|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-350 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 539.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQ 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSPAMNLL 240
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMNLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 241 SLPCVDGNVQLGEQRHPLPPRHR--DQTRVWLGVRPEHITDrVEEGHLRLPATVLQRELMGADYLLHVSTPIGTLRFsRR 318
Cdd:COG3839 243 PGTVEGGGVRLGGVRLPLPAALAaaAGGEVTLGIRPEHLRL-ADEGDGGLEATVEVVEPLGSETLVHVRLGGQELVA-RV 320
|
330 340 350
....*....|....*....|....*....|..
gi 488976089 319 HRGTVPEKGESLQIGFSPADVHLFHAETQHNL 350
Cdd:COG3839 321 PGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-344 |
7.73e-158 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 446.47 E-value: 7.73e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQ 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSpaMNLL 240
Cdd:COG3842 165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--ANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 241 SLPCVDGN---VQLGEQRHPLPPRH--RDQTRVWLGVRPEHITDRVEEGHLRLPATVLQRELMGADYLLHVSTPIG-TLR 314
Cdd:COG3842 243 PGTVLGDEgggVRTGGRTLEVPADAglAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGqELV 322
|
330 340 350
....*....|....*....|....*....|.
gi 488976089 315 FSR-RHRGTVPEKGESLQIGFSPADVHLFHA 344
Cdd:COG3842 323 VRVpNRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-347 |
9.94e-154 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 436.20 E-value: 9.94e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK-PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSPAMNL 239
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAMNL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 240 LSLPCVDGNVQL---GEQRHPLP--PRHRDQTRVWLGVRPEHITDRVEEGhlRLPATVLQRELMGADYLLHVS---TPIg 311
Cdd:PRK11650 243 LDGRVSADGAAFelaGGIALPLGggYRQYAGRKLTLGIRPEHIALSSAEG--GVPLTVDTVELLGADNLAHGRwggQPL- 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 488976089 312 TLRFSRRHRgtvPEKGESLQIGFSPADVHLFHAETQ 347
Cdd:PRK11650 320 VVRLPHQER---PAAGSTLWLHLPANQLHLFDADTG 352
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-345 |
1.86e-128 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 372.44 E-value: 1.86e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNY 82
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 83 ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSPAMNLLSL 242
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMNFLPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 243 PCVD---GNVQL---GEQRHPLPPRHRDQT---RVWLGVRPEHITDrVEEGHLRLPATVLQRELMGADYLLHVSTPIGTL 313
Cdd:PRK11000 245 KVTAtaiEQVQVelpNRQQVWLPVEGRGVQvgaNMSLGIRPEHLLP-SDIADVTLEGEVQVVEQLGNETQIHIQIPAIRQ 323
|
330 340 350
....*....|....*....|....*....|...
gi 488976089 314 RFSRRHRGTVP-EKGESLQIGFSPADVHLFHAE 345
Cdd:PRK11000 324 NLVYRQNDVVLvEEGATFAIGLPPERCHLFRED 356
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
4.61e-120 |
|
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: 345.39 E-value: 4.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-341 |
4.55e-115 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 337.89 E-value: 4.55e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI-TATTPRERNFAMIFQ 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGspAMNLL 240
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 241 SLPCVDGNVQLGEQRHPLPPRHRDQTRVwLGVRPEHIT-DRVEEGHLRLPATVLQRELMGADYLLHVSTPIGTLR----- 314
Cdd:COG1118 241 RGRVIGGQLEADGLTLPVAEPLPDGPAV-AGVRPHDIEvSREPEGENTFPATVARVSELGPEVRVELKLEDGEGQpleae 319
|
330 340
....*....|....*....|....*...
gi 488976089 315 -FSRRHRGTVPEKGESLQIGFSPADVHL 341
Cdd:COG1118 320 vTKEAWAELGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-233 |
2.53e-114 |
|
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: 331.51 E-value: 2.53e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIG 233
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
3.14e-108 |
|
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: 315.23 E-value: 3.14e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-285 |
3.30e-107 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 318.81 E-value: 3.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSpaMNLLs 241
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIF- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 242 lpcvDGNV--QLGEQR-------HPLPPRHRDQTRV--WLGV--RPEHItdRVEEGH 285
Cdd:PRK09452 252 ----DATVieRLDEQRvranvegRECNIYVNFAVEPgqKLHVllRPEDL--RVEEIN 302
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-342 |
1.71e-104 |
|
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: 311.20 E-value: 1.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSwqpRVDKVAQMLQLEALLDRK---PAKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAE---VAERVAELLDLVGLPGSErkyPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 159 LSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSpaMN 238
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--VN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 239 LLSLPCV-DGNVQLGEQR-HPLPPRHRDQTRVWLGVRPEHITDR-VEEGHLRLPATVLQRELMGADYLLHVSTP-IGTLR 314
Cdd:TIGR03265 240 WLPGTRGgGSRARVGGLTlACAPGLAQPGASVRLAVRPEDIRVSpAGNAANLLLARVEDMEFLGAFYRLRLRLEgLPGQA 319
|
330 340 350
....*....|....*....|....*....|....
gi 488976089 315 F------SRRHRGTVpEKGESLQIGFSPADVHLF 342
Cdd:TIGR03265 320 LvadvsaSEVERLGI-RAGQPIWIELPAERLRAF 352
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-234 |
2.02e-98 |
|
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: 291.55 E-value: 2.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNYAL 84
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 85 FPHLSVRDNITFGMKVRKEE----KSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:cd03296 86 FRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGS 234
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-302 |
4.69e-94 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 284.30 E-value: 4.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSPamNLLS 241
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 242 LPCVDGNVQLGEQRHPLPP---RHRDQTRVWLGVRPEHITdRVEEGHLRLPATVLQRELMGADY 302
Cdd:PRK11432 245 ATLSGDYVDIYGYRLPRPAafaFNLPDGECTVGVRPEAIT-LSEQGEESQRCTIKHVAYMGPQY 307
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-233 |
4.53e-92 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 275.14 E-value: 4.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNYA 83
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 LFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLD 163
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 164 ARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIG 233
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-339 |
3.12e-91 |
|
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: 276.30 E-value: 3.12e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 32 LVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPR 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 112 VDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHD 191
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 192 QTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSpaMNLLSLPCVD----GNVQLGEQRHPLPPRH----R 263
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIErkseQVVLAGVEGRRCDIYTdvpvE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 264 DQTRVWLGVRPEHI---TDRVEEGHLRLPATVLQRELMGADYLLHVSTPIGTL-----RFSRRHRGTVPEKGESLQIGFS 335
Cdd:TIGR01187 239 KDQPLHVVLRPEKIvieEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKvlvseFFNEDDPHMSPSIGDRVGLTWH 318
|
....
gi 488976089 336 PADV 339
Cdd:TIGR01187 319 PGSE 322
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
9.58e-90 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 270.04 E-value: 9.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF----DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRernFA 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---RG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-347 |
2.49e-86 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 264.64 E-value: 2.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNYALF 85
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 86 PHLSVRDNITFGMKV--RKEEKSSW--QPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:PRK10851 87 RHMTVFDNIAFGLTVlpRRERPNAAaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSpaMNLLS 241
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE--VNRLQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 242 LPCVDGNVQLGEQRHPLP--PRHrdQTRVWLGVRPEHItDRVEEGHLR--LPATVLQRELMGADYLLHVStPIG------ 311
Cdd:PRK10851 245 GTIRGGQFHVGAHRWPLGytPAY--QGPVDLFLRPWEV-DISRRTSLDspLPVQVLEVSPKGHYWQLVVQ-PLGwynepl 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 488976089 312 TLRFSRRHrgTVPEKGESLQIGFSPAdvHLFHAETQ 347
Cdd:PRK10851 321 TVVMHGDI--DAPQRGERLFVGLQNA--RLYNGDER 352
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-233 |
1.51e-84 |
|
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: 255.72 E-value: 1.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFdGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIG 233
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-213 |
2.12e-83 |
|
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: 252.39 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRernFAM 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNG--GHVQQV 213
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-342 |
8.38e-83 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 255.39 E-value: 8.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKrfDGKP-ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF 79
Cdd:NF040840 1 MIRIENLSK--DWKEfKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:NF040840 79 QNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGspAMNL 239
Cdd:NF040840 159 SALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 240 LslpcvDGNVQLGEQRHPLP--------PRHRdQTRVWLGVRPEHI---TDRVEEGHLR-LPATVLQRELMGADYLLHVS 307
Cdd:NF040840 237 I-----EGVAEKGGEGTILDtgnikielPEEK-KGKVRIGIRPEDItisTEKVKTSARNeFKGKVEEIEDLGPLVKLTLD 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 488976089 308 TPIgTLRFSRRHRGTVP---EKGESLQIGFSPADVHLF 342
Cdd:NF040840 311 VGI-ILVAFITRSSFLDleiNEGKEVYASFKASAVHVF 347
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-247 |
4.21e-81 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 249.62 E-value: 4.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEA--LLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGS- 234
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAd 240
|
250
....*....|...
gi 488976089 235 PAMNLLSLPCVDG 247
Cdd:COG1125 241 RGLRRLSLLRVED 253
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-277 |
1.25e-78 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 245.90 E-value: 1.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQ 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSPAM--N 238
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVfeG 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488976089 239 LLSLPCVDGNV-QLGEQRHPLPPRHR----DQTRVWLGVRPEHI 277
Cdd:PRK11607 259 VLKERQEDGLViDSPGLVHPLKVDADasvvDNVPVHVALRPEKI 302
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
4-341 |
1.32e-78 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 245.29 E-value: 1.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:TIGR03258 8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPPHKRGLALLFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:TIGR03258 88 YALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTI-YVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGspAMNLL 240
Cdd:TIGR03258 168 LDANIRANMREEIAALHEELPELTIlCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLG--AANIL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 241 SLPCVDGNVQLGEQRHPLP---------PRHRDQTRVwLGVRPEH--ITDRvEEGHLRLPATVLQRELMGADYLLHVSTP 309
Cdd:TIGR03258 246 PAIALGITEAPGLVDVSCGgavifafgdGRHDGRDKL-ACIRPEHlaLTPR-PAGEGRFHATIASVEWHGAALHLLCDLD 323
|
330 340 350
....*....|....*....|....*....|....*.
gi 488976089 310 IG----TLRFSRRHRGTVPEKGESLQIGFSPADVHL 341
Cdd:TIGR03258 324 AAcdepMLVTMLRGRGPAPERGAKLALDCEADDAVL 359
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
9.08e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 235.71 E-value: 9.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGK---PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER--- 73
Cdd:COG1136 4 LLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 ---NFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNP 150
Cdd:COG1136 84 rrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQtEAMSMADRIVVMNGGHVQQVGR 215
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-235 |
3.32e-76 |
|
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: 234.89 E-value: 3.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL-EPvSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEP-TSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLE--ALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGSP 235
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-209 |
4.81e-74 |
|
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: 227.07 E-value: 4.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT----PRERNFAM 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGmkvrkeeksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGH 209
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-246 |
5.12e-73 |
|
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: 230.37 E-value: 5.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLqNISKRFDGkPALSAlSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI------WLHDENITATTPRERN 74
Cdd:COG4148 2 MLEV-DFRLRRGG-FTLDV-DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevLQDSARGIFLPPHRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGMKVRKEEKSswQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGRKRAPRAER--RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGfiGS 234
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GE 234
|
250
....*....|..
gi 488976089 235 PAMNLLSLPCVD 246
Cdd:COG4148 235 EAGSVLEATVAA 246
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-210 |
2.06e-72 |
|
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: 224.29 E-value: 2.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG----KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER---- 73
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 --NFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAmSMADRIVVMNGGHV 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-232 |
1.35e-71 |
|
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: 224.06 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 7 ISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE------RNFAMIFQ 80
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFI 232
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-232 |
6.85e-71 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 226.14 E-value: 6.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 21 SLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE------RNFAMIFQNYALFPHLSVRDNI 94
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 95 TFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSI 174
Cdd:COG4175 127 AFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDEL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 175 MALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFI 232
Cdd:COG4175 207 LELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-214 |
2.48e-69 |
|
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: 216.39 E-value: 2.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQnISKRFDGkpalsaLSLDIH---EGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI------WLHDENITATTPR 71
Cdd:cd03297 1 MLCVD-IEKRLPD------FTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 ERNFAMIFQNYALFPHLSVRDNITFGMKvrKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:cd03297 74 QRKIGLVFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-225 |
3.26e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 214.09 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITA--TTPRE--RNFA 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKlrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFG-MKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLApIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPAN 225
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-233 |
5.79e-68 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 213.46 E-value: 5.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPaLSAlSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQ 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-LRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFG----MKVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlrpgLKLTAEQRA----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIG 233
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-226 |
6.63e-68 |
|
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: 212.96 E-value: 6.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQN--YALFpHLSVRDNITFG---MKVRKEEKSSwqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLF 153
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGpenLGLPREEIRE---RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 154 LMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANL 226
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
1.40e-67 |
|
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: 212.53 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RNF 75
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNYALFPHLSVRDNITFGM----KVRKEEKsswQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrehtDLSEAEI---RELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPaNLFVAGF 231
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240
|
.
gi 488976089 232 I 232
Cdd:COG1127 241 L 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
4.59e-66 |
|
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: 217.08 E-value: 4.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK-----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--- 72
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 --RNFAMIFQN--YALFPHLSVRDNITFGMKVRKEEKSSWqpRVDKVAQMLQL----EALLDRKPAKLSGGQRQRVAMAR 144
Cdd:COG1123 340 lrRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAE--RRERVAELLERvglpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 145 AIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-233 |
2.27e-65 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 211.25 E-value: 2.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 9 KRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP------RERNFAMIFQNY 82
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 83 ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIG 233
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
2.66e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 206.06 E-value: 2.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RN 74
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 155 MDEPLSNLDARLRSEvrdsIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGR 215
Cdd:COG2884 161 ADEPTGNLDPETSWE----IMELLEEINrrgTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
1.89e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 204.53 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENItATTPRE--RNFAMIF 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEvrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKT-VLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
3.73e-63 |
|
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: 201.19 E-value: 3.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RNFA 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFGMKVRKEEKSSW-QPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-210 |
1.32e-62 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 198.89 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIF 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHlSVRDNITFGMKVRKEEKSswQPRVDKVAQMLQL-EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 159 LSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-209 |
2.92e-62 |
|
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: 198.07 E-value: 2.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQN--YALFpHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:cd03225 81 FQNpdDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGH 209
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-210 |
1.34e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 197.59 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RN 74
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGmkvRKEEKSSWQ------PRVDKVA-----QMLQLEALLDRKPAKLSGGQRQRVAMA 143
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAG---RLGRTSTWRsllglfPPEDRERalealERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-217 |
2.55e-61 |
|
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: 196.80 E-value: 2.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGmkvRKEEKSSWQP-------RVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:COG1120 81 PQEPPAPFGLTVRELVALG---RYPHLGLFGRpsaedreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-210 |
2.93e-61 |
|
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: 195.44 E-value: 2.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNF----AM 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFG-MKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-214 |
5.25e-61 |
|
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: 195.42 E-value: 5.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT-----PR 71
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 ERNFAMIFQNY--ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQL---EALLDRKPAKLSGGQRQRVAMARAI 146
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-210 |
3.03e-60 |
|
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: 193.87 E-value: 3.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF----DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RN 74
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNY--ALFPHLSVRDNITFGMKVRKEeksswQPRVDKVAQMLQL----EALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGL-----PDREERIAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-222 |
5.81e-59 |
|
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: 190.45 E-value: 5.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR-ERNFAMIF 79
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-209 |
1.61e-58 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 189.57 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPrERNFam 77
Cdd:NF040729 2 LKIQNISKTFINNkkenEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP-DRGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGH 209
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDK 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
8.60e-58 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 188.15 E-value: 8.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG----KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPrERnfA 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
1.44e-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: 194.74 E-value: 1.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS---EGQIWLHDENITATTPRER-- 73
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQN--YALFPhLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANL 226
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-224 |
6.48e-56 |
|
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: 186.47 E-value: 6.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRFdGKPALSAlSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITA------TTPRERNFAMIF 79
Cdd:TIGR02142 4 RFSKRL-GDFSLDA-DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKvrKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-205 |
2.14e-54 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 177.67 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPV--SEGQIWLHDENITATTPRERNFAM 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGM--KVRKEEksswqpRVDKVAQMLQ---LEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALppTIGRAQ------RRARVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSmADRIVVM 205
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDL 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-221 |
2.30e-54 |
|
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: 189.66 E-value: 2.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFpHLSVRDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAI 146
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLGDPDATDE------EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTsTIYVTHDqTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKG-RT-VIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
3.36e-54 |
|
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: 178.69 E-value: 3.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERN---FAM 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGM----------------KVRKEEKSSWQpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVA 141
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAharlgrgllaallrlpRARREEREARE-RAEELLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 142 MARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
...
