALARALVK-------DPSLLLLDEP 167
Cdd:COG4138 86 VFQYLALHQPA-GASSEAVEQLLAQLAEALGLedklSRPLTQ----LSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 168 FSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPED 227
Cdd:COG4138 161 MNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-232 |
6.21e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKGKVV--ALDNVNINIENGERFGILGPSGAGKT-TFMRIIAGLDVPS----TGELYF--DDRLVASNGKLi 76
Cdd:PRK15134 8 IENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhgESLLHASEQTL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 vppedR-----KIGMVFQTWALYPNltafeniafPLTNMK------------MSKEEIRKrveEVAKILD---IHHV--- 133
Cdd:PRK15134 87 -----RgvrgnKIAMIFQEPMVSLN---------PLHTLEkqlyevlslhrgMRREAARG---EILNCLDrvgIRQAakr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 134 LNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGV 213
Cdd:PRK15134 150 LTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAV 229
|
250
....*....|....*....
gi 499226461 214 LVKGKLVQVGKPEDLYDNP 232
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSAP 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-173 |
6.68e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.56 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGElyfddrlvasngklIVPPEDRKIGM 86
Cdd:PRK11819 10 NRVSKVVPPKKQI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPAPGIKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 87 VFQTWALYPNLTAFENIA------------FPLTNMKMSKE--EIRKRVEEVAK---ILDIH--HVLNHF---------- 137
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEegvaevkaaldrFNEIYAAYAEPdaDFDALAAEQGElqeIIDAAdaWDLDSQleiamdalrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499226461 138 -PRE-----LSGGQQQRVALARALVKDPSLLLLDEPFSNLDA 173
Cdd:PRK11819 155 pPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-219 |
9.12e-20 |
|
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: 86.76 E-value: 9.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALdnvniniengerfgiLGPSGAGKTTFMRIIAGLDVPSTGELYFDdrlvasnGKLIVPPED- 81
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTAL---------------VGPSGSGKSTVVALLENFYQPQGGQVLLD-------GKPISQYEHk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 ---RKIGMVFQTWALYPNlTAFENIAFPLTNMKMskeeirKRVEEVAKILDIHHVLNHFPRE-----------LSGGQQQ 147
Cdd:cd03248 85 ylhSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSF------ECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 148 RVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlgVTLLVVSHDPADIfAIADRVGVLVKGKL 219
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-225 |
2.56e-19 |
|
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: 85.24 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTT----FMRIIAgldvPSTGELYFDDRLVASngkliVP 78
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGVDISK-----IG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 PED--RKIGMVFQTWALYP-----NLTAFEniafpltnmKMSKEEI---------RKRVEEVAKILDihHVLNHFPRELS 142
Cdd:cd03244 73 LHDlrSRISIIPQDPVLFSgtirsNLDPFG---------EYSDEELwqalervglKEFVESLPGGLD--TVVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 143 GGQQQRVALARALVKDPSLLLLDEPFSNLDarmRDSARALVKEVQSRL-GVTLLVVSHdpaDIFAIA--DRVGVLVKGKL 219
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVD---PETDALIQKTIREAFkDCTVLTIAH---RLDTIIdsDRILVLDKGRV 215
|
....*.
gi 499226461 220 VQVGKP 225
Cdd:cd03244 216 VEFDSP 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
2.93e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 1 MVRIIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS-------NG 73
Cdd:PRK11614 3 KVMLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakimRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 74 KLIVPPEDRKIgmvfqtwalYPNLTAFENIAfpLTNMKMSKEEIRKRVEEVAKIldihhvlnhFPR----------ELSG 143
Cdd:PRK11614 81 AVAIVPEGRRV---------FSRMTVEENLA--MGGFFAERDQFQERIKWVYEL---------FPRlherriqragTMSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 144 GQQQRVALARALVKDPSLLLLDEPFSNLDA----RMRDSARALVKEvqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPSLGLAPiiiqQIFDTIEQLREQ-----GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
.
gi 499226461 220 V 220
Cdd:PRK11614 216 V 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-218 |
5.26e-19 |
|
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: 84.06 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVA---LDNVNINIENGERFGILGPSGAGKTTFmriIAGLdvpsTGELYfddrlvASNGKLIVPPe 80
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSL---LSAL----LGELE------KLSGSVSVPG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 drKIGMVFQT-WALypNLTAFENIAFpltNMKMSKEEIRKRVEEVAKILDihhvLNHFPR-------E----LSGGQQQR 148
Cdd:cd03250 67 --SIAYVSQEpWIQ--NGTIRENILF---GKPFDEERYEKVIKACALEPD----LEILPDgdlteigEkginLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEV-QSRL--GVTLLVVSHDPaDIFAIADRVGVLVKGK 218
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDA---HVGRHIFENCiLGLLlnNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-213 |
9.54e-19 |
|
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: 87.15 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 28 IENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlVASNGKLIVPPEDrkigmvfqtwalypnLTAFENIAFPL 107
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISYKPQYISPDYD---------------GTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 108 TNMKMSKEEIrkrvEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDS-ARALVKEV 186
Cdd:COG1245 427 TDDFGSSYYK----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAvAKAIRRFA 502
|
170 180
....*....|....*....|....*..
gi 499226461 187 QSRlGVTLLVVSHDPADIFAIADRVGV 213
Cdd:COG1245 503 ENR-GKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-228 |
1.72e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.61 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTfmriIAGL-----DVPStGELYFDDRLVA----SNGK 74
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLltrfyDIDE-GEILLDGHDLRdytlASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 75 livppedRKIGMVFQTWALYpNLTAFENIAFPLTNmKMSKEEIrkrvEEVAK-------ILDIHHVLNHFPRE----LSG 143
Cdd:PRK11176 417 -------NQVALVSQNVHLF-NDTIANNIAYARTE-QYSREQI----EEAARmayamdfINKMDNGLDTVIGEngvlLSG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 144 GQQQRVALARALVKDPSLLLLDEPFSNLDArmrDSARAlvkeVQSRLGV-----TLLVVSHDPADIfAIADRVGVLVKGK 218
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDT---ESERA----IQAALDElqknrTSLVIAHRLSTI-EKADEILVVEDGE 555
|
250
....*....|
gi 499226461 219 LVQVGKPEDL 228
Cdd:PRK11176 556 IVERGTHAEL 565
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-226 |
2.03e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDV--PSTGELYFDdrlvasnGKLIV--PPEDRK---IGMVFQtwal 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLD-------GEDILelSPDERAragIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 94 YPnltafenIAFP-LTNM-------------KMSKEEIRKRVEEVAKILDI-HHVLNhfpREL----SGGQQQRVALARA 154
Cdd:COG0396 85 YP-------VEIPgVSVSnflrtalnarrgeELSAREFLKLLKEKMKELGLdEDFLD---RYVnegfSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 155 LVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRL--GVTLLVVSHDPADI-FAIADRVGVLVKGKLVQVGKPE 226
Cdd:COG0396 155 LLLEPKLAILDETDSGLDI---DALRIVAEGVNKLRspDRGILIITHYQRILdYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-200 |
2.54e-18 |
|
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: 86.14 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLvasngklivppedrK 83
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV--------------K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTW-ALYPNLTAFENIAFPLTNMKMSKEEI----------------RKRVeevakildihhvlnhfpRELSGGQQ 146
Cdd:TIGR03719 387 LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIpsrayvgrfnfkgsdqQKKV-----------------GQLSGGER 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499226461 147 QRVALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRLGVTlLVVSHD 200
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDV---ETLRALEEALLNFAGCA-VVISHD 499
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-221 |
2.99e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.61 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPS---TGELYFDDRLVASNGklIVPPEDRK 83
Cdd:NF040905 5 RGITKTF--PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKD--IRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTWALYPNLTAFENIaF----PLTNMKMSKEEIRKRVEE-VAKI-LDIHhvlnhfPRELSG----GQQQRVALAR 153
Cdd:NF040905 80 IVIIHQELALIPYLSIAENI-FlgneRAKRGVIDWNETNRRARElLAKVgLDES------PDTLVTdigvGKQQLVEIAK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 154 ALVKDPSLLLLDEPFSNLDArmRDSAR--ALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQ 221
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNE--EDSAAllDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-214 |
