|
Name |
Accession |
Description |
Interval |
E-value |
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-357 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 613.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSPAM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 240 NFLEGSFSANGEQFIFDGlPFSIDANIGKRH-AGQPVALGIRPEHARLVPVGtpGAVPATVDFVEELGAGRVIHCDINGS 318
Cdd:PRK11650 241 NLLDGRVSADGAAFELAG-GIALPLGGGYRQyAGRKLTLGIRPEHIALSSAE--GGVPLTVDTVELLGADNLAHGRWGGQ 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 494964880 319 SFAVAVANHTSGETGQAVALELPRDNIHLFAQDTGLRLD 357
Cdd:PRK11650 318 PLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRIE 356
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-356 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 590.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSPAMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 241 FLEGSFSANGeqFIFDGLPFSIDANIGKrHAGQPVALGIRPEHARLVPVGtPGAVPATVDFVEELGAGRVIHCDINGSSF 320
Cdd:COG3839 241 LLPGTVEGGG--VRLGGVRLPLPAALAA-AAGGEVTLGIRPEHLRLADEG-DGGLEATVEVVEPLGSETLVHVRLGGQEL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 494964880 321 AVAVANHTSGETGQAVALELPRDNIHLFAQDTGLRL 356
Cdd:COG3839 317 VARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-350 |
2.40e-161 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 456.10 E-value: 2.40e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSpaMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--AN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 241 FLEGSF-SANGEQFIFDGLPFSIDANIGKRhAGQPVALGIRPEHARLVPVGTPGAVPATVDFVEELGAGRVIHCDI-NGS 318
Cdd:COG3842 241 LLPGTVlGDEGGGVRTGGRTLEVPADAGLA-AGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLgDGQ 319
|
330 340 350
....*....|....*....|....*....|....
gi 494964880 319 SFAVAVANHTSG--ETGQAVALELPRDNIHLFAQ 350
Cdd:COG3842 320 ELVVRVPNRAALplEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-351 |
9.74e-147 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 419.43 E-value: 9.74e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSPAMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 241 FLEGSFSANGEQFIF----DGLPFSIDANIGKRHAGQPVALGIRPEHarLVP-VGTPGAVPATVDFVEELGAGRVIHCDI 315
Cdd:PRK11000 241 FLPVKVTATAIEQVQvelpNRQQVWLPVEGRGVQVGANMSLGIRPEH--LLPsDIADVTLEGEVQVVEQLGNETQIHIQI 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 494964880 316 NG--SSFAVAVANHTSGETGQAVALELPRDNIHLFAQD 351
Cdd:PRK11000 319 PAirQNLVYRQNDVVLVEEGATFAIGLPPERCHLFRED 356
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-343 |
1.11e-123 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 360.23 E-value: 1.11e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN-QLEPRERGCAMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 162 SNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGspAMNF 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 242 LEGsfSANGEQFIFDGLPFSIDANIgkrhAGQPVALGIRPEHARLVPVGT-PGAVPATVDFVEELGAGRVIHCDINGSSf 320
Cdd:COG1118 240 LRG--RVIGGQLEADGLTLPVAEPL----PDGPAVAGVRPHDIEVSREPEgENTFPATVARVSELGPEVRVELKLEDGE- 312
|
330 340
....*....|....*....|...