gi 488976089 222 NPA 224
Cdd:COG0411 243 DPR 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
8.24e-54 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 177.00 E-value: 8.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---- 72
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 -RNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 152 LFLMDEPLSNLDarlrSEVRDSIMAL----HQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:cd03258 161 VLLCDEATSALD----PETTQSILALlrdiNRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-262 |
2.84e-53 |
|
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: 176.85 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIW------LHDENITatTPReR 73
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtLDEENLW--EIR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNyalfPH-----LSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:TIGR04520 78 KVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMsMADRIVVMNGGHVQQVGRPEYLYANPANLFV 228
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVELLKE 232
|
250 260 270
....*....|....*....|....*....|....
gi 488976089 229 AGfIGSPAMNLLSLpcvdgnvQLGEQRHPLPPRH 262
Cdd:TIGR04520 233 IG-LDVPFITELAK-------ALKKRGIPLPPDI 258
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-217 |
4.09e-53 |
|
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: 175.06 E-value: 4.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPV-----SEGQIWLHDENITA--TTPRE-- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 RNFAMIFQNYALFPhLSVRDNITFGMKVRKE-EKSSWQPRVDKVAQMLQL-EALLDR-KPAKLSGGQRQRVAMARAIVRN 149
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 150 PRLFLMDEPLSNLDARLRSEVRDSIMALHQQlkTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-210 |
4.47e-53 |
|
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: 172.97 E-value: 4.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR-ERNFAMIFQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNItfgmkvrkeeksswqprvdkvaqmlqlealldrkpaKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTStIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTI-LLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-224 |
7.73e-53 |
|
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: 174.55 E-value: 7.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERN---FAMI 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNI-----------TFGMKVRKEEKSSWQpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIV 147
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsgLLLARARREEREARE-RAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 148 RNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-209 |
2.29e-52 |
|
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: 171.03 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFpHLSVRDNItfgmkvrkeeksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQlKTsTIYVTHDqTEAMSMADRIVVMNGGH 209
Cdd:cd03228 123 ATSALDPETEALILEALRALAKG-KT-VIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
5.73e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 175.65 E-value: 5.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---- 72
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 -RNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:COG1135 81 rRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 152 LFLMDEPLSNLDarlrSEVRDSIMAL----HQQLKTSTIYVTHDqteaMS----MADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:COG1135 161 VLLCDEATSALD----PETTRSILDLlkdiNRELGLTIVLITHE----MDvvrrICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|...
gi 488976089 224 ANLFVAGFIGSPA 236
Cdd:COG1135 233 QSELTRRFLPTVL 245
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-214 |
6.21e-52 |
|
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: 171.58 E-value: 6.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 21 SLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNYALFPHLSVRDNITFGMKV 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 101 RKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQ 180
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 488976089 181 LKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-225 |
8.29e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 172.20 E-value: 8.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNF----A 76
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFG-MKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPAN 225
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-210 |
9.02e-52 |
|
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: 171.98 E-value: 9.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RNF 75
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNYALFPHLSVRDNITFGmkvRKEEKSSWQP---RVDKVAQMLQLEAL-----LD---RKPAKLSGGQRQRVAMAR 144
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG---RLGRRSTWRSlfgLFPKEEKQRALAALervglLDkayQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 145 AIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-210 |
1.43e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 172.17 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIwlhdenITATTP----RErNFAM 77
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPlaeaRE-DTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKvrkeekSSWQPRVdkvAQMLQLEALLDRK---PAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLK------GQWRDAA---LQALAAVGLADRAnewPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
1.46e-51 |
|
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: 170.35 E-value: 1.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR-ERNFAMIF 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVRKEEKSswQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 488976089 160 SNLDARLRSEVRDsIMALHQQLKTSTIYVTHDQTEA 195
Cdd:COG4133 160 TALDAAGVALLAE-LIAAHLARGGAVLLTTHQPLEL 194
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-203 |
4.20e-51 |
|
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: 168.95 E-value: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RNF-AM 77
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREKlGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDqTEAMSMADRIV 203
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKT-IIIVTHD-PEVAKQADRVI 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-224 |
7.07e-51 |
|
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: 172.16 E-value: 7.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEP---VSEGQIWLHDENITATTPRE- 72
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 -----RNFAMIFQN-Y-ALFPHLSVRDNITFGMKVRKeeKSSWQPRVDKVAQMLQL------EALLDRKPAKLSGGQRQR 139
Cdd:COG0444 81 rkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIHG--GLSKAEARERAIELLERvglpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 140 VAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 488976089 220 YANPA 224
Cdd:COG0444 239 FENPR 243
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
9.21e-51 |
|
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: 177.64 E-value: 9.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFpHLSVRDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIV 147
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLGRPDASDE------ELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 148 RNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTsTIYVTHDqTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RT-VILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-217 |
1.52e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 177.28 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFpHLS 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 90 VRDNITFGmkvrKEEKSswQPRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:COG1132 430 IRENIRYG----RPDAT--DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 159 LSNLDARLRSEVRDSIMALHQQlKTsTIYVTHdQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG1132 504 TSALDTETEALIQEALERLMKG-RT-TIVIAH-RLSTIRNADRILVLDDGRIVEQGTHE 559
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-209 |
2.87e-50 |
|
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: 165.11 E-value: 2.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQ 80
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 nyalfphlsvrdnitfgmkvrkeeksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGH 209
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
1.92e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.03 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRernFAMIFQ 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---IGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYAL---FPhLSVRDNITFGM--------KVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRN 149
Cdd:COG1121 83 RAEVdwdFP-ITVRDVVLMGRygrrglfrRPSRADRE----AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 150 PRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKT-ILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-214 |
3.50e-49 |
|
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: 162.99 E-value: 3.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQ 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 nyalfphlsvrdnitfgmkvrkeeksswqprvdkVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-210 |
3.51e-49 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 165.14 E-value: 3.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALsaLSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQ 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-208 |
5.17e-49 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 163.96 E-value: 5.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFD-GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RN 74
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-222 |
1.49e-48 |
|
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: 162.99 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNF---AMI 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGMKVRKEEKSSWqpRVDKVAQML-QLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKA--RLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-214 |
2.10e-48 |
|
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: 163.02 E-value: 2.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPrERnfAMIFQNYALFPHLSVRDNITF 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DR--MVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 97 GMK--VRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSI 174
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488976089 175 MALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-210 |
3.46e-48 |
|
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: 161.89 E-value: 3.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 20 LSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQNYALFPHLSVRDNITFGMK 99
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 100 VRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQ 179
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|.
gi 488976089 180 QLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-221 |
4.72e-48 |
|
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: 162.47 E-value: 4.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RN 74
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGmkvRKEEKSSWQ------PRVDKVAQM-----LQLEALLDRKPAKLSGGQRQRVAMA 143
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG---RLGYKPTWRsllgrfSEEDKERALsalerVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-241 |
1.35e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 162.08 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-RNF-A 76
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEiRKKiG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNY-ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK13632 87 IIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMsMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGfIGSP 235
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKAK-IDSP 244
|
....*.
gi 488976089 236 AMNLLS 241
Cdd:PRK13632 245 FIYKLS 250
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-230 |
3.20e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 160.64 E-value: 3.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLhdENITATTP-RERnfAMIF 79
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL--DGKPVEGPgAER--GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVRKEEKSSwqpRVDKVAQMLQ---LEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQ---RLEIAHQMLKkvgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVgrpEYLYANPANLFVAG 230
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRFVAG 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
4.32e-46 |
|
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: 156.83 E-value: 4.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPA----LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITA------TTP 70
Cdd:COG4181 8 IIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RERNFAMIFQNYALFPHLSVRDNITFGMkvrkEEKSSWQPRvDKVAQMLQ---LEALLDRKPAKLSGGQRQRVAMARAIV 147
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPL----ELAGRRDAR-ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 148 RNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAmSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAAT 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
5.10e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 158.25 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNY-ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
5.54e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 157.22 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMI-- 78
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 --------FQNYALFPHLSVRDNITFG-MKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRN 149
Cdd:PRK11264 83 lrqhvgfvFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 150 PRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
8.48e-46 |
|
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: 155.74 E-value: 8.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER-NFAMI 78
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 159 LSNLDARLRSEVRDSImaLHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:cd03263 161 TSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-224 |
2.32e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 157.97 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKP-----------ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP 70
Cdd:COG4608 8 LEVRDLKKHFPVRGglfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RE-----RNFAMIFQN-YA-LFPHLSVRDNITFGMKV----RKEEksswqpRVDKVAQMLQLEAL----LDRKPAKLSGG 135
Cdd:COG4608 88 RElrplrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIhglaSKAE------RRERVAELLELVGLrpehADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 136 QRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDqteaMSM----ADRIVVMNGGHVQ 211
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIV 237
|
250
....*....|...
gi 488976089 212 QVGRPEYLYANPA 224
Cdd:COG4608 238 EIAPRDELYARPL 250
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-226 |
2.58e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 156.46 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RNFAMIFQN--YALFp 86
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQFpeHQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 87 HLSVRDNITFG---MKVRKEEKSSwqpRVDKVAQMLQL-EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:TIGR04521 97 EETVYKDIAFGpknLGLSEEEAEE---RVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANL 226
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-214 |
3.14e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.17 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDE------NITATTPRE--R 73
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYALFPHLSVRDNITFG-MKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
3.66e-45 |
|
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: 162.63 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFpHLSVRDNITFGmkvrKEEKSSwqprvDKVAQML---QLEALLDRKP-----------AKLSGGQRQRVAMA 143
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLA----RPDATD-----EELWAALervGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTsTIYVTHDQTeAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RT-VLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 488976089 224 A 224
Cdd:COG4987 561 G 561
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-231 |
6.86e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 158.66 E-value: 6.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 21 SLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP------RERNFAMIFQNYALFPHLSVRDNI 94
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 95 TFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSI 174
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 175 MALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGF 231
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-160 |
1.17e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 150.49 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFPHLSVRDNI 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 95 TFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRK----PAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-214 |
1.58e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 153.25 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI---TATTPRE-----R 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAirelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYALFPHLSVRDN-ITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-208 |
1.40e-43 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 150.19 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPA---LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER--- 73
Cdd:TIGR02211 1 LLKCENLGKRYqEGKLDtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 ---NFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNP 150
Cdd:TIGR02211 81 rnkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMaDRIVVMNGG 208
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-210 |
1.97e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.72 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAM 77
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKeeksswQPRVDKVAQMLQLEALLDR---------KPAKLSGGQRQRVAMARAIVR 148
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRR------GGLIDWRAMRRRARELLARlgldidpdtPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 149 NPRLFLMDEPLSNLDARlrsEVrDSIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVM-NGGHV 210
Cdd:COG1129 158 DARVLILDEPTASLTER---EV-ERLFRIIRRLKaqgVAIIYISHRLDEVFEIADRVTVLrDGRLV 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-224 |
3.46e-43 |
|
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: 149.36 E-value: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERN---FAM 77
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEeKSSWQPRVDKVAQML-QLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRD-RAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-224 |
1.89e-42 |
|
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: 147.30 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF-- 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 -QNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 159 LSNLDARLRSEVRDSImalhQQLKTSTIYV---THDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:cd03218 161 FAGVDPIAVQDIQKII----KILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-210 |
8.55e-42 |
|
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: 145.24 E-value: 8.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENIT-----ATTPRERNFAM 77
Cdd:cd03292 3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-208 |
9.67e-42 |
|
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: 144.71 E-value: 9.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTpRERNFAMIFQN 81
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 --YALFPHlSVRDNITFGMKvrkeEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 160 SNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-208 |
1.05e-41 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 144.98 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRernFAMIFQNY 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 83 AL---FPhLSVRD--------NITFGMKVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:cd03235 78 SIdrdFP-ISVRDvvlmglygHKGLFRRLSKADKA----KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-224 |
1.82e-41 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 148.10 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 34 GPSGCGKSTLLRLLAGLEPVSEGQIWLHD------ENITATTPRERNFAMIFQNYALFPHLSVRDNITFGMKvrkeekSS 107
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA------KS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 108 WQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIY 187
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 488976089 188 VTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
2.05e-41 |
|
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: 142.57 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFA---MI 78
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgiaMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQnyalfphlsvrdnitfgmkvrkeeksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 159 LSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
14-210 |
3.13e-41 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 144.01 E-value: 3.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIW-----LHDENITATTPRERNFAMIFQNYALFPHL 88
Cdd:TIGR02982 18 KQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvlgqeLHGASKKQLVQLRRRIGYIFQAHNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 SVRDNITFGMKVrkEEKSSWQPRVDKVAQMLQ---LEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:TIGR02982 98 TARQNVQMALEL--QPNLSYQEARERARAMLEavgLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488976089 166 LRSEVRDSIMALHQQLKTSTIYVTHDqTEAMSMADRIVVMNGGHV 210
Cdd:TIGR02982 176 SGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-234 |
8.56e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.10 E-value: 8.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---- 72
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 -RNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:PRK11153 81 rRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 152 LFLMDEPLSNLDarlrSEVRDSIMAL----HQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLF 227
Cdd:PRK11153 161 VLLCDEATSALD----PATTRSILELlkdiNRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
....*..
gi 488976089 228 VAGFIGS 234
Cdd:PRK11153 237 TREFIQS 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-208 |
1.00e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 142.73 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIF 79
Cdd:cd03245 5 FRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFpHLSVRDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVR 148
Cdd:cd03245 85 QDVTLF-YGTLRDNITLGAPLADDE------RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 149 NPRLFLMDEPLSNLDarLRSEVRdSIMALHQQLKTST-IYVTHdQTEAMSMADRIVVMNGG 208
Cdd:cd03245 158 DPPILLLDEPTSAMD--MNSEER-LKERLRQLLGDKTlIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-223 |
3.93e-40 |
|
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: 148.29 E-value: 3.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGK-----------PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPvSEGQIWLHDENITATTP 70
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RE-----RNFAMIFQN-YA-LFPHLSVRDNITFGMKVRKEEKSSwQPRVDKVAQMLQ----LEALLDRKPAKLSGGQRQR 139
Cdd:COG4172 355 RAlrplrRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGPGLSA-AERRARVAEALEevglDPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 140 VAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
....
gi 488976089 220 YANP 223
Cdd:COG4172 514 FDAP 517
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-214 |
9.11e-40 |
|
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: 140.20 E-value: 9.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKP----ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLhDENITATTPRE--RN 74
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDVVKEPAEarRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITF-----GMKvRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRN 149
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYfaglyGLK-GDELTA----RLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 150 PRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
1.55e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.56 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG---LEPVS--EGQIWLHDENITATT--PRE-- 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGArvEGEILLDGEDIYDPDvdVVElr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 RNFAMIFQNYALFPHlSVRDNITFGMKVR----KEEKSswqprvDKVAQMLQLEALLD------RKPA-KLSGGQRQRVA 141
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYGLRLHgiksKSELD------EIVEESLRKAALWDevkdrlKKSAlGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 142 MARAIVRNPRLFLMDEPLSNLD--ARLRSEvrDSIMALHQQLktsTI-YVTHDQTEAMSMADRIVVMNGGHVQQVGRPEY 218
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILELKKDY---TIvIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
....*..
gi 488976089 219 LYANPAN 225
Cdd:COG1117 240 IFTNPKD 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-210 |
2.54e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 140.21 E-value: 2.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG---------KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR 71
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 E-----RNFAMIFQNY--ALFPHLSVRDNITFGMK-VRKEEKSSWQPRVDKVAQMLQL-EALLDRKPAKLSGGQRQRVAM 142
Cdd:PRK10419 83 QrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-222 |
6.00e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.80 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITAT----TPRERNFAMIFQ--NYALFPH 87
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 lSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQL--EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 166 LRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-221 |
3.29e-38 |
|
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: 136.59 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFpHLSVRDNITFGmkvrKEEKSswQPRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAI 146
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG----RPGAT--REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALhQQLKTsTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERL-MKNRT-TFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-214 |
4.34e-38 |
|
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: 135.40 E-value: 4.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVvLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERnfAMIF-- 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR--RRIGyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 -QNYALFPHLSVRDNITF-----GMKVRKEEKsswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLF 153
Cdd:cd03264 78 pQEFGVYPNFTVREFLDYiawlkGIPSKEVKA-----RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 154 LMDEPLSNLDARLRSEVRDsimaLHQQLKTSTIYV--THDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRN----LLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-210 |
5.85e-38 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 136.86 E-value: 5.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG---------KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR 71
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 E-----RNFAMIFQNY--ALFPHLSVRDNItfGMKVRKEEKSSWQPRVDKVAQMLQLEAL----LDRKPAKLSGGQRQRV 140
Cdd:TIGR02769 82 QrrafrRDVQLVFQDSpsAVNPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLrsedADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 141 AMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-208 |
6.59e-38 |
|
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: 134.65 E-value: 6.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNGG 208
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLI-SSHLLSEIQKVADRIGIINKG 202
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
7.09e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.08 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR--------- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 ---ER---NFAMIFQNYALFPHLSVRDNITFG-MKVRKeeksswQPRVDKVAQMlqlEALLDR---------KPAKLSGG 135
Cdd:COG4598 88 rqlQRirtRLGMVFQSFNLWSHMTVLENVIEApVHVLG------RPKAEAIERA---EALLAKvgladkrdaYPAHLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 136 QRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGR 215
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRT-MLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
250
....*....|....*....