3.16e-18 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 85.61 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVValdnvniniengerfGILGPSGAGKTTFMRIIAGLDVPSTGEL--------------------YFDdRLVASNG 73
Cdd:COG1245 97 KKGKVT---------------GILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdYFK-KLANGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 74 KLIVPPE--DrKIGMVFQ--TWALypnltafeniafpltnmkMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRV 149
Cdd:COG1245 161 KVAHKPQyvD-LIPKVFKgtVREL------------------LEKVDERGKLDELAEKLGLENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 150 ALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-214 |
3.98e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.25 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVValdnvniniengerfGILGPSGAGKTTFMRIIAGLDVPSTG------------------EL--YFDDrlvASNG 73
Cdd:PRK13409 97 KEGKVT---------------GILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtELqnYFKK---LYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 74 KLIV---PPEDRKIGMVFQ--TWALypnltafeniafpltnmkMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQR 148
Cdd:PRK13409 159 EIKVvhkPQYVDLIPKVFKgkVREL------------------LKKVDERGKLDEVVERLGLENILDRDISELSGGELQR 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSrlGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-223 |
6.71e-18 |
|
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: 80.75 E-value: 6.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALdnvniniengerfgiLGPSGAGKTTFMRIIAGLDVPS--TGELYFddrlvasNGKLIVPPE 80
Cdd:cd03232 20 RQLLNNISGYVKPGTLTAL---------------MGESGAGKTTLLDVLAGRKTAGviTGEILI-------NGRPLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTWALYPNLTAFENIAFPltnmkmskeeirkrveevAKIldihhvlnhfpRELSGGQQQRVALARALVKDPS 160
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFS------------------ALL-----------RGLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 161 LLLLDEPFSNLDARmrdSARALVKEVQ--SRLGVTLLVVSHDP-ADIFAIADRVGVLVK-GKLVQVG 223
Cdd:cd03232 129 ILFLDEPTSGLDSQ---AAYNIVRFLKklADSGQAILCTIHQPsASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-222 |
1.34e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNV-SKVFKKGKvvaldNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFddrlvasNGKLIVP--PEDR 82
Cdd:PRK09700 268 VRNVtSRDRKKVR-----DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL-------NGKDISPrsPLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 -KIGMVFQTWA-----LYPNLTAFENIAFpLTNMKMSK----------EEIRKRVEEVAKILDIH-HVLNHFPRELSGGQ 145
Cdd:PRK09700 336 vKKGMAYITESrrdngFFPNFSIAQNMAI-SRSLKDGGykgamglfheVDEQRTAENQRELLALKcHSVNQNITELSGGN 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 146 QQRVALARALVKDPSLLLLDEPFSNLDArmrdSARALVKEVQSRL---GVTLLVVSHDPADIFAIADRVGVLVKGKLVQV 222
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDV----GAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-213 |
1.36e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.70 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 28 IENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlVASNGKLIVPPEDRKIGMVfqtwaLYPNLTAFENIAFpl 107
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISYKPQYIKPDYDGTVEDL-----LRSITDDLGSSYY-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 108 tnmkmsKEEIRKRveevakiLDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDS-ARALVKEV 186
Cdd:PRK13409 434 ------KSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAvAKAIRRIA 500
|
170 180
....*....|....*....|....*..
gi 499226461 187 QSRlGVTLLVVSHDPADIFAIADRVGV 213
Cdd:PRK13409 501 EER-EATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-219 |
1.43e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 23 NVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGK-------LIVPPEDRKIGMVFQTWALYP 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlargLVYLPEDRQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 NLTA--FENIAFPLtnmKMSKEeiRKRVEEVAKILDIHhvLNHFP---RELSGGQQQRVALARALVKDPSLLLLDEPFSN 170
Cdd:PRK15439 361 NVCAltHNRRGFWI---KPARE--NAVLERYRRALNIK--FNHAEqaaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499226461 171 LDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-228 |
3.12e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.70 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkLIVPPEDRKIGMVFQTWALYp 95
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT---VTRASLRRNIAVVFQDAGLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 NLTAFENIAFPLTNMkmSKEEIRkRVEEVAKILD-IHHVLNHFP-------RELSGGQQQRVALARALVKDPSLLLLDEP 167
Cdd:PRK13657 422 NRSIEDNIRVGRPDA--TDEEMR-AAAERAQAHDfIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 168 FSNLDARMRDSARALVKEVqsRLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:PRK13657 499 TSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-228 |
4.35e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--SNGKLivpped 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdySEAAL------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RK-IGMVFQTWALYpNLTAFENIAfpLTNMKMSKEEIRKRVEEV--AKILDIHHVLNHF----PRELSGGQQQRVALARA 154
Cdd:PRK11160 413 RQaISVVSQRVHLF-SATLRDNLL--LAAPNASDEALIEVLQQVglEKLLEDDKGLNAWlgegGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 155 LVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSrlGVTLLVVSHdpaDIFAIA--DRVGVLVKGKLVQVGKPEDL 228
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH---RLTGLEqfDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-238 |
5.09e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 81.98 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 17 KVVALDNVNINieNGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--SNGKLivppedRKIgmVFQTWALY 94
Cdd:PRK10938 17 KTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlSFEQL------QKL--VSDEWQRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 95 PN--LTAFENiAFPLTNMKMSKEEIRK--RVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSN 170
Cdd:PRK10938 87 NTdmLSPGED-DTGRTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 171 LDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVA 238
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLA 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-228 |
6.49e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVppeDR 82
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQTWALYPNlTAFENIAFpltNMKMSKEEIRKRVE-----EVAKILD--IHHVLNHFPRELSGGQQQRVALARAL 155
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTL---GRDISEEQVWQALEtvqlaELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 156 VKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlgVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDL 228
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-226 |
7.21e-17 |
|
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: 77.95 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGldVPST----GELYFDDRLVASngkliVPPEDRK---IGMVFQTWAL 93
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKYevteGEILFKGEDITD-----LPPEERArlgIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 94 YPNLTafeniafpltnmkmskeeirkrveevakildihhvLNHFPREL----SGGQQQRVALARALVKDPSLLLLDEPFS 169
Cdd:cd03217 89 IPGVK-----------------------------------NADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 170 NLDArmrDSARALVKEVQS--RLGVTLLVVSHDP--ADiFAIADRVGVLVKGKLVQVGKPE 226
Cdd:cd03217 134 GLDI---DALRLVAEVINKlrEEGKSVLIITHYQrlLD-YIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-232 |
1.69e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.53 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIA-GLDVpSTGELYFDD------RLVASNGKLIVppedrkigmVFQTWA 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDV-SEGDIRFHDipltklQLDSWRSRLAV---------VSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 LYPNLTAfENIAfpLTNMKMSKEEIrkrvEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVALARALVKDPSL 161
Cdd:PRK10789 400 LFSDTVA-NNIA--LGRPDATQQEI----EHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 162 LLLDEPFSNLDARmrdSARALVKEV-QSRLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK10789 473 LILDDALSAVDGR---TEHQILHNLrQWGEGRTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-232 |
2.15e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALdnvniniengerfgiLGPSGAGKTtfMRIIAGLDVPSTGELYFDDRLVAsNGKLIVPPE-- 80
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLAL---------------VGGSGSGKS--LTCAAALGILPAGVRQTAGRVLL-DGKPVAPCAlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 81 DRKIGMVFQTwalyPNlTAFEniafPLTNMKMSKEEI---RKRVEEVAKIL---------DIHHVLNHFPRELSGGQQQR 148
Cdd:PRK10418 78 GRKIATIMQN----PR-SAFN----PLHTMHTHARETclaLGKPADDATLTaaleavgleNAARVLKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLD----ARMRDsaraLVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGK 224
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDvvaqARILD----LLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
....*...