gi 488976089 216 PEYLYANPANLFVAGFIGS 234
Cdd:COG4598 238 PAEVFGNPKSERLRQFLSS 256
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-210 |
1.10e-37 |
|
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: 133.11 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHlSVRDNItfgmkvrkeeksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 158 PLSNLDarlrSEVRDSIMALHQQLK---TSTIYVTHdQTEAMSMADRIVVMNGGHV 210
Cdd:cd03246 123 PNSHLD----VEGERALNQAIAALKaagATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-210 |
1.86e-37 |
|
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: 142.31 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFpHLS 89
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 90 VRDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:TIGR03375 555 LRDNIALGAPYADDE------EILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 159 LSNLDARLRSEVRDsimALHQQLKTST-IYVTHdQTEAMSMADRIVVMNGGHV 210
Cdd:TIGR03375 629 TSAMDNRSEERFKD---RLKRWLAGKTlVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
2.27e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.39 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT----------- 69
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrarlgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 70 -PRErnfAMIFQNyalfphLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:COG1137 83 lPQE---ASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 149 NPRLFLMDEPLSNLD--ArlrseVRDsIMALHQQLKTSTIYV--T-HDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:COG1137 154 NPKFILLDEPFAGVDpiA-----VAD-IQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
2.91e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.16 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAM 77
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGMKVRKEEKSSWQ---PRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKaarARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 155 MDEPLSNLDArlrSEVrDSIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG3845 165 LDEPTAVLTP---QEA-DELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-210 |
3.45e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 134.44 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-----DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP--RER 73
Cdd:COG1101 1 MLELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYAL--FPHLSVRDNI----------TFGMKVRKEEKSSWQprvDKVAQM-LQLEALLDRKPAKLSGGQRQRV 140
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLalayrrgkrrGLRRGLTKKRRELFR---ELLATLgLGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 141 AMARAIVRNPRLFLMDEPLSNLDARlRSEVrdsIMALHQQL----KTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPK-TAAL---VLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-217 |
4.65e-37 |
|
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: 133.67 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQ-IWLHDENITATTPRE--RNFAM 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWElrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 I---FQNYaLFPHLSVRD--------NITFGMKVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAI 146
Cdd:COG1119 83 VspaLQLR-FPRDETVLDvvlsgffdSIGLYREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
1.36e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT------PRERNFAMIFQ--NYALFPH 87
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkklkPLRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRD----NITFGMKVRKEEKsswqprvdKVAQMLQL----EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:PRK13634 102 TVEKDicfgPMNFGVSEEDAKQ--------KAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANL 226
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-217 |
1.54e-36 |
|
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: 138.40 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK-----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIW--LHDENITATTPR-- 71
Cdd:TIGR03269 279 IIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 -----ERNFAMIFQNYALFPHLSVRDNIT--FGMKVRKEEKSSWQPRVDKVAQMLQLEA--LLDRKPAKLSGGQRQRVAM 142
Cdd:TIGR03269 359 grgraKRYIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAVITLKMVGFDEEKAeeILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-223 |
3.17e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 133.94 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP-----RERNFAMIFQN-YA-LFPHL 88
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqklLRQKIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 SVRD--------NITFGMKVRKEeksswqprvdKVAQMLQLEAL----LDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:PRK11308 110 KVGQileeplliNTSLSAAERRE----------KALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-226 |
4.11e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.16 E-value: 4.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG---KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNF 75
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNY-ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEaMSMADRIVVMNGGHVQQVGRPEYLYANPANL 226
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
6.76e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 130.97 E-value: 6.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFG--------MKVRKEEKsswqprVDKVAQMLQLEALLDRKPAKLSGGQRQR--VAMarAIVR 148
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpyskgrLTAEDREI------IDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 149 NPRLFLMDEPLSNLD--------ARLRSEVRDsimalhqqLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG4604 153 DTDYVLLDEPLNNLDmkhsvqmmKLLRRLADE--------LGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-221 |
8.71e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 137.78 E-value: 8.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLE-PVSeGQIW-----LHDENITATtprERNF 75
Cdd:TIGR03797 454 VDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFEtPES-GSVFydgqdLAGLDVQAV---RRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNYALFPHlSVRDNITFGMKVRKEEksSWQprvdkVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMAR 144
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENIAGGAPLTLDE--AWE-----AARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIAR 601
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 145 AIVRNPRLFLMDEPLSNLDARLRSEVRDSImalhQQLKTSTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:TIGR03797 602 ALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
2.23e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 135.11 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGK-PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP--RERNFAMI 78
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHlSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQ-----LEALLDRKPAKLSGGQRQRVAMARAIVRNPRLF 153
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 154 LMDEPLSNLDARLRSEVRDSIMALHQqlKTSTIYVTHDqTEAMSMADRIVVM 205
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-219 |
3.63e-35 |
|
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: 128.11 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 13 GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFPHlSV 90
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 91 RDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:cd03254 94 MENIRLGRPNATDE------EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 160 SNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTeaMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKG-RTSIIIAHRLST--IKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-223 |
3.96e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 130.98 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI-WLhDENITATTPRER-----NFAMIFQN--YALFPH 87
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWL-GKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNITFGMKVRKEEKSSWQPRvDKVAQMLQ----LEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLD 163
Cdd:PRK15079 115 MTIGEIIAEPLRTYHPKLSRQEVK-DRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 164 ARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-217 |
4.51e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 128.59 E-value: 4.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGmkvRKEEKSSW-------QPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYG---RSPWLSLWgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-222 |
5.64e-35 |
|
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: 128.04 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKP---ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:cd03249 3 FKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPhLSVRDNITFG---MKVRKEEKSSWQPRVDKVAQML--QLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLF 153
Cdd:cd03249 83 SQEPVLFD-GTIAENIRYGkpdATDEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 154 LMDEPLSNLDARLRSEVRDsimALHQQLK-TSTIYVTHDQTeAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:cd03249 162 LLDEATSALDAESEKLVQE---ALDRAMKgRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-221 |
6.61e-35 |
|
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: 127.73 E-value: 6.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI---TATTPReRNFAMIFQNYALFpHL 88
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrevTLDSLR-RAIGVVPQDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 SVRDNITFG-MKVRKEEksswqprVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:cd03253 90 TIGYNIRYGrPDATDEE-------VIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQlKTsTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKG-RT-TIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-214 |
1.48e-34 |
|
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: 133.33 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHlSVRDNIT-FGmkvrkeeksswQPRVDKV---AQMLQLEALLDRKP-----------AKLSGGQRQRVAM 142
Cdd:COG4618 411 LPQDVELFDG-TIAENIArFG-----------DADPEKVvaaAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTeAMSMADRIVVMNGGHVQQVG 214
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFG 548
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
1.61e-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: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYAL-FPhLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIV-------RNP 150
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 151 RLFLMDEPLSNLDarlrsevrdsimaLHQQLKT------------STIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG4559 160 RWLFLDEPTSALD-------------LAHQHAVlrlarqlarrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-217 |
2.70e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYAL-FPhLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR------NPR 151
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 152 LFLMDEPLSNLDARlrsevrdsimalHQQL------------KTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:PRK13548 161 WLLLDEPTSALDLA------------HQHHvlrlarqlaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-208 |
2.70e-34 |
|
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: 125.27 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 8 SKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHdenitattpreRNFAMIFQNYALFPh 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-----------GSIAYVSQEPWIQN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNITFGMKVRKEeksswqpRVDKVAQMLQLEALLDRKPAK-----------LSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:cd03250 80 GTIRENILFGKPFDEE-------RYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 157 EPLSNLDARLRSEV-RDSIMALHQQLKTsTIYVTHdQTEAMSMADRIVVMNGG 208
Cdd:cd03250 153 DPLSAVDAHVGRHIfENCILGLLLNNKT-RILVTH-QLQLLPHADQIVVLDNG 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-219 |
9.30e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 124.40 E-value: 9.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWL--HDENITATTPReRNFAMIFQNY 82
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVagHDVVREPREVR-RRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 83 ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-213 |
1.20e-33 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 124.06 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHlSVRDNITFGMKVRKEeksswQPRVDKVAQMLQL----EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQ-----QPDPAIFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEaMSMADRIVVM--NGGHVQQV 213
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQEA 220
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-223 |
1.62e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 124.95 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKP---------ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITA--TTP 70
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYgdYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RERNFAMIFQ--NYALFPHLSV--------RDNITFGMKVRKEeksswqprvdKVAQMLQLEALL----DRKPAKLSGGQ 136
Cdd:COG4167 85 RCKHIRMIFQdpNTSLNPRLNIgqileeplRLNTDLTAEEREE----------RIFATLRLVGLLpehaNFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 137 RQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRP 216
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
....*..
gi 488976089 217 EYLYANP 223
Cdd:COG4167 235 AEVFANP 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-205 |
7.83e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 10 RFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGqiwlhdeniTATTPRERNFAMIFQNYAL---FP 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------TVRRAGGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 87 hLSVRDNITFGmkvRKEEKSSWQP-------RVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:NF040873 72 -LTVRDLVAMG---RWARRGLWRRltrddraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488976089 160 SNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSmADRIVVM 205
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-223 |
8.07e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 123.34 E-value: 8.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTpRERNFA---- 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMS-RSRLYTvrkr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 --MIFQNYALFPHLSVRDNITFGMKvrkeEKSSWQPRVDKVAQMLQLEALLDR-----KPAKLSGGQRQRVAMARAIVRN 149
Cdd:PRK11831 86 msMLFQSGALFTDMNVFDNVAYPLR----EHTQLPAPLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 150 PRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-210 |
8.95e-33 |
|
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: 120.61 E-value: 8.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISkrfdGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF- 79
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 -----QNYALFPHLSVRDNITFgmkvrkeeksswqprvdkvaqmlqlealldrkPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:cd03215 80 vpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-224 |
9.41e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.88 E-value: 9.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG----KPALSALSLDIHEGEFVVLVGPSGCGKS----TLLRLLAGLEPVSEGQIWLHDENITATTPRE 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 ------RNFAMIFQN--YALFPHLSVRDNITFGMKVRKeeKSSWQPRVDKVAQMLQL------EALLDRKPAKLSGGQRQ 138
Cdd:COG4172 86 lrrirgNRIAMIFQEpmTSLNPLHTIGKQIAEVLRLHR--GLSGAAARARALELLERvgipdpERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 139 RVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEY 218
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
....*.
gi 488976089 219 LYANPA 224
Cdd:COG4172 244 LFAAPQ 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 |
1.09e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 121.23 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT-------PRERn 74
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 famifqnyALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:cd03269 80 --------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-240 |
1.94e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.51 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKP---ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT--PRERNF 75
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNY-ALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYANPANLFVAGFIGS 234
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVP 242
|
....*.
gi 488976089 235 PAMNLL 240
Cdd:PRK13642 243 FSSNLM 248
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-210 |
3.32e-32 |
|
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: 120.32 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER---NFAMI 78
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGMKVRKEEKsswQPRVDKVAQMLQ-LEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS---RKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 158 PLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-212 |
3.79e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.31 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGK---PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP------ 70
Cdd:PRK11629 5 LLQCDNLCKRYqEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RERNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNP 150
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMaDRIVVMNGGHVQQ 212
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-191 |
4.33e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.95 E-value: 4.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHdenitattPRERnFAMIFQNYA 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--------KGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 LFPHLSVRDNITFG------MKVRKEEKS--------------------------SWQPRVDKVAQMLQL-EALLDRKPA 130
Cdd:COG0488 72 LDDDLTVLDTVLDGdaelraLEAELEELEaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 131 KLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsevrDSIMALHQQLKTST---IYVTHD 191
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLEEFLKNYPgtvLVVSHD 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-217 |
6.17e-32 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 120.17 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLE--PVSEGQIWLHDENITATTPRERnfA--- 76
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDER--Arag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 --MIFQNYALFPHLSVRDNITFGMKVRKEEKSS---WQPRVDKVAQMLQL-EALLDRkP--AKLSGGQRQRVAMARAIVR 148
Cdd:COG0396 79 ifLAFQYPVEIPGVSVSNFLRTALNARRGEELSareFLKLLKEKMKELGLdEDFLDR-YvnEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 149 NPRLFLMDEPLSNLDA-RLRSeVRDSIMALHQQlKTSTIYVTHDQT--EAMSmADRIVVMNGGHVQQVGRPE 217
Cdd:COG0396 158 EPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHYQRilDYIK-PDFVHVLVDGRIVKSGGKE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-208 |
1.13e-31 |
|
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: 119.08 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-----DGK--PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDE----NITATT 69
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 70 PRErnfamIfqnyalfphLSVRDNiTFG-----MKVRkeeksswqPRV---DKVAQML------------QLEALLDR-- 127
Cdd:COG4778 84 PRE-----I---------LALRRR-TIGyvsqfLRVI--------PRVsalDVVAEPLlergvdreearaRARELLARln 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 128 --------KPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSImalhQQLK---TSTIYVTHDqTEAM 196
Cdd:COG4778 141 lperlwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI----EEAKargTAIIGIFHD-EEVR 215
|
250
....*....|...
gi 488976089 197 S-MADRIVVMNGG 208
Cdd:COG4778 216 EaVADRVVDVTPF 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
1.17e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.24 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPA--LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFA 76
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQN-YALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK13648 87 IVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLY 220
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
2.35e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-RN-FAMIFQNY--ALFPh 87
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQDPddQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNITFG---MKVRKEEKSSwqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDA 164
Cdd:PRK13647 95 STVWDDVAFGpvnMGLDKDEVER---RVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 165 RLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLyANPANLFVAG---------FIGSP 235
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL-TDEDIVEQAGlrlplvaqiFEDLP 249
|
....*...
gi 488976089 236 AMNLLSLP 243
Cdd:PRK13647 250 ELGQSKLP 257
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-225 |
1.03e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.18 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL-----EPVSEGQIWLHDENI----TATTPR 71
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 ERNFAMIFQNYALFPhLSVRDNITFGMKVRKE----------EKSSWQPRV-DKVAQMLQLEALldrkpaKLSGGQRQRV 140
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkdkqvldeavEKSLKGASIwDEVKDRLHDSAL------GLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 141 AMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLktSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLY 220
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
....*
gi 488976089 221 ANPAN 225
Cdd:PRK14239 236 MNPKH 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
1.13e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL-----EPVSEGQIWLHDENITATTPRE--RN 74
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGMKVRK--EEKSSWQPRVDKVAQMLQL----EALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLktSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-233 |
1.40e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 116.87 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL-----EPVSEGQIWLHDENITA--TTPRE--RNFAMIFQNYALFPH 87
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdVDPIEvrREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNITFGMKVRKEEKSswQPRVDKVAQ-MLQLEALLDR-------KPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKS--KKELDERVEwALKKAALWDEvkdrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 160 SNLDARLRSEVRDSIMALHQQLktSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPAN----LFVAGFIG 233
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHelteKYVTGALG 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-210 |
1.54e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.90 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT-------PRER 73
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 nfamifqnyALFPHLSVRDNITF-----GMKvRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:COG4152 81 ---------GLYPKMKVGEQLVYlarlkGLS-KAEAKR----RADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-227 |
1.90e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 121.35 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKST----LLRLLAglepvSEGQIW-----LHDENITATTPRERNFAMIFQ-- 80
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWfdgqpLHNLNRRQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSSWQpRVDKVAQMLQlEALLD-----RKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVHQPTLSAAQ-REQQVIAVME-EVGLDpetrhRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLF 227
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-207 |
2.61e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 115.26 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP------RERNFAMIFQNYALFPHLSV 90
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaklRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 91 RDNITFGMKVRKE-EKSSWQPRVDKVAQmLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSE 169
Cdd:PRK10584 106 LENVELPALLRGEsSRQSRNGAKALLEQ-LGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 488976089 170 VRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-164 |
2.82e-30 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 114.59 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQ 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NyALFPHLSVRDNITFGMKVRKEEKSSwqprVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PRK13539 82 N-AMKPALTVAENLEFWAAFLGGEELD----IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
....
gi 488976089 161 NLDA 164
Cdd:PRK13539 157 ALDA 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-223 |
4.22e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.84 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--------- 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 ------RNFAMIFQNYALFPHLSVRDNITFG-MKVRKEEKSSWQPRVDKVAQMLQL-EALLDRKPAKLSGGQRQRVAMAR 144
Cdd:PRK10619 86 qlrllrTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 145 AIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-221 |
5.32e-30 |
|
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: 120.59 E-value: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHlSVRDNITFGmkvRKEEKSSwqPRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAI 146
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG---RTEQADR--AEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlkTSTIYVTHDQTeAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQG--RTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-221 |
5.68e-30 |
|
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: 114.89 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWL--HDENITATTPRERNFAM 77
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFpHLSVRDNITF---GMKVRK-EEKSSWQPRVDKVAQM-LQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALadpGMSMERvIEAAKLAGAHDFISELpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 153 FLMDEPLSNLDarLRSEvRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:cd03252 160 LIFDEATSALD--YESE-HAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-210 |
1.45e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.43 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RN 74
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRV----DKVaqmlqleALLDRK---PAKLSGGQRQRVAMARAIV 147
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVsaalDKV-------GLLDKAknfPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 148 RNPRLFLMDEPLSNLDARLrsevRDSIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDAL----SEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-210 |
2.93e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 118.67 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSAL---SLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP------ 70
Cdd:PRK10535 4 LLELKDIRRSYpSGEEQVEVLkgiSLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RERNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNP 150
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 151 RLFLMDEPLSNLDARLRSEVrdsiMALHQQLKT---STIYVTHDQTEAmSMADRIVVMNGGHV 210
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEV----MAILHQLRDrghTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-210 |
2.99e-29 |
|
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: 112.56 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKPA---LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR--ERNFAMIF 79
Cdd:cd03248 15 QNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHlSVRDNITFGMK-------VRKEEKSSWQPRVDKVAQMLQLEAllDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:cd03248 95 QEPVLFAR-SLQDNIAYGLQscsfecvKEAAQKAHAHSFISELASGYDTEV--GEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 153 FLMDEPLSNLDARLRSEVRdsiMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:cd03248 172 LILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-225 |
3.23e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 112.46 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 20 LSLDIHEGEFVVLVGPSGCGKST----LLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIFQN--YALFPHLSVRDN 93
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITFGMKVRkeEKSSWQPRVDKVAQML-----QLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRS 168
Cdd:TIGR02770 85 AIETLRSL--GKLSKQARALILEALEavglpDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 169 EVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPAN 225
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
4.17e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.93 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER-NFAMIFQ 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNIT-----FGMKVRKEEKSswqprVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK13536 122 FDNLDLEFTVRENLLvfgryFGMSTREIEAV-----IPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-224 |
4.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.16 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLH--DENITATTPRERNF-A 76
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQN-YALFPHLSVRDNITFG--------MKVRKeeksswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIV 147
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGpenlclppIEIRK--------RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 148 RNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDqTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-217 |
6.83e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.10 E-value: 6.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF----------------------DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 59 WLHdENITAttPRErnFAMIFQnyalfPHLSVRDNITF-----GMKvRKEEKSswqpRVDKVAQMLQLEALLDRkPAK-L 132
Cdd:COG1134 84 EVN-GRVSA--LLE--LGAGFH-----PELTGRENIYLngrllGLS-RKEIDE----KFDEIVEFAELGDFIDQ-PVKtY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 133 SGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQ 212
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
....*
gi 488976089 213 VGRPE 217
Cdd:COG1134 227 DGDPE 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-211 |
7.17e-29 |
|
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: 111.66 E-value: 7.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKR-FDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDEnitatTPRER------NF 75
Cdd:cd03267 22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-----VPWKRrkkflrRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIF-QNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:cd03267 97 GVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQ 211
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-230 |
1.03e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL---EPVSEGQIWLHDENITATTP---RERnFAMIFQNY-ALFP 86
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVwdiREK-VGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 87 HLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 167 RSEVRDSIMALHQQLKTSTIYVTHDQTEAmSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAG 230
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIG 241
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-221 |
1.62e-28 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 116.77 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWL--HDENITATTPRERNFAM 77
Cdd:TIGR01846 456 ITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVdgVDLAIADPAWLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHlSVRDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAI 146
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNPGAPFE------HVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 147 VRNPRLFLMDEPLSNLDArlrsEVRDSIMA-LHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:TIGR01846 609 VGNPRILIFDEATSALDY----ESEALIMRnMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-225 |
2.54e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.03 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLR-------LLAGLEpvSEGQIWLHDENITAT--TPRE 72
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPdvDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 --RNFAMIFQNYALFPHlSVRDNITFGMKVrkeekSSWQPRVDK-VAQMLQLEALLDRKPAKL-------SGGQRQRVAM 142
Cdd:PRK14243 89 vrRRIGMVFQKPNPFPK-SIYDNIAYGARI-----NGYKGDMDElVERSLRQAALWDEVKDKLkqsglslSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLD--ARLRSEvrdsimALHQQLKT--STIYVTHDQTEAMSMADRIVVMNG---------GH 209
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSDMTAFFNVeltegggryGY 236
|
250
....*....|....*.
gi 488976089 210 VQQVGRPEYLYANPAN 225
Cdd:PRK14243 237 LVEFDRTEKIFNSPQQ 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
4.40e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.51 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS-----EGQIWLHDENI----TATTPRE 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyerrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 RNFAMIFQNYALFPhLSVRDNITFGMKVrkeekSSWQPRV---DKVAQMLQLEALLDRKPAK-------LSGGQRQRVAM 142
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKI-----VGWRPKLeidDIVESALKDADLWDEIKHKihksaldLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNG-----GHVQQVGRPE 217
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
....*...
gi 488976089 218 YLYANPAN 225
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-214 |
4.51e-28 |
|
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: 109.16 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHdENITattprernfAMIFQNYALFPHLSVRDN 93
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR-GRVS---------SLLGLGGGFNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITF-----GMKvRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRS 168
Cdd:cd03220 105 IYLngrllGLS-RKEIDE----KIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488976089 169 EVRDSIMALHQQLKTStIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03220 180 KCQRRLRELLKQGKTV-ILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-210 |
4.64e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.35 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISkrfdGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAM 77
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQN---YALFPHLSVRDNIT---------FGMKVRKEEKSswqpRVDKVAQMLQLEAL-LDRKPAKLSGGQRQRVAMAR 144
Cdd:COG1129 332 VPEDrkgEGLVLDLSIRENITlasldrlsrGGLLDRRRERA----LAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 145 AIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-210 |
4.68e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNIS-KRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF- 79
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAy 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 -----QNYALFPHLSVRDNITFGmKVRKEEKSSW----QPRVDKVAQMLqLEAL------LDRKPAKLSGGQRQRVAMAR 144
Cdd:COG3845 338 ipedrLGRGLVPDMSVAENLILG-RYRRPPFSRGgfldRKAIRAFAEEL-IEEFdvrtpgPDTPARSLSGGNQQKVILAR 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 145 AIVRNPRLFLMDEPLSNLDARlrsevrdSIMALHQQLK------TSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVG-------AIEFIHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-210 |
1.08e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 107.25 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 13 GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPVS-EGQIWLHDENITATTPRERnFAMIFQNYALFPHLSV 90
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGvSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 91 RDNITFGMKVRKeeksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEV 170
Cdd:cd03213 100 RETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488976089 171 RDSIMALHQQLKTsTIYVTHD-QTEAMSMADRIVVMNGGHV 210
Cdd:cd03213 151 MSLLRRLADTGRT-IICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-227 |
1.53e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.40 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVsEGQIWLHDENITATTPRE--RNFAMIFQNYALFpHLS 89
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 90 VRDNITFGMKVRKEEksswqpRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:PRK11174 439 LRDNVLLGNPDASDE------QLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 159 LSNLDARLRSEVRDSIMALHQQlkTSTIYVTH--DQTEAMsmaDRIVVMNGGHVQQVGRPEYLYANPaNLF 227
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRR--QTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
1.77e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.47 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMI 78
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGMKVRKEEKSSWQPR----VDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTStIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTA-VAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-222 |
2.52e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER---NFAMI 78
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGMKVRKE-EKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 158 PLSNLDARLRSEVRDSImalhQQLKTSTIYV---THDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:PRK10895 164 PFAGVDPISVIDIKRII----EHLRDSGLGVlitDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-210 |
4.98e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGK--PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITA---TTPRErNFA 76
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseAALRQ-AIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHlSVRDNITFGmkvrKEEKSSwqprvDKVAQMLQ---LEALLDRKPA----------KLSGGQRQRVAMA 143
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLA----APNASD-----EALIEVLQqvgLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRSEvrdsIMAL---HQQLKTsTIYVTHDQTEAMSMaDRIVVMNGGHV 210
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQ----ILELlaeHAQNKT-VLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-221 |
5.94e-27 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 111.96 E-value: 5.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFD--GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIwLHDENITATTPRER---NFAMI 78
Cdd:TIGR03796 480 LRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI-LFDGIPREEIPREVlanSVAMV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHlSVRDNITFgmkvrkeekssWQPRV---------------DKVAQML-QLEALLDRKPAKLSGGQRQRVAM 142
Cdd:TIGR03796 559 DQDIFLFEG-TVRDNLTL-----------WDPTIpdadlvrackdaaihDVITSRPgGYDAELAEGGANLSGGQRQRLEI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDArlrsEVRDSIMALHQQLKTSTIYVTHdQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDP----ETEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-191 |
8.75e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 110.91 E-value: 8.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG-KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF- 79
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVc 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 -QNYALFpHLSVRDNITFGMKVRKEEKSSWqprvdkVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIV 147
Cdd:TIGR02868 415 aQDAHLF-DTTVRENLRLARPDATDEELWA------ALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488976089 148 RNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLktSTIYVTHD 191
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-214 |
9.56e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.55 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDE-----NITATTPRERNF 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AM------IFQNYA--LFPHLSVRDNI---TFGMKVR-----KEEKSSWQPRVDKVAqmlqleALLDRKPAKLSGGQRQR 139
Cdd:PRK11701 86 LLrtewgfVHQHPRdgLRMQVSAGGNIgerLMAVGARhygdiRATAGDWLERVEIDA------ARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 140 VAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-208 |
9.62e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 110.39 E-value: 9.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR---ERNFAMI 78
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFGmkvRKEEKSSWQPRVDKVAQ-MLQLEAL-LDRKP----AKLSGGQRQRVAMARAIVRNPRL 152
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLG---QLPHKGGIVNRRLLNYEaREQLEHLgVDIDPdtplKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 153 FLMDEPLSNLDARlrsEVrDSIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:PRK11288 162 IAFDEPTSSLSAR---EI-EQLFRVIRELRaegRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
1.89e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.84 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAM 77
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALF------------PHLSVRDNITFGM----KVRKEEKSSwqprVDKVAQMLQ---LEALLDRKPAKLSGGQRQ 138
Cdd:PRK11300 85 TFQHVRLFremtvienllvaQHQQLKTGLFSGLlktpAFRRAESEA----LDRAATWLErvgLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 139 RVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEY 218
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*
gi 488976089 219 LYANP 223
Cdd:PRK11300 241 IRNNP 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-210 |
2.00e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 109.76 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF- 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 --QNYALFPHLSVRDNITFGMKVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDE 157
Cdd:PRK15439 91 vpQEPLLFPNLSVKENILFGLPKRQASMQ----KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 158 PLSNLD----ARLRSEVRdsimALhQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK15439 167 PTASLTpaetERLFSRIR----EL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-217 |
2.13e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 104.93 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 22 LDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDEnitATTPRERNFAMIFQNYAL---FPhLSVRDNITFGM 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 99 K-----VRKEEKSSWQPrVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDS 173
Cdd:TIGR03771 77 TghigwLRRPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 174 IMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNG-----GHVQQVGRPE 217
Cdd:TIGR03771 156 FIELAGA-GTAILMTTHDLAQAMATCDRVVLLNGrviadGTPQQLQDPA 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-232 |
2.20e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRF---DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDE---------NITATTPReR 73
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLR-K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYALFPHLSVRDNITF-----GMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYplkshGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLktSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFV 228
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....
gi 488976089 229 AGFI 232
Cdd:PRK14246 249 EKYV 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-222 |
2.25e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHD---ENITATTPRERNFAMIFQNyalfPHLS- 89
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDNQi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 90 ----VRDNITFG---MKVRKEEKSSwqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:PRK13633 99 vatiVEEDVAFGpenLGIPPEEIRE---RVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
2.43e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.04 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG-KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-RNF-AM 77
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFvGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNY--ALFPHlSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK13652 83 VFQNPddQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-208 |
3.02e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.10 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR---ERNFAM 77
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGmkvRKEEKSSWQ-PRVD-----KVAQML----QLEALLDRKPAKLSGGQRQRVAMARAIV 147
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG---RHLTKKVCGvNIIDwremrVRAAMMllrvGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 148 RNPRLFLMDEPLSNLDarlRSEVrDSIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:PRK09700 162 LDAKVIIMDEPTSSLT---NKEV-DYLFLIMNQLRkegTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-210 |
4.17e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.09 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLePVSEGQIWLHDENITATTPRERNFA---- 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-ITGDKSAGSHIELLGRTVQREGRLArdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 -------MIFQNYALFPHLSVRDNITFGMKvrkEEKSSWQPRVDKVAQMLQLEAL--LDR---------KPAKLSGGQRQ 138
Cdd:PRK09984 83 ksrantgYIFQQFNLVNRLSVLENVLIGAL---GSTPFWRTCFSWFTREQKQRALqaLTRvgmvhfahqRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 139 RVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-190 |
6.09e-26 |
|
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: 102.82 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP-RERNFAMIFQ 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKV-RKEEKSSWqprvDKVAQMlQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIhGGAQRTIE----DALAAV-GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|.
gi 488976089 160 SNLDARlRSEVRDSIMALHQQLKTSTIYVTH 190
Cdd:TIGR01189 156 TALDKA-GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-222 |
6.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKP-----ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR------- 71
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 72 ERNFAMIFQ--NYALFPHlSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQL-EALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
7.16e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.09 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIWLHDENITATTPRE---RNF 75
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDterAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQP---RVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGIMDYDAmylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 153 FLMDEPLSNLDArlrSEVRdSIMALHQQLK---TSTIYVTHDQTEAMSMADRIVVM-NGGHV 210
Cdd:PRK13549 165 LILDEPTASLTE---SETA-VLLDIIRDLKahgIACIYISHKLNEVKAISDTICVIrDGRHI 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-214 |
8.31e-26 |
|
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: 108.20 E-value: 8.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:TIGR01842 317 LSVENVTIVPPGgkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHlSVRDNIT-FGMKVRKEEksswqprVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARA 145
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIArFGENADPEK-------IIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 146 IVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHdQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-216 |
9.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.44 E-value: 9.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNIS------KRFDGkPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT------ 69
Cdd:PRK13649 3 INLQNVSytyqagTPFEG-RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 70 PRERNFAMIFQnyalFPHL-----SVRDNITFGMK---VRKEEKSswQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVA 141
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQnfgVSQEEAE--ALAREKLALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 142 MARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRP 216
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-224 |
1.23e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.03 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI----TATTPRErNFA 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqTAKIMRE-AVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFGMKVrkEEKSSWQPRVDKVAQML-QLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQlkTSTIY-VTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQ--GMTIFlVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-233 |
3.18e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDE--------NITATTPRERNFAM 77
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPhLSVRDNITFGMKV-----RKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAhklvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLktSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANL----FV 228
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYV 262
|
....*
gi 488976089 229 AGFIG 233
Cdd:PRK14271 263 AGLSG 267
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-224 |
4.30e-25 |
|
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: 106.95 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 15 PALSALSLDIHEGEFVVLVGPSGCGKSTLLR-LLAGLEPVsEGQIwlHDENITATTPRErnfamifqnyALFPHLSVRDN 93
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHV--HMKGSVAYVPQQ----------AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITFGMKVrkeEKSSWQPRVDKVAQMLQLEAL-------LDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:TIGR00957 719 ILFGKAL---NEKYYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 167 RSEVRDSIMALHQQLKTST-IYVTHDQTeAMSMADRIVVMNGGHVQQVGR-PEYLYANPA 224
Cdd:TIGR00957 796 GKHIFEHVIGPEGVLKNKTrILVTHGIS-YLPQVDVIIVMSGGKISEMGSyQELLQRDGA 854
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-210 |
7.31e-25 |
|
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: 105.29 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIWLHDENITATTPRE---RNF 75
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDterAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQP----RVDKVAQMLQLEALLDRKP-AKLSGGQRQRVAMARAIVRNP 150
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDSIMALhQQLKTSTIYVTHDQTEAMSMADRI-VVMNGGHV 210
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTIcVIRDGQHV 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-223 |
7.93e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.57 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR--ERNFAMIFQNYALFPHlSVR 91
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 92 DNITFGMKVRKEEKSSWQPRV----DKVAQMLQ-LEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMAAAKAanahDFIMEFPNgYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 167 RSEVRDSimalhQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:TIGR00958 653 EQLLQES-----RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-210 |
7.97e-25 |
|
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: 105.67 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 15 PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFpHLSVRD 92
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 93 NITFGmkvrKEEKSswQPRVDKVAQMLQLEALLDRKPA-----------KLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:COG5265 451 NIAYG----RPDAS--EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 162 LDARLRSEVRDSIMALHQQLKT-------STIyvTHdqteamsmADRIVVMNGGHV 210
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTlviahrlSTI--VD--------ADEILVLEAGRI 570
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-217 |
9.33e-25 |
|
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: 104.88 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLE--PVSEGQI--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 59 ----------------WLHDENITATTpRERNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLE 122
Cdd:TIGR03269 81 pcpvcggtlepeevdfWNLSDKLRRRI-RKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 123 ALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHdQTEAMS-MADR 201
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDK 238
|
250
....*....|....*.