gi 499226461 225 PEDLYDNP 232
Cdd:PRK10418 225 VETLFNAP 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-217 |
3.52e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 80.15 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALdnvniniengerfgiLGPSGAGKTTFMRIIAGLdvPSTGELYFDDRLVasNGklivPPED- 81
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTAL---------------MGASGAGKTTLLNVLAER--VTTGVITGGDRLV--NG----RPLDs 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 ---RKIGMVFQTWALYPNLTAFENI---AFPLTNMKMSKEEIRKRVEEVAKILDIHH---VLNHFPRE-LSGGQQQRVAL 151
Cdd:TIGR00956 833 sfqRSIGYVQQQDLHLPTSTVRESLrfsAYLRQPKSVSKSEKMEYVEEVIKLLEMESyadAVVGVPGEgLNVEQRKRLTI 912
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 152 ARALVKDPSLLL-LDEPFSNLDARmrdSARALVKEVQ--SRLGVTLLVVSHDP-ADIFAIADRVGVLVKG 217
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQ---TAWSICKLMRklADHGQAILCTIHQPsAILFEEFDRLLLLQKG 979
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
3.76e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.14 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgkliVPPEDRKIGMVFQTWALYPNLTAF 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD----LCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 101 ENIAFPLTNMKMSKEeirkrVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSAR 180
Cdd:PRK13540 93 ENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170 180
....*....|....*....|
gi 499226461 181 ALVKEVQSRLGVTLLVVSHD 200
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQD 187
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-232 |
4.42e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.92 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFK--KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVP----STGELYFDD----RLVasngkl 75
Cdd:PRK15093 6 IRNLTIEFKtsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDidllRLS------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 76 ivPPEDRK-----IGMVFQTwalyPN--LTAFENI------AFPLTNMK---MSKEEIRKR--VEEVAK--ILDIHHVLN 135
Cdd:PRK15093 80 --PRERRKlvghnVSMIFQE----PQscLDPSERVgrqlmqNIPGWTYKgrwWQRFGWRKRraIELLHRvgIKDHKDAMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 136 HFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNldarMRDSARALVKEVQSRL----GVTLLVVSHDPADIFAIADRV 211
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNA----MEPTTQAQIFRLLTRLnqnnNTTILLISHDLQMLSQWADKI 229
|
250 260
....*....|....*....|.
gi 499226461 212 GVLVKGKLVQVGKPEDLYDNP 232
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTP 250
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-214 |
5.65e-16 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 76.64 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 31 GERFGILGPSGAGKTTFMRIIAGLDVPSTG------------------EL--YFDdRLVASNGKLIVPPedrkigmvfQT 90
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgsELqnYFT-KLLEGDVKVIVKP---------QY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 91 WALYPNltAFENIAFPLtnmkMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSN 170
Cdd:cd03236 96 VDLIPK--AVKGKVGEL----LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499226461 171 LDARMRDSARALVKEVqSRLGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:cd03236 170 LDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-220 |
1.19e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFKKgkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivpPEDRK-- 83
Cdd:PRK10762 7 LKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNG-----PKSSQea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 -IGMVFQTWALYPNLTAFENIAF--PLTNmKMSKEEIRKRVEEVAKILDiHHVLNHFPR----ELSGGQQQRVALARALV 156
Cdd:PRK10762 80 gIGIIHQELNLIPQLTIAENIFLgrEFVN-RFGRIDWKKMYAEADKLLA-RLNLRFSSDklvgELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-173 |
1.40e-15 |
|
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: 74.45 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 15 KGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngklIVPPEDRKIGMVFQTWALY 94
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSIARGLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 95 PNLTAFENIAFpltnmkMSKEEIRKRVEEVAKILDIHHVlNHFP-RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDA 173
Cdd:cd03231 86 TTLSVLENLRF------WHADHSDEQVEEALARVGLNGF-EDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-222 |
4.09e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAG--LDVPSTGELYFDDRLVASNGKLIvppeDrkigmvfqtwALYPNLT 98
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI----D----------AIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFpLTNMKMSKEEIRKRVeevakildihhvlnhfPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDarmRDS 178
Cdd:COG2401 112 FKDAVEL-LNAVGLSDAVLWLRR----------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD---RQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499226461 179 ARALVKEVQS---RLGVTLLVVSHDPaDIFA--IADRVGVLVKGKLVQV 222
Cdd:COG2401 172 AKRVARNLQKlarRAGITLVVATHHY-DVIDdlQPDLLIFVGYGGVPEE 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-172 |
5.66e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 74.12 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgklivppedrkigmvfQTWALYPNlTAF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS----------------QFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 101 ENIAFPLtnmkmSKEEIRKRveEVAKILDIHHVLNHFPRE-----------LSGGQQQRVALARALVKDPSLLLLDEPFS 169
Cdd:cd03291 116 ENIIFGV-----SYDEYRYK--SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 499226461 170 NLD 172
Cdd:cd03291 189 YLD 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-233 |
5.93e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.67 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVValdnvniniengerfGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVAS-NGKLIVpped 81
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVT---------------GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFA---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIA---FPLTNM--KMSKEEiRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALV 156
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRELVAigrYPWHGAlgRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPV 233
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-219 |
6.15e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGL-DVPSTGELYFDDRLV-------ASNGKLIVPPEDRKI-GMVfqtw 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnpaqAIRAGIAMVPEDRKRhGIV---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 alyPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIH--HVLNHFP----RELSGGQQQRVALARALVKDPSLLLLD 165
Cdd:TIGR02633 352 ---PILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499226461 166 EPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-172 |
1.48e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 74.95 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgklivppedrkigmvfQTWALYPNlTAF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSP----------------QTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 101 ENIAFPLtnmkmSKEEIRKRveEVAKILDIHHVLNHFPRE-----------LSGGQQQRVALARALVKDPSLLLLDEPFS 169
Cdd:TIGR01271 505 DNIIFGL-----SYDEYRYT--SVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 499226461 170 NLD 172
Cdd:TIGR01271 578 HLD 580
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-200 |
1.49e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGElyfddrlvasngklIVPPEDRK 83
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT--------------IKIGETVK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQTW-ALYPNLTAFENIAFPLTNMKMSKEEI----------------RKRVeevakildihhvlnhfpRELSGGQQ 146
Cdd:PRK11819 389 LAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIpsrayvgrfnfkggdqQKKV-----------------GVLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499226461 147 QRVALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRLGvTLLVVSHD 200
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDV---ETLRALEEALLEFPG-CAVVISHD 501
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-225 |
2.44e-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: 70.90 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASngkliVPPED- 81
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIST-----IPLEDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 -RKIGMVFQTWALYP-----NLTAFEniafpltnmKMSKEEIRK--RVEEVAkildihhvLNhfpreLSGGQQQRVALAR 153
Cdd:cd03369 81 rSSLTIIPQDPTLFSgtirsNLDPFD---------EYSDEEIYGalRVSEGG--------LN-----LSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 154 ALVKDPSLLLLDEPFSNLDArmrdSARALVKEV--QSRLGVTLLVVSHDPADIfAIADRVGVLVKGKLVQVGKP 225
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDY----ATDALIQKTirEEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-228 |
3.78e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.89 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 9 VSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNgkliVPPEDRKIGMVF 88
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN----ISDVHQNMGYCP 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 89 QTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPF 168
Cdd:TIGR01257 2019 QFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 169 SNLDARMRdsaRALVKEVQS--RLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:TIGR01257 2099 TGMDPQAR---RMLWNTIVSiiREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-228 |
5.45e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFKKgkVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVasNGKLIVPPEDRKIGM 86
Cdd:PRK10982 2 SNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSKEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 87 VFQTWALYPNLTAFENI---AFPLTNMKMSKEEIRKRVEEVAKILDIhhvlNHFPRE----LSGGQQQRVALARALVKDP 159
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDI----DIDPRAkvatLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 160 SLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-230 |
8.11e-14 |
|
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: 72.46 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVppeDRKIGMVFQTWALYPNlTA 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 100 FENIAFPlTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPREL-------SGGQQQRVALARALVKDPSLLLLDEPFSNLD 172
Cdd:TIGR01193 565 LENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELseegssiSGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 173 ARmrdSARALVKEVQSRLGVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:TIGR01193 644 TI---TEKKIVNNLLNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-167 |
8.45e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYF------DDRLVASNGKLIvpp 79
Cdd:NF033858 4 LEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRRAVCPRI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 80 edrkigmvfqtwA---------LYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDihhvLNHFP----RELSGGQQ 146
Cdd:NF033858 79 ------------AympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATG----LAPFAdrpaGKLSGGMK 142
|
170 180
....*....|....*....|.