gi 488976089 202 IVVMNGGHVQQVGRPE 217
Cdd:TIGR03269 239 AIWLENGEIKEEGTPD 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
9.43e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 9.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER-NFAMIFQ 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNIT-----FGMKVRKEEKsswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK13537 88 FDNLDPDFTVRENLLvfgryFGLSAAAARA-----LVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-209 |
1.12e-24 |
|
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: 97.52 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHdenitattprernfamifqn 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 yalfphlsvrDNITFGMkvrkeeksswqprvdkVAQmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03221 61 ----------STVKIGY----------------FEQ--------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488976089 162 LDArlrsevrDSIMALHQQLKTST---IYVTHDQTEAMSMADRIVVMNGGH 209
Cdd:cd03221 101 LDL-------ESIEALEEALKEYPgtvILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-258 |
1.30e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE------RNFAMIFQ--NYALF 85
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 86 PHLSVRD------NITFGMKVRKEEKSSWQPRVDKVaqmlqlEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:PRK13641 100 ENTVLKDvefgpkNFGFSEDEAKEKALKWLKKVGLS------EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 160 SNLDARLRSEVRDsIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPaNLFVAGFIGSPAMNL 239
Cdd:PRK13641 174 AGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATSR 251
|
250
....*....|....*....
gi 488976089 240 LSLPCVDGNVQLGEQrhPL 258
Cdd:PRK13641 252 FASKLEKGGFKFSEM--PL 268
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-207 |
1.76e-24 |
|
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: 100.18 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 8 SKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENItATTPRErnfamIFQNYALfph 87
Cdd:cd03237 6 MKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQY-----IKADYEG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 lSVRDnitFGMKVRKEEKSSWQPRVDkVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLR 167
Cdd:cd03237 77 -TVRD---LLSSITKDFYTHPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488976089 168 SEVRDSI--MALHQQlKTSTIyVTHDQTEAMSMADRIVVMNG 207
Cdd:cd03237 152 LMASKVIrrFAENNE-KTAFV-VEHDIIMIDYLADRLIVFEG 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
2.30e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIWLHDENI----TATTPRERN 74
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKP-TSGEVLIKGEPIkydkKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 FAMIFQNY--ALF-PhlSVRDNITFG---MKVRKEEKsswQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:PRK13639 80 VGIVFQNPddQLFaP--TVEEDVAFGplnLGLSKEEV---EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 149 NPRLFLMDEPLSNLDARLRSevrdSIMALHQQLKTSTIYV---THDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP-- 223
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGAS----QIMKLLYDLNKEGITIiisTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIet 230
|
....*.
gi 488976089 224 ---ANL 226
Cdd:PRK13639 231 irkANL 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-211 |
2.49e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHdENITATTprernFAmifQ 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETVKIGY-----FD---Q 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALF-PHLSVRDNITFGMKVRKEEksswqprvdKVAQMlqLEALL------DRKPAKLSGGQRQRVAMARAIVRNPRLF 153
Cdd:COG0488 386 HQEELdPDKTVLDELRDGAPGGTEQ---------EVRGY--LGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 154 LMDEPLSNLDArlrsevrDSIMALHQQLKT---STIYVTHDQTEAMSMADRIVVMNGGHVQ 211
Cdd:COG0488 455 LLDEPTNHLDI-------ETLEALEEALDDfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-210 |
2.75e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.93 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGK-----PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI-WL--HDENITATTPRE--- 72
Cdd:PRK13651 5 VKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkDEKNKKKTKEKEkvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 --------------------RNFAMIFQ--NYALFPHlSVRDNITFG---MKVRKEEKsswQPRVDKVAQMLQL-EALLD 126
Cdd:PRK13651 85 eklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGpvsMGVSKEEA---KKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 127 RKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMN 206
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 488976089 207 GGHV 210
Cdd:PRK13651 240 DGKI 243
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-214 |
3.78e-24 |
|
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: 99.52 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDEN-----ITATTPRERNF 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AM------IFQNyalfPHLSVRDNITFGMKVR--------------KEEKSSWQPRVDKVAqmlqleALLDRKPAKLSGG 135
Cdd:TIGR02323 83 LMrtewgfVHQN----PRDGLRMRVSAGANIGerlmaigarhygniRATAQDWLEEVEIDP------TRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 136 QRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
6.49e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.31 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKP-----ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRER-- 73
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHEli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 ---------NF-------AMIFQ--NYALFPHlSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQL-EALLDRKPAKLSG 134
Cdd:PRK13631 101 tnpyskkikNFkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 135 GQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|
gi 488976089 215 RPEYLYANPA 224
Cdd:PRK13631 259 TPYEIFTDQH 268
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-214 |
1.61e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.84 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI-TATTPRERNFAMI 78
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNyalfPHL---SVRDNITfgmkvrkeeksswqprvdkvaqmlqlealldrkpAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:cd03247 81 NQR----PYLfdtTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 156 DEPLSNLDARLRSEVRDSIMalhQQLKTST-IYVTHDQTeAMSMADRIVVMNGGHVQQVG 214
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTlIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-208 |
1.74e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNIS-KRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIwlhdenitaTTPRERNfaMIF 79
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI---------ARPAGAR--VLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 ---QNYalFPHLSVRDNITFGmkvRKEEKSSwQPRVDKVAQMLQLEALLDR------KPAKLSGGQRQRVAMARAIVRNP 150
Cdd:COG4178 431 lpqRPY--LPLGTLREALLYP---ATAEAFS-DAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 151 RLFLMDEPLSNLDArlrsEVRDSIMA-LHQQLKTST-IYVTHdQTEAMSMADRIVVMNGG 208
Cdd:COG4178 505 DWLFLDEATSALDE----ENEAALYQlLREELPGTTvISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-232 |
1.93e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.58 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGK-PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR--ERNFAMIFQN 81
Cdd:PRK13657 338 DDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHlSVRDNITFGMKVRKEEKsswqprVDKVAQMLQLEALLDRKPAK-----------LSGGQRQRVAMARAIVRNP 150
Cdd:PRK13657 418 AGLFNR-SIEDNIRVGRPDATDEE------MRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDsimALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP---ANLF 227
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKA---ALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGgrfAALL 567
|
....*
gi 488976089 228 VAGFI 232
Cdd:PRK13657 568 RAQGM 572
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-221 |
2.82e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.86 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGK--PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI---TATTPRErNFA 76
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLASLRN-QVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFpHLSVRDNITFGmkvRKEEKSSWQprVDKVAQML-------QLEALLD----RKPAKLSGGQRQRVAMARA 145
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYA---RTEQYSREQ--IEEAARMAyamdfinKMDNGLDtvigENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 146 IVRNPRLFLMDEPLSNLDArlRSEvRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:PRK11176 495 LLRDSPILILDEATSALDT--ESE-RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-210 |
2.95e-23 |
|
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: 96.19 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL---EPVSEGQIWLHDENITATTPRERnFAMIFQNYALFPHLSVRDN 93
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITFGMKVRKEEKSSwQPRVDKVAQMLQLEALLDRKPAK-----LSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRS 168
Cdd:cd03234 102 LTYTAILRLPRKSS-DAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 169 EV-----------RDSIMALHQqlKTSTIYvthdqteamSMADRIVVMNGGHV 210
Cdd:cd03234 181 NLvstlsqlarrnRIVILTIHQ--PRSDLF---------RLFDRILLLSSGEI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-217 |
3.59e-23 |
|
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: 95.29 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLE--PVSEGQIWLHDENITATTPRERNFA--- 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHLSVRDNITFgmkvrkeeksswqprVDKvaqmlqlealldrkpaKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLRY---------------VNE----------------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSM-ADRIVVMNGGHVQQVGRPE 217
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-220 |
4.75e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT------PRERNFAMIFQ--NYALFPH 87
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDnITFGMK---VRKEEKSswQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDA 164
Cdd:PRK13643 101 TVLKD-VAFGPQnfgIPKEKAE--KIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 165 RLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLY 220
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
1.11e-22 |
|
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: 94.48 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITaTTPRE---RNFA 76
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHdlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHlSVRDNI-TFGMKVRKE-----EKSSWQPRVDkvAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNP 150
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLdPFGEYSDEElwqalERVGLKEFVE--SLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDSIMalhQQLKTST-IYVTHdQTEAMSMADRIVVMNGGHVQQVGRP 216
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIR---EAFKDCTvLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-243 |
1.15e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGK----PALSALSLDIHEGEFVVLVGPSGCGKS----TLLRLL--AGLEpVSEGQIWLHDENITATTP 70
Cdd:PRK10261 12 VLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLRRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RER-----------NFAMIFQN--YALFPHLSVRDNITFGMKVR----KEEKSSWQPRVDKVAQMLQLEALLDRKPAKLS 133
Cdd:PRK10261 91 SEQsaaqmrhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHqgasREEAMVEAKRMLDQVRIPEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 134 GGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQV 213
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260 270
....*....|....*....|....*....|....
gi 488976089 214 GRPEYLYANPANLFVAGFIGS----PAMNLLSLP 243
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAvpqlGAMKGLDYP 284
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-223 |
1.62e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.77 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE-----RNFAMIFQN-YA-LFPHL 88
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 SVRDNITFGMKVRKEEKSSWQPRvdKVAQMLQLEALLD----RKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDA 164
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 165 RLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-210 |
2.00e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIwlhdeNITATTPRE------RNFAMIF-QNYALF 85
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEV-----RVLGYVPFKrrkefaRRIGVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 86 PHLSVRDniTFGM--KVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR-LFLmDEPLSNL 162
Cdd:COG4586 109 WDLPAID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKiLFL-DEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-217 |
2.66e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.14 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNIS--KRfdgkpaLSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPvSEGQIWLHDENITATTPRE--RNFAM 77
Cdd:COG4138 1 LQLNDVAvaGR------LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 ifqnyalfphLSVRDNITFGMKV---------RKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:COG4138 74 ----------LSQQQSPPFAMPVfqylalhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 149 -----NP--RLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG4138 144 vwptiNPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETA 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-223 |
3.90e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.19 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF--DGKP--ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL----EPVSEGQIWLHDENITATTPRE 72
Cdd:PRK11022 3 LLNVDKLSVHFgdESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 R------NFAMIFQN--YALFPHLSVRDNITFGMKVRKEEKSSWqpRVDKVAQMLQL------EALLDRKPAKLSGGQRQ 138
Cdd:PRK11022 83 RrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKT--RRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 139 RVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEY 218
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*
gi 488976089 219 LYANP 223
Cdd:PRK11022 241 IFRAP 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-193 |
4.61e-22 |
|
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: 91.45 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIwlhdenitaTTPRERNFAMIFQNyALFPHLSVR 91
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFLPQR-PYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 92 DNITFgmkvrkeeksSWqprvDKVaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsEVR 171
Cdd:cd03223 82 EQLIY----------PW----DDV----------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESE 127
|
170 180
....*....|....*....|..
gi 488976089 172 DSIMALHQQLKTSTIYVTHDQT 193
Cdd:cd03223 128 DRLYQLLKELGITVISVGHRPS 149
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
4.84e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.14 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTP----RERNF 75
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQ--NYALFPhLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLF 153
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 154 LMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-208 |
6.79e-22 |
|
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: 92.39 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 13 GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI-W----LHDENITATTPRERNFAMIFQNYALFPH 87
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWsnknESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNITFGMKVRKE------EKSSWQPRVDKVAQMLQLEalLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:cd03290 93 ATVEENITFGSPFNKQrykavtDACSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488976089 162 LDARLRSEV-RDSIMALHQQLKTSTIYVTHdQTEAMSMADRIVVMNGG 208
Cdd:cd03290 171 LDIHLSDHLmQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-219 |
1.13e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR--ERNFAMIFQ 80
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGM--------KVRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRypwhgalgRFGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-190 |
1.73e-21 |
|
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: 91.02 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR-ERNFAMIFQNYALFPHLSV 90
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 91 RDNITFGMKVRKEEKSSwqprvDKVAQMlQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDArlRSEV 170
Cdd:cd03231 91 LENLRFWHADHSDEQVE-----EALARV-GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK--AGVA 162
|
170 180
....*....|....*....|.
gi 488976089 171 R-DSIMALHQQLKTSTIYVTH 190
Cdd:cd03231 163 RfAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-217 |
2.75e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 19 ALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFPHLSVRDNITF 96
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 97 G--------MKVRKEEKSSwqprVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRS 168
Cdd:PRK10253 105 GryphqplfTRWRKEDEEA----VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 169 EVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-221 |
3.18e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.78 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR--ERNFAMIFQNYALFPHlS 89
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 90 VRDNITFGMKVRkeEKSSWQprvdkVAQMLQLEALLDRKPA-----------KLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:PRK10790 431 FLANVTLGRDIS--EEQVWQ-----ALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 159 LSNLDARLRSEVRDSIMALHQQlkTSTIYVTHdQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-231 |
5.54e-21 |
|
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: 94.70 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFD--GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENI-TATTPRERNFAMIFQ 80
Cdd:TIGR01257 931 VKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEeksSWQPrvdkvAQmLQLEALLD---------RKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGR---SWEE-----AQ-LEMEAMLEdtglhhkrnEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDsiMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLyanpANLFVAGF 231
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWD--LLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-221 |
5.68e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT------PRERNFAMIFQnyalFPHL- 88
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirPVRKRIGMVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 ----SVRDNITFGMKvrkeeksSWQPRVDKVAQ-----MLQL---EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:PRK13646 98 lfedTVEREIIFGPK-------NFKMNLDEVKNyahrlLMDLgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 157 EPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-229 |
6.15e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.42 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITAT---TpRERNFAMIfQN 81
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiaT-RRRVGYMS-QA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNIT-----FGMkvrkeEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMD 156
Cdd:NF033858 348 FSLYGELTVRQNLElharlFHL-----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 157 EPLSNLD--ArlrsevRDSIMALHQQLktS-----TIYV-THDQTEAMSmADRIVVMNGGHVQQVGRPEYLYA--NPANL 226
Cdd:NF033858 423 EPTSGVDpvA------RDMFWRLLIEL--SredgvTIFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAarGAATL 493
|
....*.
gi 488976089 227 ---FVA 229
Cdd:NF033858 494 eeaFIA 499
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-228 |
6.21e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 26 EGEFVVLVGPSGCGKSTLLRLLAGLEP---VSEGQIWLHDENITATTPRERNfAMIFQNYALFPHLSVRDNITFGMKVR- 101
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 102 -----KEEKsswQPRVDKVAQMLQLealldRKPAK-----------LSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:TIGR00955 129 prrvtKKEK---RERVDEVLQALGL-----RKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 166 LRSEVRDSIMALHQqlKTSTIYVTHDQ--TEAMSMADRIVVMNGGHVQQVGRPEYL-------------YANPANLFV 228
Cdd:TIGR00955 201 MAYSVVQVLKGLAQ--KGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlghpcpeNYNPADFYV 276
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-214 |
8.77e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 93.65 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 13 GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHD---ENITATTPReRNFAMIFQNYALFPHlS 89
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLR-QFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 90 VRDNITFGMKVRKEEKSSWQP--------RVDKVAQMLQLEalLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:TIGR01193 564 ILENLLLGAKENVSQDEIWAAceiaeikdDIENMPLGYQTE--LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSN 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 162 LDARLRSEVRDSIMALhqQLKTsTIYVTHDQTEAmSMADRIVVMNGGHVQQVG 214
Cdd:TIGR01193 642 LDTITEKKIVNNLLNL--QDKT-IIFVAHRLSVA-KQSDKIIVLDHGKIIEQG 690
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-222 |
1.32e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 93.65 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPVSEGQIWLHDEniTATTPRernFAMIFqnyalfpHLSVRD 92
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--VAYVPQ---VSWIF-------NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 93 NITFGmkvrkeekSSWQP-RVDKVAQMLQLEALLDRKPA-----------KLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PLN03130 698 NILFG--------SPFDPeRYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 161 NLDARLRSEVRDSimALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:PLN03130 770 ALDAHVGRQVFDK--CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-223 |
2.37e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.08 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKP---------ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENIT--ATT 69
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 70 PRERNFAMIFQN--YALFPHLSVRDNITFGMKVRKEEKSswQPRVDKVAQMLQLEALLDRK----PAKLSGGQRQRVAMA 143
Cdd:PRK15112 84 YRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTDLEP--EQREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-270 |
3.03e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAmifq 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 nyALFPhLSVRDNITFGMKVRKEEKSSWQPRVdkvaqmlQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PRK09544 80 --TTLP-LTVNRFLRLRPGTKKEDILPALKRV-------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNgGHVQQVGRPEYLYANPAnlFVAGFiGSpamnll 240
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHPE--FISMF-GP------ 219
|
250 260 270
....*....|....*....|....*....|
gi 488976089 241 slpcvDGNVQLGEQRHPLPPRHRDQTRVWL 270
Cdd:PRK09544 220 -----RGAEQLGIYRHHHNHRHDLQGRIVL 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-222 |
3.97e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.96 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEgqiwlhdeniTATTPRERNFAMIFQNYALFpHLSVRDN 93
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----------TSSVVIRGSVAYVPQVSWIF-NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITFGMKVrkeEKSSWQPRVDKVAQMLQLEALLDR-------KPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:PLN03232 699 ILFGSDF---ESERYWRAIDVTALQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 167 RSEVRDSIMalHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYAN 222
Cdd:PLN03232 776 AHQVFDSCM--KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-214 |
4.26e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.15 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWlhdenitattpRERNFAMIFQNyALFPHLSVRDN 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITFgmkvRKEEKSSwqpRVDKVAQMLQLEALLDR-----------KPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:PTZ00243 741 ILF----FDEEDAA---RLADAVRVSQLEADLAQlgggleteigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 163 DARLRSEVRDSIMALHQQLKTStIYVTHdQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:PTZ00243 814 DAHVGERVVEECFLGALAGKTR-VLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-164 |
6.64e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.40 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPrERNFAMIF- 79
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 --QNyALFPHLSVRDNITFGMKVRKEeksswqPRVDKVAQMLQLEALLDRK--PAK-LSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK13538 80 ghQP-GIKTELTALENLRFYQRLHGP------GDDEALWEALAQVGLAGFEdvPVRqLSAGQQRRVALARLWLTRAPLWI 152
|
170
....*....|
gi 488976089 155 MDEPLSNLDA 164
Cdd:PRK13538 153 LDEPFTAIDK 162
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-223 |
1.24e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.16 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITAT---TPRERnFAMIFQNYALFPHlSV 90
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSWRSR-LAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 91 RDNITFGmkvrkeEKSSWQPRVDKVAQMLQLEALLDRKP-----------AKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:PRK10789 406 ANNIALG------RPDATQQEIEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 160 SNLDARLRSEVrdsIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK10789 480 SAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-223 |
1.24e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.42 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEP----VSEGQIWLHDENITATTPRER------NFAMIFQN--YA 83
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 LFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQL---------EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:COG4170 102 LDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELlhrvgikdhKDIMNSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-207 |
1.27e-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: 89.84 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRFDGKpALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIwlhDENIT-ATTPRErnfamIFQNYa 83
Cdd:COG1245 346 DLTKSYGGF-SLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGvLKP-DEGEV---DEDLKiSYKPQY-----ISPDY- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 lfpHLSVRDNItfgMKVRKEEKSS--WQPRVdkvAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSN 161
Cdd:COG1245 415 ---DGTVEEFL---RSANTDDFGSsyYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488976089 162 LDARLRSEVRDSIMALHQQLKTSTIYVTHDqteaMSM----ADRIVVMNG 207
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVFEG 531
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-208 |
1.37e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 89.65 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF-DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGL-EPVSeGQIWLHDENITATTPRE--RNFAM 77
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQS-GEILLDGKPVTAEQPEDyrKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDnitfGMKVRKEEKSSWQPRVdKVAQMLQLE--ALLDrkpAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PRK10522 402 VFTDFHLFDQLLGPE----GKPANPALVEKWLERL-KMAHKLELEdgRISN---LKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 156 DEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQtEAMSMADRIVVMNGG 208
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNG 525
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-208 |
2.05e-19 |
|
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: 86.83 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 13 GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIwLHDENITATTprerNFAMIFQNyalfphlSVR 91
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEP-SEGKI-KHSGRISFSS----QFSWIMPG-------TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 92 DNITFGMkvrkeekSSWQPRVDKVAQMLQLEALLDRKPAK-----------LSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:cd03291 116 ENIIFGV-------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTStIYVThDQTEAMSMADRIVVMNGG 208
Cdd:cd03291 189 YLDVFTEKEIFESCVCKLMANKTR-ILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-210 |
2.56e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.24 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITA----TTPRE---- 72
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqDPPRNvegt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 ---------RNFAMIFQNYALFPHLSVRD----NITFGMKVRK--EEKSSWQ--PRVDKVAQMLQLEAllDRKPAKLSGG 135
Cdd:PRK11147 83 vydfvaegiEEQAEYLKRYHDISHLVETDpsekNLNELAKLQEqlDHHNLWQleNRINEVLAQLGLDP--DAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 136 QRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsevrDSIMALHQQLKT---STIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-207 |
5.91e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.94 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRFDGKpALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIwlhDENIT-ATTPRErnfamIFQNYa 83
Cdd:PRK13409 345 DLTKKLGDF-SLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGvLKP-DEGEV---DPELKiSYKPQY-----IKPDY- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 lfpHLSVRDNItfgMKVRKEEKSSW-QPrvdKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:PRK13409 414 ---DGTVEDLL---RSITDDLGSSYyKS---EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488976089 163 DARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-243 |
9.16e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.93 E-value: 9.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF---DGK-PALSALSLDIHEGEFVVLVGPSGCGKS----TLLRLLAGlEPVSEGQIWLHDENITATTPRE 72
Cdd:PRK09473 12 LLDVKDLRVTFstpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 RN------FAMIFQN--YALFPHLSVRDNItfgMKVRKEEKS-SWQPRVDKVAQMLQL----EAlldRK-----PAKLSG 134
Cdd:PRK09473 91 LNklraeqISMIFQDpmTSLNPYMRVGEQL---MEVLMLHKGmSKAEAFEESVRMLDAvkmpEA---RKrmkmyPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 135 GQRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsEVRDSIMALHQQLK----TSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDV----TVQAQIMTLLNELKrefnTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488976089 211 QQVGRPEYLYANPANLFVAGFI-----------------GSPAmNLLSLP 243
Cdd:PRK09473 241 MEYGNARDVFYQPSHPYSIGLLnavprldaegeslltipGNPP-NLLRLP 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-224 |
1.11e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRF----DGKPALSALSLDIHEGEFVVLVGPSGCGKS----TLLRLLAGlEPVS--------EGQIWLHDEN 64
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS-PPVVypsgdirfHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 65 ITATTPRERNFAMIFQN--------YALFPHLSVRDNITFGMKvRKEEKSSWQPRVDKVAqMLQLEALLDRKPAKLSGGQ 136
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEpmvslnplHTLEKQLYEVLSLHRGMR-REAARGEILNCLDRVG-IRQAAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 137 RQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRP 216
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
....*...
gi 488976089 217 EYLYANPA 224
Cdd:PRK15134 242 ATLFSAPT 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-231 |
1.15e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATT----PRERNFA 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQN--YALFpHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK13638 81 TVFQDpeQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 155 MDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGF 231
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-200 |
1.54e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.69 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITAT-TPRERNFAMIF 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLSVRDNITFGMKVrkeekSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPL 159
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488976089 160 SNLDARLRSEVRDSIMAlHQQlKTSTIYVTHDQTEAMSMAD 200
Cdd:PRK13540 156 VALDELSLLTIITKIQE-HRA-KGGAVLLTSHQDLPLNKAD 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-216 |
5.75e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 81.30 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENItATTPRE---RNFA 76
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-STIPLEdlrSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHlSVRDNITfgmkvrkeeksswqpRVDKVAQMLQLEAL-LDRKPAKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLD---------------PFDEYSDEEIYGALrVSEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 156 DEPLSNLDARLRSEVRDSImalHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRP 216
Cdd:cd03369 150 DEATASIDYATDALIQKTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-221 |
6.85e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIfqny 82
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 83 A---------LFPHLSVRDNITF-----GMkvRKEEksswqpRVDKVAQMLQ---LEALLDRKPAKLSGGQRQRVAMARA 145
Cdd:NF033858 79 AympqglgknLYPTLSVFENLDFfgrlfGQ--DAAE------RRRRIDELLRatgLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 146 IVRNPRLFLMDE------PLS-----NLDARLRSEvRDSIMALhqqlkTSTIYvthdqteaMSMADR---IVVMNGGHVQ 211
Cdd:NF033858 151 LIHDPDLLILDEpttgvdPLSrrqfwELIDRIRAE-RPGMSVL-----VATAY--------MEEAERfdwLVAMDAGRVL 216
|
250
....*....|
gi 488976089 212 QVGRPEYLYA 221
Cdd:NF033858 217 ATGTPAELLA 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-209 |
7.50e-18 |
|
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: 85.35 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 13 GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIwLHDENITATTprernfamifQNYALFPHlSVR 91
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP-SEGKI-KHSGRISFSP----------QTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 92 DNITFGMkvrkeekSSWQPRVDKVAQMLQLEALLDRKPAK-----------LSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:TIGR01271 505 DNIIFGL-------SYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 161 NLDARLRSEVRDSIMALHQQLKTStIYVThDQTEAMSMADRIVVMNGGH 209
Cdd:TIGR01271 578 HLDVVTEKEIFESCLCKLMSNKTR-ILVT-SKLEHLKKADKILLLHEGV 624
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-210 |
7.96e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 20 LSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNFAMIF------QNYALFPHLSVRDN 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITfgmKVRKEEKSSWQPRVDKVAQMLQLEALLDRK------PAK-LSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:PRK15439 362 VC---ALTHNRRGFWIKPARENAVLERYRRALNIKfnhaeqAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488976089 167 RSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-217 |
9.58e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 84.08 E-value: 9.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF---DGKP--ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTpRER--- 73
Cdd:COG4615 328 LELRGVTYRYpgeDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN-REAyrq 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYALFPHLSVRDNitfgmkvrkeeksswQPRVDKVAQML-QLEalLDRKPA---------KLSGGQRQRVAMA 143
Cdd:COG4615 407 LFSAVFSDFHLFDRLLGLDG---------------EADPARARELLeRLE--LDHKVSvedgrfsttDLSQGQRKRLALL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRsEV--RDSIMALHQQLKTsTIYVTHDQTeAMSMADRIVVMNGGHVQQVGRPE 217
Cdd:COG4615 470 VALLEDRPILVFDEWAADQDPEFR-RVfyTELLPELKARGKT-VIAISHDDR-YFDLADRVLKMDYGKLVELTGPA 542
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-210 |
9.67e-18 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 80.38 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNIS----KRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS---EGQIWL--HDENITATTPRe 72
Cdd:cd03233 4 LSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYngIPYKEFAEKYP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 RNFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSwqprvdkvaqmlqlealldrkpaKLSGGQRQRVAMARAIVRNPRL 152
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVR-----------------------GISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyVTHDQT--EAMSMADRIVVMNGGHV 210
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEGRQ 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-215 |
1.04e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.55 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 6 NISKRFDGKPALSALSLDIHE-------------GEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIWLHDENITATTP 70
Cdd:PLN03211 60 NIKRILGHKPKISDETRQIQErtilngvtgmaspGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 71 RERNFamIFQNYALFPHLSVRDNITFGMKVR------KEEKSSWQPRVDKVAQMLQLEALL--DRKPAKLSGGQRQRVAM 142
Cdd:PLN03211 140 KRTGF--VTQDDILYPHLTVRETLVFCSLLRlpksltKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSI 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGR 215
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-208 |
1.28e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPR---ERNFAM 77
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQNYALFPHLSVRDNITFGmkvrKEEKSSW--------QPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRN 149
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLG----REFVNRFgridwkkmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 150 PRLFLMDEPlsnLDARLRSEVRdSIMALHQQLKTS---TIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:PRK10762 160 SKVIIMDEP---TDALTDTETE-SLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-191 |
2.08e-17 |
|
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: 83.45 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFD-GKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLhDENITAttprernfAMIFQN 81
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIKV--------GYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKvrkeEKSSWQPRVDKV---------------AQMLQLEALLD------------------RK 128
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVA----EIKDALDRFNEIsakyaepdadfdklaAEQAELQEIIDaadawdldsqleiamdalRC 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 129 P------AKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsevrDSIMALHQQLKT---STIYVTHD 191
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLQEypgTVVAVTHD 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-224 |
2.77e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.51 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGkPALSALSLDIHEGEFVVLVGPSGCGKS-TLLRLLAGLEP---VSEGQIWLHDENITATTPRERNFAM 77
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQN--YALFPHLSVRDNitfgmkVRKEEKSSWQPRVDkvAQMLQ-LEA--------LLDRKPAKLSGGQRQRVAMARAI 146
Cdd:PRK10418 84 IMQNprSAFNPLHTMHTH------ARETCLALGKPADD--ATLTAaLEAvglenaarVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPA 224
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-208 |
4.59e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIWLHDE-----NITATtpRER 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEvcrfkDIRDS--EAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYALFPHLSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQ---LEALLDRKPAKLSGGQRQRVAMARAIVRNP 150
Cdd:NF040905 79 GIVIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAkvgLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 151 RLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTStIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITS-IIISHKLNEIRRVADSITVLRDG 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-217 |
5.17e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRfdgkPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPvSEGQIWLHDENITATTPRERN------- 74
Cdd:PRK03695 1 MQLNDVAVS----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELArhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 75 ------FAM-IFQNYALfpHLSVRDNITFGMKVrkeeksswqprVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIV 147
Cdd:PRK03695 76 qqqtppFAMpVFQYLTL--HQPDKTRTEAVASA-----------LNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 148 R-----NP--RLFLMDEPLSNLD----ARLrsevrDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRP 216
Cdd:PRK03695 143 QvwpdiNPagQLLLLDEPMNSLDvaqqAAL-----DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
.
gi 488976089 217 E 217
Cdd:PRK03695 218 D 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-210 |
8.29e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 15 PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAMIFQNY---ALFPHL 88
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 SVRDNIT---------FGMKVRKEEKsswQPRVDKVAQMLQLEA-LLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEP 158
Cdd:PRK10762 346 SVKENMSltalryfsrAGGSLKHADE---QQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 159 LSNLDARLRSEvrdsIMALHQQLKT---STIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK10762 423 TRGVDVGAKKE----IYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-213 |
9.13e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKpaLSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAMIFQN 81
Cdd:PRK09700 269 RNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 Y---ALFPHLSVRDNITFGMKVRKEE-KSSW--------QPRVDKVAQMLQLE-ALLDRKPAKLSGGQRQRVAMARAIVR 148
Cdd:PRK09700 347 RrdnGFFPNFSIAQNMAISRSLKDGGyKGAMglfhevdeQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQV 213
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-226 |
1.36e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 15 PALSA-LSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRErnfaMIFQNYAL--------- 84
Cdd:PRK11288 266 PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD----AIRAGIMLcpedrkaeg 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 85 -FPHLSVRDNI---------TFGMKV--RKEEKSSwqprvDKVAQMLQLEALLDRKP-AKLSGGQRQRVAMARAIVRNPR 151
Cdd:PRK11288 342 iIPVHSVADNInisarrhhlRAGCLInnRWEAENA-----DRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQ-QVGRPEylyANPANL 226
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAgELAREQ---ATERQA 488
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-240 |
2.23e-15 |
|
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: 77.75 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITAttprerNFAMI 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVRDNITFG---MKVRKEEKSSWQPRVDKVA----QMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGrehLYLYARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKtSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLFVAGF 231
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTM 2169
|
250
....*....|
gi 488976089 232 -IGSPAMNLL 240
Cdd:TIGR01257 2170 kIKSPKDDLL 2179
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-216 |
2.25e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.25 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS--------EGQIWLHDENITATTPRE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 73 --RNFAMIFQ-NYALFPhLSVRDNITFGM--KVRKEEKSSWQPRvDKVAQMLQL---EALLDRKPAKLSGGQRQRVAMAR 144
Cdd:PRK13547 81 laRLRAVLPQaAQPAFA-FSAREIVLLGRypHARRAGALTHRDG-EIAWQALALagaTALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 145 AI---------VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGR 215
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
.