gi 499226461 147 QRVALARALVKDPSLLLLDEP 167
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEP 163
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-172 |
8.71e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 24 VNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRlVASNGKlivppEDRKIGMVFQTWALYPNLTAFENI 103
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGD-----RSRFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 104 AFpltnmkMSKEEIRKRVEEVAKILDIHHVLNH---FPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLD 172
Cdd:PRK13543 104 HF------LCGLHGRRAKQMPGSALAIVGLAGYedtLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-220 |
9.79e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 9.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVskvfkKGKVVALDnVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLV-------ASNGK 74
Cdd:PRK11288 256 VRLRLDGL-----KGPGLREP-ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprdAIRAG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 75 LIVPPEDRKI-GMVfqtwalyPNLTAFENI----------AFPLTNMKMSKEEIRKRVEEVA-KILDIHHVLnhfpRELS 142
Cdd:PRK11288 330 IMLCPEDRKAeGII-------PVHSVADNInisarrhhlrAGCLINNRWEAENADRFIRSLNiKTPSREQLI----MNLS 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 143 GGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLV 220
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-214 |
1.81e-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: 67.98 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 28 IENGERFGILGPSGAGKTTFMRIIAGLDVPSTgelyfddrlvasngklivppedrkigmvfqtwalypnltafENIAFPL 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG-----------------------------------------DNDEWDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 108 TNMKMSKEEIrkrveevakildihhvlnhfprELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQ 187
Cdd:cd03222 61 ITPVYKPQYI----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*..
gi 499226461 188 SRLGVTLLVVSHDPADIFAIADRVGVL 214
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-226 |
4.38e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDvpstgelyfddRLVASNGKLIVPPEDRk 83
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-----------RLASGKISILGQPTRQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 igmvfqtwALYPNLTAF----ENI--AFP--------------LTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSG 143
Cdd:PRK15056 74 --------ALQKNLVAYvpqsEEVdwSFPvlvedvvmmgryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 144 GQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVgVLVKGKLVQVG 223
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
...
gi 499226461 224 KPE 226
Cdd:PRK15056 224 PTE 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-228 |
5.35e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 12 VFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGlDVPS---------TGELYFDDRLVASNGKL------I 76
Cdd:PRK13547 9 VARRHRAI-LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPrlarlrA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 VPPEDRKIGMVFQTWAL-----YPNltafeniAFPLTNMKMSKEEIRKRVEEVA--KILDIHHVLNhfpreLSGGQQQRV 149
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIvllgrYPH-------ARRAGALTHRDGEIAWQALALAgaTALVGRDVTT-----LSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 150 ALARALVK---------DPSLLLLDEPFSNLDA----RMRDSARALVKEVQsrLGVtlLVVSHDPADIFAIADRVGVLVK 216
Cdd:PRK13547 155 QFARVLAQlwpphdaaqPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWN--LGV--LAIVHDPNLAARHADRIAMLAD 230
|
250
....*....|..
gi 499226461 217 GKLVQVGKPEDL 228
Cdd:PRK13547 231 GAIVAHGAPADV 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-219 |
5.62e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 22 DNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVP--STGELYFDDRLVA--------SNGKLIVPpEDRK-IGMVfqt 90
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA-YPgrWEGEIFIDGKPVKirnpqqaiAQGIAMVP-EDRKrDGIV--- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 91 walyPNLTAFENIAFPLTNmKMSKeeiRKRVEEVAKILDIHHVLNHF------PR----ELSGGQQQRVALARALVKDPS 160
Cdd:PRK13549 354 ----PVMGVGKNITLAALD-RFTG---GSRIDDAAELKTILESIQRLkvktasPElaiaRLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 161 LLLLDEPFSNLDArmrdSAR--------ALVKEvqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PRK13549 426 ILILDEPTRGIDV----GAKyeiyklinQLVQQ-----GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-224 |
6.84e-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: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 11 KVFKKGKVVA-LDNVNINIENGERFGILGPSGAGKTTFMRIIAGldvPSTGELYFDDRLVASNGkliVPPED---RKIGM 86
Cdd:TIGR00956 66 KKFRDTKTFDiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITYDG---ITPEEikkHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 87 VF---QTWALYPNLTAFENIAF------PLTNMK-MSKEEIRKRVEEV-AKILDIHH-----VLNHFPRELSGGQQQRVA 150
Cdd:TIGR00956 140 VVynaETDVHFPHLTVGETLDFaarcktPQNRPDgVSREEYAKHIADVyMATYGLSHtrntkVGNDFVRGVSGGERKRVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 151 LARALVKDPSLLLLDEPFSNLdarmrDSARAL-----VKEVQSRLGVTLLVVSHDPA-DIFAIADRVGVLVKGKLVQVGK 224
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGL-----DSATALefiraLKTSANILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIYFGP 294
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-228 |
9.01e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.61 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 6 VKNVSKVFkkGKVVALDNVNINIENGERFGILGPSGAGKTTFMrIIAGLDVPSTGELYFDDRLVASNGKLIvppeDRKIG 85
Cdd:NF000106 16 VRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRAL----RRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 MVFQT-WALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLL 164
Cdd:NF000106 89 *HRPVr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 165 DEPFSNLDARMR----DSARALVKEvqsrlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:NF000106 169 DEPTTGLDPRTRnevwDEVRSMVRD-----GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-219 |
9.69e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGklivPPEDRK-IGMVFQTWALYPNLT 98
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ----PEDYRKlFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFP-------LTNMKMSkeeiRKRVEEVAKILDIhhvlnhfprELSGGQQQRVALARALVKDPSLLLLDEPFSNL 171
Cdd:PRK10522 414 GPEGKPANpalvekwLERLKMA----HKLELEDGRISNL---------KLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499226461 172 DARMRdsaRALVKEVQSRL---GVTLLVVSHDPAdIFAIADRVGVLVKGKL 219
Cdd:PRK10522 481 DPHFR---REFYQVLLPLLqemGKTIFAISHDDH-YFIHADRLLEMRNGQL 527
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
3-201 |
1.29e-12 |
|
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: 68.62 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdvpstGELYfddrlvasNGKLIVPPEDR 82
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-----WPVY--------GGRLTKPAKGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 kigMVFQTWALYPNLTAF-ENIAFPLTNMKMSKEEIR-KRVEEVAKILDIHHVLNH---------FPRELSGGQQQRVAL 151
Cdd:TIGR00954 517 ---LFYVPQRPYMTLGTLrDQIIYPDSSEDMKRRGLSdKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAM 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499226461 152 ARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVqsrlGVTLLVVSHDP 201
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSHRK 639
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-228 |
2.47e-12 |
|
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: 68.43 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNG------KLI 76
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrfKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 77 VPPEDRkigmVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDihHVLNHFPRELSGGQQQRVALARALV 156
Cdd:TIGR00957 1364 IIPQDP----VLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499226461 157 KDPSLLLLDEPFSNLDARMRDSARALVKEVQSrlGVTLLVVSHDPADIFAIAdRVGVLVKGKLVQVGKPEDL 228
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-177 |
2.49e-12 |
|
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: 65.43 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDR-KIGMVFQ-TWALypNLT 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQkPWLL--NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 99 AFENIAFpltNMKMSKEEIRKRVEEVAKILDIHhVLNHFPR--------ELSGGQQQRVALARALVKDPSLLLLDEPFSN 170
Cdd:cd03290 95 VEENITF---GSPFNKQRYKAVTDACSLQPDID-LLPFGDQteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
....*..