gi 488976089 216 P 216
Cdd:PRK13547 239 P 239
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-207 |
2.96e-15 |
|
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: 72.99 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 23 DIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPVSEGQIWlhdenitattprernfamifqnyalfphlsvrDNITFGMKVR 101
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGqLIPNGDNDEW--------------------------------DGITPVYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 102 KeeksswqprvdkvaqmlqlealldrkpAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQL 181
Cdd:cd03222 69 Y---------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....*.
gi 488976089 182 KTSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-219 |
3.80e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 54 SEGQIWLHDENITATTPRE-RN-FAMIFQNYALFpHLSVRDNITFGmkvrKEEKSswQPRVDKVAQMLQLEALLDRKPAK 131
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNlFSIVSQEPMLF-NMSIYENIKFG----KEDAT--REDVKRACKFAAIDEFIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 132 -----------LSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHdQTEAMSMAD 200
Cdd:PTZ00265 1348 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1426
|
170 180
....*....|....*....|....
gi 488976089 201 RIVVMN-----GGHVQQVGRPEYL 219
Cdd:PTZ00265 1427 KIVVFNnpdrtGSFVQAHGTHEEL 1450
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-207 |
4.02e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 74.33 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 26 EGEFVVLVGPSGCGKSTLLRLLAG-----LEPVSEGQIWlhDENITATTPRE-RNF-----------AMIFQNYALFPHL 88
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPPDW--DEILDEFRGSElQNYftkllegdvkvIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 ---SVRDNITfgmkvRKEEKSswqpRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:cd03236 103 vkgKVGELLK-----KKDERG----KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488976089 166 LRSEVRDSIMALHQQLKtSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-208 |
4.76e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAMIFQ 80
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRK----EEKSSWQprvDKVAQMLQLEALLD--RKPAKLSGGQRQRVAMARAIVRNPRLFL 154
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKgmfvDQDKMYR---DTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 155 MDEPLSNLDARlrsEVrDSIMALHQQLKT---STIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:PRK10982 158 MDEPTSSLTEK---EV-NHLFTIIRKLKErgcGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-192 |
4.90e-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: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEP--VSEGQIWLHDENItattPRERnfamif 79
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF----GREA------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 qnyalfphlSVRDNItfgmkvrkeeksswqPRVDKVAQMLQL--------EALLDRKPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:COG2401 101 ---------SLIDAI---------------GRKGDFKDAVELlnavglsdAVLWLRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQ 192
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-174 |
5.50e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 72.60 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKpALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATtpRERNFAMIFQ 80
Cdd:PRK13541 1 MLSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDNITFGMKVRKEEKSswqprVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PRK13541 78 NLGLKLEMTVFENLKFWSEIYNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170
....*....|....
gi 488976089 161 NLDARLRSEVRDSI 174
Cdd:PRK13541 153 NLSKENRDLLNNLI 166
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-227 |
6.45e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.17 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 15 PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENIT--ATTPRERNFAMIFQNYALFPHlSVRD 92
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 93 NIT-FGmkvRKEEKSSWqprvdKVAQMLQLEALLDRKPAKL-----------SGGQRQRVAMARAIVRNPRLFLMDEPLS 160
Cdd:PLN03232 1329 NIDpFS---EHNDADLW-----EALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 161 NLDARLRSEVRDSImalHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLF 227
Cdd:PLN03232 1401 SVDVRTDSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-206 |
8.05e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 20 LSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHD----ENITATTPRERnFAMIFQNYALFPHlSVRDNIT 95
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSK-IGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 96 FGM---------------------------------------------------KVRKEEKSSWQPRVDKVAQML----- 119
Cdd:PTZ00265 482 YSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIKDSEVVDVSKKVlihdf 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 120 ------QLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHdQT 193
Cdd:PTZ00265 562 vsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-RL 640
|
250
....*....|...
gi 488976089 194 EAMSMADRIVVMN 206
Cdd:PTZ00265 641 STIRYANTIFVLS 653
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-227 |
8.15e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKP-ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE--RNFAMIFQNYALFPHl 88
Cdd:PTZ00243 1320 EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 SVRDNITFGMKVRKEEksswqprvdkVAQMLQLEALLDRKPAKLSG--------------GQRQRVAMARAIVRNPRLF- 153
Cdd:PTZ00243 1399 TVRQNVDPFLEASSAE----------VWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSGFi 1468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488976089 154 LMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyvTHdQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLF 227
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTVITI--AH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-191 |
1.03e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 3 SLQNISKRFDG-KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLhDENITAttprernfAMIFQN 81
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-APGIKV--------GYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 82 YALFPHLSVRDNITFGMKvrkeEKSSWQPRVDKV---------------AQMLQLEALLD------------------RK 128
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVA----EVKAALDRFNEIyaayaepdadfdalaAEQGELQEIIDaadawdldsqleiamdalRC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 129 P------AKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsevrDSIMALHQQLKT---STIYVTHD 191
Cdd:PRK11819 155 PpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLEQFLHDypgTVVAVTHD 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-190 |
1.92e-14 |
|
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: 74.40 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 20 LSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGqiwlhdeniTATTPRERNFAMIFQNyalfPHLSV---RDNITF 96
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---------RLTKPAKGKLFYVPQR----PYMTLgtlRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 97 GMKVRK-EEKSSWQPRVDKVAQMLQLEALLDRKPA---------KLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDArl 166
Cdd:TIGR00954 538 PDSSEDmKRRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV-- 615
|
170 180
....*....|....*....|....
gi 488976089 167 rsEVRDSIMALHQQLKTSTIYVTH 190
Cdd:TIGR00954 616 --DVEGYMYRLCREFGITLFSVSH 637
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-211 |
4.19e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 20 LSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVS-EGQIWLHDENITATTPR---ERNFAMIFQN---YALFPHLSVRD 92
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 93 NIT------FGMKVRKEEKSSwQPRVDKVAQMLQLEALLDRKP-AKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:TIGR02633 359 NITlsvlksFCFKMRIDAAAE-LQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488976089 166 LRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQ 211
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-165 |
1.14e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 72.57 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 27 GEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIwlhdeNITATTPRERNFAMIF----QNYALFPHLSVRDNITFG--- 97
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDI-----RISGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSafl 980
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488976089 98 ---MKVRKEEKSSWqprVDKVAQMLQLEALLDR-----KPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:PLN03140 981 rlpKEVSKEEKMMF---VDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-203 |
1.53e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI-WlhDENItattprerNFAMIFQ 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkW--SENA--------NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYAL-FPH-LSVRDNItfgmkvrkeekSSW-QPRVDKvaQMLQ--LEALL---D--RKPAK-LSGGQRQRVAMARAIVRN 149
Cdd:PRK15064 390 DHAYdFENdLTLFDWM-----------SQWrQEGDDE--QAVRgtLGRLLfsqDdiKKSVKvLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 150 PRLFLMDEPLSNLDArlrsevrDSIMALHQQLKT---STIYVTHDQTEAMSMADRIV 203
Cdd:PRK15064 457 PNVLVMDEPTNHMDM-------ESIESLNMALEKyegTLIFVSHDREFVSSLATRII 506
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-192 |
2.00e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGlEP---VSEGQIWLHDENITATTPRERNFAM 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 I---FQNYALFPHLSVRDNITFGMKVRKeeKSSWQPRVDKVA------QMLQL----EALLDRKPAK-LSGGQRQRVAMA 143
Cdd:CHL00131 86 IflaFQYPIEIPGVSNADFLRLAYNSKR--KFQGLPELDPLEfleiinEKLKLvgmdPSFLSRNVNEgFSGGEKKRNEIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 144 RAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQ 192
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQ 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-207 |
2.22e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITaTTPRERNFAMIFQNYALFPHLSVR 91
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 92 DNITF--GMKVRKEEKSSwqprvdkvAQMLQLEALLDRKPA---KLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:PRK13543 101 ENLHFlcGLHGRRAKQMP--------GSALAIVGLAGYEDTlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488976089 167 RSEVrDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:PRK13543 173 ITLV-NRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-223 |
2.40e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEP----VSEGQIWLHDENITATTPRER------NFAMIFQ--NYA 83
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQepQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 LFPHLSVRDNIT-----FGMKVRKEEKSSWQPRvdKVAQMLQLEALLDRK------PAKLSGGQRQRVAMARAIVRNPRL 152
Cdd:PRK15093 102 LDPSERVGRQLMqnipgWTYKGRWWQRFGWRKR--RAIELLHRVGIKDHKdamrsfPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 153 FLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANP 223
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-192 |
2.46e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.05 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLE--PVSEGQIWLHDENITATTPRER---NF 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 76 AMIFQNYALFPHLS----VRDNITFGMKVRKEE---KSSWQPRVDKVAQMLQLEA-LLDRK-PAKLSGGQRQRVAMARAI 146
Cdd:PRK09580 81 FMAFQYPVEIPGVSnqffLQTALNAVRSYRGQEpldRFDFQDLMEEKIALLKMPEdLLTRSvNVGFSGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488976089 147 VRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQ 192
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQ 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-207 |
4.52e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 26 EGEFVVLVGPSGCGKSTLLRLLAG-LEP----VSEGQIWlhDENITAttprernfamiFQNYALFPHLS-VRDN-ITFGM 98
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGeLKPnlgdYDEEPSW--DEVLKR-----------FRGTELQDYFKkLANGeIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 99 KVR-------------KE--EKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLD 163
Cdd:COG1245 165 KPQyvdlipkvfkgtvREllEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488976089 164 ARLRSEVRDSIMALHQQLKtSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:COG1245 245 IYQRLNVARLIRELAEEGK-YVLVVEHDLAILDYLADYVHILYG 287
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-214 |
7.71e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.50 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 27 GEFVVLVGPSGCGKSTLLRLLAGLEPVS--EGQIWLHDENITATTPRERNFAMifQNYALFPHLSVRDNITFGMKVRKee 104
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRSTGYVE--QQDVHSPNLTVREALRFSALLRG-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 105 ksswqprvdkvaqmlqlealldrkpakLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDarlrSEVRDSIMALHQQLKTS 184
Cdd:cd03232 109 ---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD----SQAAYNIVRFLKKLADS 157
|
170 180 190
....*....|....*....|....*....|....*
gi 488976089 185 --TIYVTHDQTEA--MSMADRIVVM-NGGHVQQVG 214
Cdd:cd03232 158 gqAILCTIHQPSAsiFEKFDRLLLLkRGGKTVYFG 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-208 |
1.58e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 21 SLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEP-VSEGQIWLHDENITATTPRE---RNFAMIFQN---YALFPHLSVRDN 93
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 94 ITFGMKvrkeEKSSWQPRVDKVAQMLQLEALLDR----------KPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLD 163
Cdd:PRK13549 362 ITLAAL----DRFTGGSRIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488976089 164 ARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGG 208
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-207 |
1.61e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 26 EGEFVVLVGPSGCGKSTLLRLLAG-LEP----VSEGQIWlhDENItattpreRNFA-MIFQNYalFPHLS---VR----- 91
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGeLIPnlgdYEEEPSW--DEVL-------KRFRgTELQNY--FKKLYngeIKvvhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 92 ---DNI--TFGMKVRKE-EKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:PRK13409 167 qyvDLIpkVFKGKVRELlKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488976089 166 LRSEVRDSIMALHQqlKTSTIYVTHDQTEAMSMADRIVVMNG 207
Cdd:PRK13409 247 QRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAYG 286
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-218 |
1.73e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 66.76 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDEnitattprernFAMIFQNYALFPHLSVRDNIT 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 96 FGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIM 175
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488976089 176 ALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGR-----PEY 218
Cdd:PRK13546 188 EFKEQNKT-IFFVSHNLGQVRQFCTKIAWIEGGKLKDYGElddvlPKY 234
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
270-342 |
3.23e-12 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 61.48 E-value: 3.23e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 270 LGVRPEHItdRVEEGHLRLPATVLQRELMGADYLLHVSTPIGTLRFSRRHRGTV--PEKGESLQIGFSPADVHLF 342
Cdd:pfam08402 1 LAIRPEKI--RLAAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHArpPAPGDRVGLGWDPEDAHVL 73
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-207 |
6.19e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 12 DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTpRERNFAMIFQNYAL---FPHL 88
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVAYVPQSEEVdwsFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 sVRDNITFG----MKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDA 164
Cdd:PRK15056 97 -VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488976089 165 RLRSEVRDSIMALHQQLKTSTIyVTHDQTEAMSMADRIVVMNG 207
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCDYTVMVKG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-212 |
8.04e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.86 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPvSEGQIWLHD---ENITATTPReRNFA 76
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTLQTWR-KAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHlsvrdniTFGMKVRKEEKSSWQpRVDKVAQMLQLEALLDRKPAKL-----------SGGQRQRVAMARA 145
Cdd:TIGR01271 1296 VIPQKVFIFSG-------TFRKNLDPYEQWSDE-EIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARS 1367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488976089 146 IVRNPRLFLMDEPLSNLDARLRSEVRDSimaLHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQ 212
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKT---LKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
2.75e-11 |
|
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: 64.97 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNF--AMIFQNYALFPHlSVRDNI 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFkiTIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 95 T-FGmkvRKEEKSSWQprvdkVAQMLQLEALLDRKPAKL-----------SGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:TIGR00957 1381 DpFS---QYSDEEVWW-----ALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 163 DARLRSEVRDSImalHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYA 221
Cdd:TIGR00957 1453 DLETDNLIQSTI---RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-163 |
4.50e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPVSegqiwlhdENITATTPRERNFamiFQNY 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADS--------GRIHCGTKLEVAY---FDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 83 --ALFPHLSVRDNITFGmkvRKEEKSSWQPRvdKVAQMLQleallD--------RKPAK-LSGGQRQRVAMARAIVRNPR 151
Cdd:PRK11147 391 raELDPEKTVMDNLAEG---KQEVMVNGRPR--HVLGYLQ-----DflfhpkraMTPVKaLSGGERNRLLLARLFLKPSN 460
|
170
....*....|..
gi 488976089 152 LFLMDEPLSNLD 163
Cdd:PRK11147 461 LLILDEPTNDLD 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-212 |
6.98e-11 |
|
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: 62.18 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRF--DGKPALSALSLDIHEGEFVVLVGPSGCGKSTL----LRLLAglepvSEGQIWLHDENITATTPRE--R 73
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKwrK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 74 NFAMIFQNYALFPHlSVRDNITFGMKVRKEEksSWqprvdKVAQMLQLEALLDRKPAKL-----------SGGQRQRVAM 142
Cdd:cd03289 78 AFGVIPQKVFIFSG-TFRKNLDPYGKWSDEE--IW-----KVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 143 ARAIVRNPRLFLMDEPLSNLDARLRSEVRDSimaLHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQ 212
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKT---LKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-270 |
8.83e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQ-------IWL------------- 60
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshITRlsfeqlqklvsde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 61 -HDENITATTPRE----RNFAMIFQNyalfphlSVRDNitfgmkvrkeeksswqPRVDKVAQMLQLEALLDRKPAKLSGG 135
Cdd:PRK10938 83 wQRNNTDMLSPGEddtgRTTAEIIQD-------EVKDP----------------ARCEQLAQQFGITALLDRRFKYLSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 136 QRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGR 215
Cdd:PRK10938 140 ETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 216 PEYLYANPanlFVAGFIGSPAMNLLSLPCVDGNvqlgEQRHPLPPrhrDQTRVWL 270
Cdd:PRK10938 219 REEILQQA---LVAQLAHSEQLEGVQLPEPDEP----SARHALPA---NEPRIVL 263
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-208 |
1.17e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 27 GEFVVLVGPSGCGKSTLLRLLAglEPVSEGQIwLHDENITATTPRERNFAMIF----QNYALFPHLSVRDNITFGMKVR- 101
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVI-TGGDRLVNGRPLDSSFQRSIgyvqQQDLHLPTSTVRESLRFSAYLRq 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 102 -----KEEKSSWqprVDKVAQMLQLE----ALLDRKPAKLSGGQRQRVAMARAIVRNPRLFL-MDEPLSNLDARLRSevr 171
Cdd:TIGR00956 866 pksvsKSEKMEY---VEEVIKLLEMEsyadAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW--- 939
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488976089 172 dSIMALHQQLKTS--TIYVTHDQTEAMSMA--DRIVVMNGG 208
Cdd:TIGR00956 940 -SICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-227 |
1.29e-10 |
|
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: 61.08 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNISKRFDG--KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITAT---TPRERnFA 76
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 77 MIFQNYALFPHlSVRDNItfgmkvrKEEKSSWQPRVDKVAQMLQLEALLDRKPAKL-----------SGGQRQRVAMARA 145
Cdd:cd03288 99 IILQDPILFSG-SIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 146 IVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIyvTHDQTEAMSmADRIVVMNGGHVQQVGRPEYLYANPAN 225
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI--AHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
..