gi 499226461 171 LDARMRD 177
Cdd:cd03290 171 LDIHLSD 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-203 |
2.73e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVskVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGlDVPS--------------TGELYFDDRl 68
Cdd:PRK10938 260 RIVLNNG--VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGETIWDIK- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 69 vasngklivppedRKIGMVFQTWAL-YP-NLTA--------FENIAFpltnMKMSKEEIRKRVEEVAKILDIHHVLNHFP 138
Cdd:PRK10938 336 -------------KHIGYVSSSLHLdYRvSTSVrnvilsgfFDSIGI----YQAVSDRQQKLAQQWLDILGIDKRTADAP 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 139 -RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVkEVQSRLGVT-LLVVSHDPAD 203
Cdd:PRK10938 399 fHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV-DVLISEGETqLLFVSHHAED 464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
96-218 |
3.03e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 NLTAFENIAFpltnmkmSKEE-IRKRVEEVAKILDIHHVLNHFP-----------RELSGGQQQRVALARALVKDPSLLL 163
Cdd:PTZ00265 1309 NMSIYENIKF-------GKEDaTREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILL 1381
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 164 LDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADI--------FAIADRVGVLVKGK 218
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIkrsdkivvFNNPDRTGSFVQAH 1444
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-220 |
9.63e-12 |
|
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: 63.44 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 7 KNVSKVFKKGKVVA--LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPS---TGELYFDDRlvasNGKLIVPPED 81
Cdd:cd03233 7 RNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI----PYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQTWALYPNLTAFENIAFPLtNMKMskeeirkrveevakildihhvlNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFAL-RCKG----------------------NEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 162 LLLDEPFSNLdarmrDSARAL-----VKEVQSRLGVTLLVVSHDPAD-IFAIADRVGVLVKGKLV 220
Cdd:cd03233 140 LCWDNSTRGL-----DSSTALeilkcIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-219 |
1.05e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 2 VRIIVKNVSkvfkkGKVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGlDVPST-GElyfddrlVASNGKLIVP-- 78
Cdd:PRK10762 256 VRLKVDNLS-----GPGV--NDVSFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPRTsGY-------VTLDGHEVVTrs 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 79 ------------PEDRK-IGMVFqtwalypNLTAFENIAfpLTNM-KMSKEEIR-KRVEEVAKILDIHHVLN-HFP---- 138
Cdd:PRK10762 321 pqdglangivyiSEDRKrDGLVL-------GMSVKENMS--LTALrYFSRAGGSlKHADEQQAVSDFIRLFNiKTPsmeq 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 139 --RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVK 216
Cdd:PRK10762 392 aiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHE 470
|
...
gi 499226461 217 GKL 219
Cdd:PRK10762 471 GRI 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-211 |
1.27e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVvaLDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDdrlvasngklivppEDRK 83
Cdd:PRK15064 320 LEVENLTKGFDNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--------------ENAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 IGMVFQ-TWALYPN-LTAFE-------------NIAFPLTNMKMSKEEIRKRVeevakildihhvlnhfpRELSGGQQQR 148
Cdd:PRK15064 384 IGYYAQdHAYDFENdLTLFDwmsqwrqegddeqAVRGTLGRLLFSQDDIKKSV-----------------KVLSGGEKGR 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 149 VALARALVKDPSLLLLDEPFSNLDarMrDSARALVKEVQSRLGvTLLVVSHDPADIFAIADRV 211
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMD--M-ESIESLNMALEKYEG-TLIFVSHDREFVSSLATRI 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-200 |
1.43e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVV-ALDNVNINIEN-------------GERFGILGPSGAGKTTFMRIIAGLDVPSTGEL---------YFDdrlvasn 72
Cdd:PRK11147 316 GKIVfEMENVNYQIDGkqlvkdfsaqvqrGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFD------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 73 gklivppEDRKigmvfqtwALYPNLTAFENIAfpltnmkMSKEEI----RKRveevakildihHVLNH-----FP----- 138
Cdd:PRK11147 389 -------QHRA--------ELDPEKTVMDNLA-------EGKQEVmvngRPR-----------HVLGYlqdflFHpkram 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499226461 139 ---RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSrlgvTLLVVSHD 200
Cdd:PRK11147 436 tpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG----TVLLVSHD 496
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-204 |
2.89e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 18 VVALDNVNINIENGERFG------------ILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlvaSNGKLIVPPEDRKIG 85
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDlsitflpsaityIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN----CNINNIAKPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 86 mvfQTWALYPNLTAFENIAFpltnmkmsKEEIRKRVEEV-AKI--LDIHHVLNHFPRELSGGQQQRVALARALVKDPSLL 162
Cdd:PRK13541 77 ---HNLGLKLEMTVFENLKF--------WSEIYNSAETLyAAIhyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499226461 163 LLDEPFSNLDARMRDSARALVKeVQSRLGVTLLVVSHDPADI 204
Cdd:PRK13541 146 LLDEVETNLSKENRDLLNNLIV-MKANSGGIVLLSSHLESSI 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-174 |
3.98e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVAL-DNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDrlvASNGKLIVPPED 81
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 R-KIGMVFQTWALYPNlTAFENIAFPLTNMK----MSKE---------------------------------------EI 117
Cdd:PTZ00265 459 RsKIGVVSQDPLLFSN-SIKNNIKYSLYSLKdleaLSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliEM 537
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 118 RKRVE--------EVAKILDIHHVLNHFP-----------RELSGGQQQRVALARALVKDPSLLLLDEPFSNLDAR 174
Cdd:PTZ00265 538 RKNYQtikdsevvDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-228 |
4.63e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.53 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFkkgkvVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEL--YFDDRLVASNGklivpped 81
Cdd:PRK13546 28 LIPKHKNKTF-----FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdrNGEVSVIAISA-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 rkigmvfqtwALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSL 161
Cdd:PRK13546 95 ----------GLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499226461 162 LLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDL 228
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-200 |
9.59e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 16 GKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFddrlvasnGKLIvppedrKIGMVFQTWALYp 95
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------AKGI------KLGYFAQHQLEF- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 nLTAFENiafPLTNM-KMSKEEIRKRVEEVA--------KILDIhhvlnhfPRELSGGQQQRVALARALVKDPSLLLLDE 166
Cdd:PRK10636 388 -LRADES---PLQHLaRLAPQELEQKLRDYLggfgfqgdKVTEE-------TRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190
....*....|....*....|....*....|....
gi 499226461 167 PFSNLDARMRdsaRALVKEVQSRLGvTLLVVSHD 200
Cdd:PRK10636 457 PTNHLDLDMR---QALTEALIDFEG-ALVVVSHD 486
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-199 |
1.16e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYfddrlVASNGKLIVppedrkIGMvfqtwALYPNLTA 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD-----IKGSAALIA------ISS-----GLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 100 FENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSA 179
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|
gi 499226461 180 RALVKEVQSRlGVTLLVVSH 199
Cdd:PRK13545 183 LDKMNEFKEQ-GKTIFFISH 201
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-200 |
2.54e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 23 NVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFD--DRLvasnGKL----IVPPEDRKIGMVF----QTW- 91
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnERL----GKLrqdqFAFEEFTVLDTVImghtELWe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 ------ALYPNLTAFENiafplTNMKMSKEEIR----------KRVEEVAKILDIhHVLNHFP--RELSGGQQQRVALAR 153
Cdd:PRK15064 95 vkqerdRIYALPEMSEE-----DGMKVADLEVKfaemdgytaeARAGELLLGVGI-PEEQHYGlmSEVAPGWKLRVLLAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499226461 154 ALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRlGVTLLVVSHD 200
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDI---NTIRWLEDVLNER-NSTMIIISHD 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
5-217 |
2.84e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 5 IVKNVSKVFKKGKVVALdnvniniengerfgiLGPSGAGKTTFMRIIAGldvPSTGElYFDDRLVASNGKLIVPPEDRKI 84
Cdd:PLN03140 895 LLREVTGAFRPGVLTAL---------------MGVSGAGKTTLMDVLAG---RKTGG-YIEGDIRISGFPKKQETFARIS 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 85 GMVFQTWALYPNLTAFENI---AFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNH---FP--RELSGGQQQRVALARALV 156
Cdd:PLN03140 956 GYCEQNDIHSPQVTVRESLiysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELV 1035
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 157 KDPSLLLLDEPFSNLDARmrdSARALVKEVQSRL--GVTLLVVSHDPA-DIFAIADRVGVLVKG 217
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLDAR---AAAIVMRTVRNTVdtGRTVVCTIHQPSiDIFEAFDELLLMKRG 1096
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-199 |
5.07e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.48 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdVPSTGELYFDDrlvASNGKLIVPPEDR 82
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDG---VSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 83 KIGMVFQ-----TWALYPNLTAFEniafpltnmKMSKEEIRKRVEEVAkildIHHVLNHFPREL-----------SGGQQ 146
Cdd:cd03289 78 AFGVIPQkvfifSGTFRKNLDPYG---------KWSDEEIWKVAEEVG----LKSVIEQFPGQLdfvlvdggcvlSHGHK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499226461 147 QRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKevQSRLGVTLLVVSH 199
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEH 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-201 |
8.85e-10 |
|
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: 57.62 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 36 ILGPSGAGKTTfmrIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDR-KIGMVFQ-----TWALYPNLTAFENIAFpltn 109
Cdd:cd03240 27 IVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLIREGEVRaQVKLAFEnangkKYTITRSLAILENVIF---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 110 mkmskeeIRKrvEEVAKILDIHhvlnhfPRELSGGQQQ------RVALARALVKDPSLLLLDEPFSNLDA-RMRDSARAL 182
Cdd:cd03240 100 -------CHQ--GESNWPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEI 164
|
170
....*....|....*....
gi 499226461 183 VKEVQSRLGVTLLVVSHDP 201
Cdd:cd03240 165 IEERKSQKNFQLIVITHDE 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-194 |
1.95e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRiiAGLDVPST-GELYFDDrlvASNGKLIVPPED 81
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS--ALLRLLSTeGEIQIDG---VSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 82 RKIGMVFQ-----TWALYPNLTAFEniafpltnmKMSKEEIRKRVEEVAkildIHHVLNHFPREL-----------SGGQ 145
Cdd:TIGR01271 1292 KAFGVIPQkvfifSGTFRKNLDPYE---------QWSDEEIWKVAEEVG----LKSVIEQFPDKLdfvlvdggyvlSNGH 1358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499226461 146 QQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTL 194
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-231 |
2.43e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFmrIIAGLdvpstGEL-YFDDRLVASNGKLIVPPEdrkIGMVFqtwalypNLTA 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSL--ISAML-----GELsHAETSSVVIRGSVAYVPQ---VSWIF-------NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 100 FENIAFpltNMKMSKEEIRKRVEEVAkildIHHVLNHFP-REL----------SGGQQQRVALARALVKDPSLLLLDEPF 168
Cdd:PLN03232 696 RENILF---GSDFESERYWRAIDVTA----LQHDLDLLPgRDLteigergvniSGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 169 SNLDARM-RDSARALVKEvqSRLGVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:PLN03232 769 SALDAHVaHQVFDSCMKD--ELKGKTRVLVTNQ-LHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-230 |
3.74e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 4 IIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIagldvpsTGELYFDDRLVASNGKLIVPPEdrk 83
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-------LAEMDKVEGHVHMKGSVAYVPQ--- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 84 igmvfQTWalYPNLTAFENIAFPltnmKMSKEEIRKRVEEVAKILDIHHVLNHFPR--------ELSGGQQQRVALARAL 155
Cdd:TIGR00957 707 -----QAW--IQNDSLRENILFG----KALNEKYYQQVLEACALLPDLEILPSGDRteigekgvNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 156 VKDPSLLLLDEPFSNLDARMrdsARALVKEVQSRLGV----TLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLYD 230
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHV---GKHIFEHVIGPEGVlknkTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-234 |
6.97e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 32 ERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVppeDRKIGMVFQTWALYPNLTAFENIAFPLTN-- 109
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPVLFSGTVRFNIDPFSEHNda 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 110 ---MKMSKEEIRKRVEEVAKILDIHhvLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMrDS--ARALVK 184
Cdd:PLN03232 1340 dlwEALERAHIKDVIDRNPFGLDAE--VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT-DSliQRTIRE 1416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499226461 185 EVQSrlgVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDLYDNPVS 234
Cdd:PLN03232 1417 EFKS---CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-219 |
2.62e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 23 NVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLvasngKLIVPPEDRKIGMvfqtwALYPNLTAFEN 102
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----RMAVFSQHHVDGL-----DLSSNPLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 103 IAFPltnmKMSKEEIRKRVEE--VAKILDIHHVLNhfpreLSGGQQQRVALARALVKDPSLLLLDEPFSNLDArmrDSAR 180
Cdd:PLN03073 597 RCFP----GVPEQKLRAHLGSfgVTGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAVE 664
|
170 180 190
....*....|....*....|....*....|....*....
gi 499226461 181 ALVKEVQSRLGvTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PLN03073 665 ALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-246 |
4.01e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 19 VALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYfddrlvasngklivppEDRKIGMV-FQTWALypNL 97
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------------AERSIAYVpQQAWIM--NA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 98 TAFENIAFpltnmkmSKEEIRKRVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVALARALVKDPSLLLLDE 166
Cdd:PTZ00243 736 TVRGNILF-------FDEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 167 PFSNLDARMrdsARALVKEV-QSRL-GVTLLVVSHDpADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSiqvASLIGEI 244
Cdd:PTZ00243 809 PLSALDAHV---GERVVEECfLGALaGKTRVLATHQ-VHVVPRADYVVALGDGRVEFSGSSADFMRTSLY---ATLAAEL 881
|
..
gi 499226461 245 NE 246
Cdd:PTZ00243 882 KE 883
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-210 |
4.59e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 31 GERFGILGPSGAGKTTFMRIIAG-LDVPSTGELYFDDRlvasngklivppedrkigmvfqtwalypnltafeniafpltn 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 110 mkmskeeirkRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALV-----K 184
Cdd:smart00382 40 ----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllL 109
|
170 180
....*....|....*....|....*.