gi 488976089 226 LF 227
Cdd:cd03288 248 VF 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-227 |
1.30e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 15 PALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENIT--ATTPRERNFAMIFQNYALFPHlSVRD 92
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfGLMDLRKVLGIIPQAPVLFSG-TVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 93 NIT-FGMKVRKE-----EKSSWQPRVDKVAqmLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARL 166
Cdd:PLN03130 1332 NLDpFNEHNDADlweslERAHLKDVIRRNS--LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488976089 167 RSEVRDSImalHQQLKTSTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYLYANPANLF 227
Cdd:PLN03130 1410 DALIQKTI---REEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-210 |
1.62e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 14 KPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRE---RNFAMIFQ---NYALFPH 87
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNI----------TFGMKVRKEEKSSWQPRVDkvaqmlqleALLDRKPA------KLSGGQRQRVAMARAIVRNPR 151
Cdd:PRK10982 341 LDIGFNSlisnirnyknKVGLLDNSRMKSDTQWVID---------SMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 152 LFLMDEPLSNLDARLRSEVRDSIMALHQQLKtSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-163 |
2.59e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIWLHDENITATTPRERNfamifqnyAL 84
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD--------AL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 85 FPHLSVRDNITFG---MKVRKEEKSSwqprvdkvaqmlqlEALLDR----------KPAKLSGGQRQRVAMARAIVRNPR 151
Cdd:TIGR03719 398 DPNKTVWEEISGGldiIKLGKREIPS--------------RAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 488976089 152 LFLMDEPLSNLD 163
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-202 |
2.74e-10 |
|
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: 58.15 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 27 GEFVVLVGPSGCGKSTLLRLLAG-LEPVSEGQIWLHDENITATTPRERnfamifqnyalfphlsvrdnitfgmkvrkeek 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 106 sswqprvdkvaqmlqLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMA-----LHQQ 180
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSE 114
|
170 180
....*....|....*....|..
gi 488976089 181 LKTSTIYVTHDQTEAMSMADRI 202
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
88-219 |
7.25e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDNITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLR 167
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488976089 168 SEVRDSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVGRPEYL 219
Cdd:NF000106 181 NEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-195 |
2.41e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 4 LQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPV--------------SEGQIW---------- 59
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgysndltlfgrrrgSGETIWdikkhigyvs 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 60 --LHDENITATTPRERNFAMIFQNYALFPHLSVRDnitfgmkvrkeeksswQPRVDKVAQMLQLEALLDRKP-AKLSGGQ 136
Cdd:PRK10938 343 ssLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQ----------------QKLAQQWLDILGIDKRTADAPfHSLSWGQ 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 137 RQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKTSTIYVTHDQTEA 195
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-214 |
3.75e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIwlhdeNITATTprernfAMIFQNYALFPHLSVRDNIT 95
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA------ALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 96 FG---MKVRKEEKSSWQPRVDKVAQMLQLEalldRKPAK-LSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVR 171
Cdd:PRK13545 108 LKglmMGLTKEKIKEIIPEIIEFADIGKFI----YQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488976089 172 DSIMALHQQLKTsTIYVTHDQTEAMSMADRIVVMNGGHVQQVG 214
Cdd:PRK13545 184 DKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-214 |
2.22e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 16 ALSALSLDIHEGEFVVLVGPSGCGKSTLLrlLAGLEPVSEGQiwlhdenitattprernfamifqnYALFPHLSVRDNIT 95
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKAR------------------------LISFLPKFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 96 FgmkvrkeeksswqprVDKVAQMLQ--LEAL-LDRKPAKLSGGQRQRVAMARAIVRNPR--LFLMDEPLSNLDARLRSEV 170
Cdd:cd03238 64 F---------------IDQLQFLIDvgLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488976089 171 RDSIMALHQQlKTSTIYVTHDQTeAMSMADRIVVM------NGGHVQQVG 214
Cdd:cd03238 129 LEVIKGLIDL-GNTVILIEHNLD-VLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-210 |
8.12e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPAL-SALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPVSeGQIWlhdenitaTTPRERnFAMI 78
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSS-GTVF--------RSAKVR-MAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 79 FQNYALFPHLSVrDNITFGMKVRK---EEKSSWQPRVDKVAQMLQLEALLdrkpaKLSGGQRQRVAMARAIVRNPRLFLM 155
Cdd:PLN03073 578 SQHHVDGLDLSS-NPLLYMMRCFPgvpEQKLRAHLGSFGVTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 156 DEPLSNLDArlrsevrDSIMALHQQL---KTSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:PLN03073 652 DEPSNHLDL-------DAVEALIQGLvlfQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
233-277 |
1.22e-07 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 47.96 E-value: 1.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488976089 233 GSPAMNLLSLPCVDGN--VQLGEQRHPLPPRHRDQTR------VWLGVRPEHI 277
Cdd:pfam17912 1 GSPPMNFLPATVVEDGllVLGGGVTLPLPEGQVLALKlyvgkeVILGIRPEHI 53
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-191 |
1.91e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPvSEGQIWLhDENITATTPRERNFAmiF 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEP-SAGNVSL-DPNERLGKLRQDQFA--F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QN------------------------YALfPHLSVRDnitfGMKVRKEEKsswqprvdKVAQM-------------LQLE 122
Cdd:PRK15064 77 EEftvldtvimghtelwevkqerdriYAL-PEMSEED----GMKVADLEV--------KFAEMdgytaearagellLGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488976089 123 ALLDRKPAKLSG---GQRQRVAMARAIVRNPRLFLMDEPLSNLDArlrsevrDSIMALHQQL--KTST-IYVTHD 191
Cdd:PRK15064 144 IPEEQHYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDI-------NTIRWLEDVLneRNSTmIIISHD 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-213 |
3.94e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 24 IHEGEFVVLVGPSGCGKSTLLRLLA----GLEPVSEGQIWLHDENITATTPRER-NFAMIFQNYALFPHLSVRDNITFGM 98
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 99 KVRK--------EEKSSWQPRVDKVAQMLQLEALLDRKPAK-----LSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDAR 165
Cdd:TIGR00956 164 RCKTpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488976089 166 LRSEVRDSIMALHQQLK-TSTIYVTHDQTEAMSMADRIVVMNGGhvQQV 213
Cdd:TIGR00956 244 TALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEG--YQI 290
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-163 |
1.16e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 5 QNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQIwlhdeNITATTprerNFAMIFQNY-A 83
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIGETV----KLAYVDQSRdA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 84 LFPHLSVRDNITFG---MKVRKEEKSSwqprvdkvaqmlqlEALLDR---------KPAK-LSGGQRQRVAMARAIVRNP 150
Cdd:PRK11819 399 LDPNKTVWEEISGGldiIKVGNREIPS--------------RAYVGRfnfkggdqqKKVGvLSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 488976089 151 RLFLMDEPLSNLD 163
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-211 |
1.39e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 1 MLSLQNISKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAG-LEPVSeGQIWLhDENITATTPRERNFAMIF 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVS-GEIGL-AKGIKLGYFAQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 80 QNYALFPHLS----------VRDNI-TFGMKvrkeeksswqprVDKVAQmlqlealldrKPAKLSGGQRQRVAMARAIVR 148
Cdd:PRK10636 390 ADESPLQHLArlapqeleqkLRDYLgGFGFQ------------GDKVTE----------ETRRFSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488976089 149 NPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLktstIYVTHDQTEAMSMADRIVVMNGGHVQ 211
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
9-205 |
1.39e-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: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 9 KRFdgKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRllaglepvsegqiwlhdenitattprernfAMIFqnyalfphl 88
Cdd:cd03227 5 GRF--PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD------------------------------AIGL--------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 89 svrdnITFGMKVRKEEKSSWQPRVDKVAQMLQLEALLDrkpaKLSGGQRQRVAMA-----RAIVRNPrLFLMDEPLSNLD 163
Cdd:cd03227 44 -----ALGGAQSATRRRSGVKAGCIVAAVSAELIFTRL----QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488976089 164 ARLRSEVRDSIMAlHQQLKTSTIYVTHDQtEAMSMADRIVVM 205
Cdd:cd03227 114 PRDGQALAEAILE-HLVKGAQVIVITHLP-ELAELADKLIHI 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-226 |
1.41e-06 |
|
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: 50.01 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 125 LDRKPAKLSGGQRQRVAMARAI------VrnprLFLMDEPLSNLDARLRSEVRDSIMALhQQLKTSTIYVTHDQtEAMSM 198
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE-DTIRA 555
|
90 100 110
....*....|....*....|....*....|....
gi 488976089 199 ADRIVVM------NGGHVQQVGRPEYLYANPANL 226
Cdd:TIGR00630 556 ADYVIDIgpgageHGGEVVASGTPEEILANPDSL 589
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-210 |
1.98e-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: 48.02 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 17 LSALSLDIHEGEFVVLVGPSGCGKSTL----------LRLLAGLEPVSEGQIWLH-----------------DENITATT 69
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLGQMdkpdvdsieglspaiaiDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 70 PRErNFAMIFQNYALFPHLSVRDNItfgmkvrkeeksswqprVDKVAQMLQ--LEAL-LDRKPAKLSGGQRQRVAMARAI 146
Cdd:cd03270 91 PRS-TVGTVTEIYDYLRLLFARVGI-----------------RERLGFLVDvgLGYLtLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488976089 147 VRNPR--LFLMDEPLSNLDARLRSEVRDSIMALhQQLKTSTIYVTHDQtEAMSMADRIVVM------NGGHV 210
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDIgpgagvHGGEI 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-191 |
2.68e-06 |
|
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: 47.60 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 2 LSLQNIskrfdgKPALSALSLDIHEGeFVVLVGPSGCGKSTLLRL----LAGLEPVSeGQIWLHDENITATTPRERNFAM 77
Cdd:cd03240 4 LSIRNI------RSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEAlkyaLTGELPPN-SKGGAHDPKLIREGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 78 IFQN-----YALFPHLSVRDNITFgmkVRKEEkSSWqprvdkvaqmlqleaLLDRKPAKLSGGQRQ------RVAMARAI 146
Cdd:cd03240 76 AFENangkkYTITRSLAILENVIF---CHQGE-SNW---------------PLLDMRGRCSGGEKVlasliiRLALAETF 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488976089 147 VRNPRLFLMDEPLSNLDA-RLRSEVRDSIMALHQQLKTSTIYVTHD 191
Cdd:cd03240 137 GSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-218 |
2.20e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 24 IHEGEFVVLVGPSGCGKSTLLRLLAGLEPVSEGQI---------WLHDENITATTPR-------ERNFAmifQNYALFPH 87
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQETPALPQPAleyvidgDREYR---QLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 88 LSVRDN----ITFGMKVRKEEKSSWQPRVDKVAQMLQL-EALLDRKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNL 162
Cdd:PRK10636 101 ANERNDghaiATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488976089 163 DArlrsevrDSIMALHQQLKTST---IYVTHDQTEAMSMADRIVvmnggHVQQVGRPEY 218
Cdd:PRK10636 181 DL-------DAVIWLEKWLKSYQgtlILISHDRDFLDPIVDKII-----HIEQQSLFEY 227
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
16-52 |
9.42e-05 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 43.62 E-value: 9.42e-05
10 20 30
....*....|....*....|....*....|....*....
gi 488976089 16 ALSALSLDIHEGE-FVVLVGPSGCGKSTLLR-LLAGLEP 52
Cdd:COG3267 31 ALARLEYALAQGGgFVVLTGEVGTGKTTLLRrLLERLPD 69
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
125-226 |
2.38e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 125 LDRKPAKLSGGQRQRVAMARAI------VrnprLFLMDEPlsnldarlrsevrdSImALHQQ-----LKT---------S 184
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATQIgsglvgV----LYVLDEP--------------SI-GLHQRdndrlIETlkrlrdlgnT 539
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488976089 185 TIYVTHDQtEAMSMADRIVVM------NGGHVQQVGRPEYLYANPANL 226
Cdd:COG0178 540 VIVVEHDE-DTIRAADYIIDIgpgageHGGEVVAQGTPEEILKNPDSL 586
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
8-167 |
3.45e-04 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 42.64 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 8 SKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGlEPVSEGQIWLHDENI-------TATTPRERNFAMIFQ 80
Cdd:TIGR00602 91 KKIEEVETWLKAQVLENAPKRILLITGPSGCGKSTTIKILSK-ELGIQVQEWSNPTLPdfqkndhKVTLSLESCFSNFQS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 81 NYALFPHLSVRDnitfgmkvrkeeKSSWQPRVDKVAQMLQLeALLDRKPAKLSGGQR-QRVAMARAIVRNPRL---FLMD 156
Cdd:TIGR00602 170 QIEVFSEFLLRA------------TNKLQMLGDDLMTDKKI-ILVEDLPNQFYRDTRaLHEILRWKYVSIGRCplvFIIT 236
|
170
....*....|.
gi 488976089 157 EPLSNLDARLR 167
Cdd:TIGR00602 237 ESLEGDNNQRR 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-163 |
4.78e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 4.78e-04
10 20 30
....*....|....*....|....*....|....*..
gi 488976089 127 RKPAKLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLD 163
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
30-72 |
6.86e-04 |
|
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213788 Cd Length: 179 Bit Score: 40.17 E-value: 6.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488976089 30 VVLVGPSGCGKSTLLRLLagLEpvSEGQIWLhdeNITATT--PRE 72
Cdd:TIGR03263 3 IVISGPSGAGKSTLVKAL--LE--EDPNLKF---SISATTrkPRP 40
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
125-226 |
1.08e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 125 LDRKPAKLSGGQRQRVAMARAI------VrnprLFLMDEPlsnldarlrsevrdSImALHQQ-----LKT---------S 184
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEP--------------SI-GLHQRdndrlIETlkhlrdlgnT 543
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488976089 185 TIYVTHDQtEAMSMADRIVVM------NGGHVQQVGRPEYLYANPANL 226
Cdd:PRK00349 544 LIVVEHDE-DTIRAADYIVDIgpgagvHGGEVVASGTPEEIMKNPNSL 590
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
26-54 |
1.22e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 38.66 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|
gi 488976089 26 EGEFVVLVGPSGCGKSTLLR-LLAGLEPVS 54
Cdd:COG4639 1 MLSLVVLIGLPGSGKSTFARrLFAPTEVVS 30
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
8-85 |
1.37e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 39.17 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488976089 8 SKRFDGKPALSALSLDIHEGEFVVLVGPSGCGKSTLLRLLAGlEPVSEGQIWLHDENITATTPRERNFAMIFQNYALF 85
Cdd:pfam03215 26 RKIKDVQEWLDAMFLENAKHRILLISGPSGCGKSTVIKELSK-ELGPKYREWSNPTSFRSPPNQVTDFRGDCIVNSRF 102
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
30-72 |
1.40e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 38.28 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488976089 30 VVLVGPSGCGKSTLLRLlagLEPVSEGQIWLhdeNITATT--PRE 72
Cdd:cd00071 2 IVLSGPSGVGKSTLLKR---LLEEFDPNFGF---SVSHTTrkPRP 40
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-226 |
1.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 125 LDRKPAKLSGGQRQRVAMARAIvrNPRLF----LMDEPLSNLDARLRSEVRDSIMALHQQlKTSTIYVTHDQtEAMSMAD 200
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLAD 545
|
90 100 110
....*....|....*....|....*....|..
gi 488976089 201 RIVVMN------GGHVQQVGRPEYLYANPANL 226
Cdd:PRK00635 546 RIIDIGpgagifGGEVLFNGSPREFLAKSDSL 577
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
25-72 |
1.89e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 38.92 E-value: 1.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488976089 25 HEGEFVVLVGPSGCGKSTLLRLLagLEpvSEGQIWLhdeNITATT--PRE 72
Cdd:PRK00300 3 RRGLLIVLSGPSGAGKSTLVKAL--LE--RDPNLQL---SVSATTraPRP 45
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
131-210 |
3.15e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488976089 131 KLSGGQRQRVAMARAIVRNPRLFLMDEPLSNLDARLRSEVRDSIMALHQQLKtSTIYVTHDQTEAMSMADRIVVMNGGHV 210
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
27-72 |
5.12e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 37.74 E-value: 5.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488976089 27 GEFVVLVGPSGCGKSTLLRLLAGLEPvsegQIWLhdeNITATT--PRE 72
Cdd:COG0194 2 GKLIVLSGPSGAGKTTLVKALLERDP----DLRF---SVSATTrpPRP 42
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-49 |
5.68e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 5.68e-03
10 20
....*....|....*....|....
gi 488976089 26 EGEFVVLVGPSGCGKSTLLRLLAG 49
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-49 |
6.05e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 6.05e-03
|
| AAA_28 |
pfam13521 |
AAA domain; |
29-48 |
6.77e-03 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 36.86 E-value: 6.77e-03
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
30-48 |
7.16e-03 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 36.65 E-value: 7.16e-03
|
| |