gi 499226461 185 EVQSRLGVTLLVVSHDPADIFAIADR 210
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-199 |
1.31e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 26 INIENGERFGILGPSGAGKTTFMRIIA--GLD-VPSTGE-LYFDDRLVASNGKLIVPPEDRKI---------GMVFQTWA 92
Cdd:PLN03073 198 VTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDgIPKNCQiLHVEQEVVGDDTTALQCVLNTDIertqlleeeAQLVAQQR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 93 LYPNLTAFENIAFPlTNMKMSKEEIRKRVEEVAKILD-------------IHHVLNHFP-------RELSGGQQQRVALA 152
Cdd:PLN03073 278 ELEFETETGKGKGA-NKDGVDKDAVSQRLEEIYKRLElidaytaearaasILAGLSFTPemqvkatKTFSGGWRMRIALA 356
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499226461 153 RALVKDPSLLLLDEPFSNLDARmrdsARALVKEVQSRLGVTLLVVSH 199
Cdd:PLN03073 357 RALFIEPDLLLLDEPTNHLDLH----AVLWLETYLLKWPKTFIVVSH 399
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-223 |
3.41e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLdvPS----TGELYFDDRLVasngkLIVPPEDRK---IGMVFQtwal 93
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESI-----LDLEPEERAhlgIFLAFQ---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 94 YP------NLTAFENIAFPLTNMKMSKEEIR--KRVEEVAKILDI----HHVLNHFPRE-LSGGQQQRVALARALVKDPS 160
Cdd:CHL00131 92 YPieipgvSNADFLRLAYNSKRKFQGLPELDplEFLEIINEKLKLvgmdPSFLSRNVNEgFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 161 LLLLDEPFSNLDArmrDSARALVKEVQS--RLGVTLLVVSHDPADI-FAIADRVGVLVKGKLVQVG 223
Cdd:CHL00131 172 LAILDETDSGLDI---DALKIIAEGINKlmTSENSIILITHYQRLLdYIKPDYVHVMQNGKIIKTG 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-173 |
4.95e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGlDVPSTgelyfDDRLVASNGKLIVPPEdrkIGMVFqtwalypNLTAF 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPR-----SDASVVIRGTVAYVPQ---VSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 101 ENIAFPLtnmkmskEEIRKRVEEVAKILDIHHVLNHFPR-----------ELSGGQQQRVALARALVKDPSLLLLDEPFS 169
Cdd:PLN03130 697 DNILFGS-------PFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
....
gi 499226461 170 NLDA 173
Cdd:PLN03130 770 ALDA 773
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-235 |
9.66e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 13 FKKGKVVALDNVNINIENGERFGILGPSGAGKTT----FMRIIaglDVpSTGELYFDDRLVASNGkliVPPEDRKIGMVF 88
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTllltFMRMV---EV-CGGEIRVNGREIGAYG---LRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 89 QTWALYP-----NLTAFeniafpltnMKMSKEEI---------RKRVEEVAKILDihhvlnhfPRELSGG------QQQR 148
Cdd:PTZ00243 1391 QDPVLFDgtvrqNVDPF---------LEASSAEVwaalelvglRERVASESEGID--------SRVLEGGsnysvgQRQL 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 149 VALARALVKDPS-LLLLDEPFSNLDArmrdsarALVKEVQSRL-----GVTLLVVSHDPADIfAIADRVGVLVKGKLVQV 222
Cdd:PTZ00243 1454 MCMARALLKKGSgFILMDEATANIDP-------ALDRQIQATVmsafsAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEM 1525
|
250
....*....|...
gi 499226461 223 GKPEDLYDNPVSI 235
Cdd:PTZ00243 1526 GSPRELVMNRQSI 1538
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
141-211 |
1.26e-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: 1.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 141 LSGGQQQRVALARALVKDPS--LLLLDEPFSNLDARMRDSARALVKEVQSrLGVTLLVVSHDPaDIFAIADRV 211
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDE-DTIRAADHV 208
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-210 |
1.51e-06 |
|
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: 47.74 E-value: 1.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 141 LSGGQQQRVALARAL----VKDPSLLLLDEPFSNLDARMRDSARALVKEvQSRLGVTLLVVSHDPaDIFAIADR 210
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLP-ELAELADK 149
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-219 |
4.73e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 20 ALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVA--------SNGKLIVPPEDRKIGmvfqtw 91
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneaiNHGFALVTEERRSTG------ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 92 aLYPNLtafeNIAFP--LTNMKMSKEEI-----RKRVEEVAKILDIHHVLNHFPR----ELSGGQQQRVALARALVKDPS 160
Cdd:PRK10982 337 -IYAYL----DIGFNslISNIRNYKNKVglldnSRMKSDTQWVIDSMRVKTPGHRtqigSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 161 LLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIFAIADRVGVLVKGKL 219
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-228 |
6.80e-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: 46.83 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTT----FMRIIaglDVpstgelyFDDRLVASN---GKLIVPPEDRKIGMVFQTWAL 93
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSlslaFFRMV---DI-------FDGKIVIDGidiSKLPLHTLRSRLSIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 94 YPNLTAFeniafpltNMKMSKEEIRKRVEEVAKILDIHHVLNHFPREL-----------SGGQQQRVALARALVKDPSLL 162
Cdd:cd03288 107 FSGSIRF--------NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 163 LLDEPFSNLDARMRDSARALVkeVQSRLGVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDL 228
Cdd:cd03288 179 IMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-211 |
8.85e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 14 KKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGldvpstgelyfddRLVASNGKLIVPpedrkigmvfQTWAL 93
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-------------EISADGGSYTFP----------GNWQL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 94 ------------------------YPNLTAFENIA--------FPLTNMKMSKEE---IRKRVEEVAKILDI-HHVLNHF 137
Cdd:PRK10636 67 awvnqetpalpqpaleyvidgdreYRQLEAQLHDAnerndghaIATIHGKLDAIDawtIRSRAASLLHGLGFsNEQLERP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499226461 138 PRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDArmrDSARALVKEVQSRLGvTLLVVSHDPADIFAIADRV 211
Cdd:PRK10636 147 VSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-231 |
1.09e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLivppEDRKI-GMVFQTWALYP---- 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM----DLRKVlGIIPQAPVLFSgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 -NLTAF--ENIAFPLTNMKMS--KEEIRKRV----EEVAKILDihhvlnhfprELSGGQQQRVALARALVKDPSLLLLDE 166
Cdd:PLN03130 1331 fNLDPFneHNDADLWESLERAhlKDVIRRNSlgldAEVSEAGE----------NFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 167 PFSNLDARmrdsARALVK-----EVQSrlgVTLLVVSHDPADIFAiADRVGVLVKGKLVQVGKPEDLYDN 231
Cdd:PLN03130 1401 ATAAVDVR----TDALIQktireEFKS---CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-200 |
1.16e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.77 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 3 RIIVKNVsKVFKKGKVVALDNvNINIengerfgILGPSGAGKTTFMRIIA-------------GLDVPSTG------ELY 63
Cdd:COG0419 4 RLRLENF-RSYRDTETIDFDD-GLNL-------IVGPNGAGKSTILEAIRyalygkarsrsklRSDLINVGseeasvELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 64 FDD-----RLVASNGKLIV----PPEDRK--IGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEvakILDIHH 132
Cdd:COG0419 75 FEHggkryRIERRQGEFAEfleaKPSERKeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQE---ILAQLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499226461 133 VLNHFpRELSGGQQQRVALARALVkdpslLLLDepFSNLDARMRDSARALVKEvqsrlgvtLLVVSHD 200
Cdd:COG0419 152 GLDPI-ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE--------LAIITHV 203
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-185 |
2.15e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 42.61 E-value: 2.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 139 RELSGGQQQR---VALARALV----------KDPSLLLLDEPFSNLDARMRDSARALVKE 185
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-244 |
2.24e-05 |
|
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: 46.16 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 141 LSGGQQQRVALAR----ALVKdpSLLLLDEPFSNLdaRMRDSARALVKEVQSR-LGVTLLVVSHDPADIFAiADRV---- 211
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTG--VLYVLDEPSIGL--HQRDNRRLINTLKRLRdLGNTLIVVEHDEDTIRA-ADYVidig 563
|
90 100 110
....*....|....*....|....*....|....*.
gi 499226461 212 ---GVLvKGKLVQVGKPEDLYDNPVSIQVASLIGEI 244
Cdd:TIGR00630 564 pgaGEH-GGEVVASGTPEEILANPDSLTGQYLSGRK 598
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
141-235 |
3.95e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 141 LSGGQQQRVALARA----LVKdpSLLLLDEPfS-------N---LDA--RMRDsaralvkevqsrLGVTLLVVSHDPADI 204
Cdd:COG0178 486 LSGGEAQRIRLATQigsgLVG--VLYVLDEP-SiglhqrdNdrlIETlkRLRD------------LGNTVIVVEHDEDTI 550
|
90 100 110
....*....|....*....|....*....|....*...
gi 499226461 205 FAiADRV-------GVLvKGKLVQVGKPEDLYDNPVSI 235
Cdd:COG0178 551 RA-ADYIidigpgaGEH-GGEVVAQGTPEEILKNPDSL 586
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-167 |
6.58e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 17 KVValDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPS--TGELYFDDRLV-------ASNGKLIVPPEDRKigmv 87
Cdd:NF040905 274 KVV--DDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEVdvstvsdAIDAGLAYVTEDRK---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 88 fqTWALypNL--TAFENIafPLTNM-KMSK-------EEIRKrVEEVAKILDI------HHVLNhfpreLSGGQQQRVAL 151
Cdd:NF040905 348 --GYGL--NLidDIKRNI--TLANLgKVSRrgvidenEEIKV-AEEYRKKMNIktpsvfQKVGN-----LSGGNQQKVVL 415
|
170
....*....|....*.
gi 499226461 152 ARALVKDPSLLLLDEP 167
Cdd:NF040905 416 SKWLFTDPDVLILDEP 431
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-247 |
9.29e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 134 LNHFP-----RELSGGQQQRVALARAL---VKDPSLLLLDEPFSNLDARmrdSARALVKEVQS--RLGVTLLVVSHDpAD 203
Cdd:PRK00635 798 LDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTH---DIKALIYVLQSltHQGHTVVIIEHN-MH 873
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499226461 204 IFAIADRV------GVLVKGKLVQVGKPEDL--YDNPVSIQVASLIGEINEL 247
Cdd:PRK00635 874 VVKVADYVlelgpeGGNLGGYLLASCSPEELihLHTPTAKALRPYLSSPQEL 925
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-228 |
9.56e-05 |
|
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: 44.23 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 141 LSGGQQQRVALARALVKD---PSLLLLDEPFSNLdaRMRDSARALvkEVQSRL---GVTLLVVSHDpADIFAIADRV--- 211
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL--HFDDIKKLL--EVLQRLvdkGNTVVVIEHN-LDVIKTADYIidl 904
|
90 100
....*....|....*....|
gi 499226461 212 ---GVLVKGKLVQVGKPEDL 228
Cdd:TIGR00630 905 gpeGGDGGGTVVASGTPEEV 924
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-223 |
2.40e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 21 LDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDvpstgELYFDDRLVASNGK--LIVPPEDRK---IGMVFQtwalYP 95
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-----DYEVTGGTVEFKGKdlLELSPEDRAgegIFMAFQ----YP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 96 -NLTAFENIAFPLTNMKMSKE----------EIRKRVEEVAKILDIhhvlnhfPREL---------SGGQQQRVALARAL 155
Cdd:PRK09580 88 vEIPGVSNQFFLQTALNAVRSyrgqepldrfDFQDLMEEKIALLKM-------PEDLltrsvnvgfSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499226461 156 VKDPSLLLLDEPFSNLDArmrDSARALVKEVQS-RLGV-TLLVVSHDPADIFAIA-DRVGVLVKGKLVQVG 223
Cdd:PRK09580 161 VLEPELCILDESDSGLDI---DALKIVADGVNSlRDGKrSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-225 |
3.34e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 140 ELSGGQQQRVALARALVK---DPSLLLLDEPFSNLdaRMRDSARALvkEVQSRL---GVTLLVVSHDpADIFAIADRV-- 211
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGL--HFHDVKKLL--EVLQRLvdkGNTVVVIEHN-LDVIKCADWIid 243
|
90
....*....|....*...
gi 499226461 212 ----GVLVKGKLVQVGKP 225
Cdd:cd03271 244 lgpeGGDGGGQVVASGTP 261
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
245-283 |
3.55e-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: 37.81 E-value: 3.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499226461 245 NELEGKVTNEGVVIGSLRFPVS----VSSDRAIIGIRPEDVKL 283
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPelagAEGSEVVAYVRPHDLEI 43
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-235 |
3.64e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 141 LSGGQQQRVALARALVKDPS--LLLLDEPFSNLDARMRDSARALVKEVQSRlGVTLLVVSHDPADIfAIADRV------- 211
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMI-SLADRIidigpga 554
|
90 100
....*....|....*....|....
gi 499226461 212 GVLvKGKLVQVGKPEDLYDNPVSI 235
Cdd:PRK00635 555 GIF-GGEVLFNGSPREFLAKSDSL 577
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
141-211 |
5.48e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.38 E-value: 5.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499226461 141 LSGGQQQRVALARALVKDP--SLLLLDEPFSNLDARMRDSARALVKEVQSrLGVTLLVVSHDPaDIFAIADRV 211
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNL-DVLSSADWI 158
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
139-222 |
9.32e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 139 RELSGGQQQRVALARALVKDPSL----------LLLDEPFSNLDARMRDSARALVKEVQSrLGVTLLVVSHDPADIFAIA 208
Cdd:TIGR00618 949 ATLSGGETFLASLSLALALADLLstsggtvldsLFIDEGFGSLDEDSLDRAIGILDAIRE-GSKMIGIISHVPEFRERIP 1027
|
90
....*....|....
gi 499226461 209 DRVGVLVKGKLVQV 222
Cdd:TIGR00618 1028 HRILVKKTNAGSHV 1041
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
19-228 |
1.34e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 39.66 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 19 VALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGEL--YFDDRLVASNGKLIVP--PEDRKIGMVFQTWALy 94
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFigLRGDALPLGANSFILPglTGEENARMMASLYGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 95 pNLTAFENIAFPLTNMKMSKEEirkRVEEVAKILDIHhvlnhfprelsggqqqrVALARALVKDPSLLLLDEPFSNLD-- 172
Cdd:PRK15177 80 -DGDEFSHFCYQLTQLEQCYTD---RVSEYSVTMKTH-----------------LAFAINLLLPCRLYIADGKLYTGDna 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499226461 173 ARMRDSArALVKEVQSRlgvTLLVVSHDPADIFAIADRVGVLVKGKLVQVgkpEDL 228
Cdd:PRK15177 139 TQLRMQA-ALACQLQQK---GLIVLTHNPRLIKEHCHAFGVLLHGKITMC---EDL 187
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
141-210 |
5.59e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 38.22 E-value: 5.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499226461 141 LSGGQQQRVALA---------RALVKDPSLLLLDEPFSNLDARMRdsaRALVKEVQSrLGVTLLVVSHDPADIFAIADR 210
Cdd:PRK00064 274 GSTGQQKLLLLAlklaeaellKEETGEAPILLLDDVASELDDGRR---AALLERLKG-LGAQVFITTTDLEDLADLLEN 348
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
141-234 |
6.15e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499226461 141 LSGGQQQRVALARALVK---DPSLLLLDEPFSNLdaRMRDSARALvkEVQSRL---GVTLLVVSHDPaDIFAIADRV--- 211
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGL--HFHDIRKLL--EVLHRLvdkGNTVVVIEHNL-DVIKTADWIidl 901
|
90 100 110
....*....|....*....|....*....|
gi 499226461 212 -------GvlvkGKLVQVGKPEDLYDNPVS 234
Cdd:COG0178 902 gpeggdgG----GEIVAEGTPEEVAKVKAS 927
|
|
| |