gi 494964880 321 avavanhtsgetGQAVALELPRD 343
Cdd:COG1118 313 ------------GQPLEAEVTKE 323
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.35e-123 |
|
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: 354.64 E-value: 1.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
2.76e-118 |
|
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: 341.91 E-value: 2.76e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-349 |
5.00e-114 |
|
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: 335.85 E-value: 5.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSpaMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--VN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 241 FLEGSFSANGEQFIFDGlpfSIDANIGKRHAGQPVALGIRPEHARLVPVGT-PGAVPATVDFVEELGAGRVIHCDINGSS 319
Cdd:TIGR03265 240 WLPGTRGGGSRARVGGL---TLACAPGLAQPGASVRLAVRPEDIRVSPAGNaANLLLARVEDMEFLGAFYRLRLRLEGLP 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 494964880 320 FAVAVA-------NHTSGETGQAVALELPRDNIHLFA 349
Cdd:TIGR03265 317 GQALVAdvsasevERLGIRAGQPIWIELPAERLRAFA 353
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
4.83e-113 |
|
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: 327.94 E-value: 4.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-304 |
4.83e-107 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 318.81 E-value: 4.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSpaMNFLE 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIFD 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 244 GS-FSANGEQFI---FDGLPFSIDANIgKRHAGQPVALGIRPEHARLVPVGTPGAVPATVDFVEE 304
Cdd:PRK09452 253 ATvIERLDEQRVranVEGRECNIYVNF-AVEPGQKLHVLLRPEDLRVEEINDDEHAEGLIGYVRE 316
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-348 |
3.63e-101 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 303.07 E-value: 3.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAYGR-NPVVH---GVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ-----LEP 72
Cdd:NF040933 1 VTVRVENVTKIFKKgKKEVValdNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 73 RERGCAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 153 KVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGS 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 233 FIGSpaMNFLEGSFSANGeqfIFDGLPFSIDANIGKRHAGQpVALGIRPEHARLVP---VGTPGAV---PATVDFVE-EL 305
Cdd:NF040933 241 LIGD--INLLEGKVEEEG---LVDGNDLKIPLPNPKLEAGE-VIIGIRPEDIDISEsdmRLPPGFVevgKGRVKVSSyAG 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 494964880 306 GAGRVIHCDINGSSFAVAVANHTSGETGQAVALELPRDNIHLF 348
Cdd:NF040933 315 GVFRVVVSPIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
1.02e-100 |
|
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: 297.71 E-value: 1.02e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQ 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAgvPREER------DRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVK--PRSERppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGS 236
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-292 |
1.67e-98 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 296.25 E-value: 1.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 9 VRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQNYALYP 88
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 89 HMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKL 168
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 169 RVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSPamNFLEGSFSa 248
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFPATLS- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 494964880 249 nGEQFIFDGLPFSIDANIGKRHAGQPVALGIRPEHARLVPVGTP 292
Cdd:PRK11432 249 -GDYVDIYGYRLPRPAAFAFNLPDGECTVGVRPEAITLSEQGEE 291
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-338 |
1.44e-93 |
|
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: 282.85 E-value: 1.44e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 34 ILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRR 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 114 IKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 194 QVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSpaMNFLEGS-FSANGEQFIFDGL---PFSIDANIGKR 269
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATvIERKSEQVVLAGVegrRCDIYTDVPVE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 270 hAGQPVALGIRPEHARLV---PVGTPGAVPATVDFVEELGAGRVIHCDI--NGSSFAVAVAN----HTSGETGQAVAL 338
Cdd:TIGR01187 239 -KDQPLHVVLRPEKIVIEeedEANSSNAIIGHVIDITYLGMTLEVHVRLetGQKVLVSEFFNeddpHMSPSIGDRVGL 315
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-207 |
2.32e-92 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 276.97 E-value: 2.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAY----GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRerg 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 CAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVM 207
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
1.61e-89 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 268.98 E-value: 1.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-253 |
8.55e-89 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 271.57 E-value: 8.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVagVPREER------DRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTV--LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 158 DEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSp 237
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE- 239
|
250
....*....|....*.
gi 494964880 238 aMNFLEGSFsaNGEQF 253
Cdd:PRK10851 240 -VNRLQGTI--RGGQF 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-207 |
9.20e-85 |
|
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: 256.24 E-value: 9.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG----RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRergCAM 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVM 207
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-307 |
3.18e-82 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 254.23 E-value: 3.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYgRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:NF040840 2 IRIENLSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGspAMNFLE 243
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENIIE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 244 GSFSANGEQFIFDGLPFSIDAnigKRHAGQPVALGIRPEHARLV--PVGTPG--AVPATVDFVEELGA 307
Cdd:NF040840 239 GVAEKGGEGTILDTGNIKIEL---PEEKKGKVRIGIRPEDITISteKVKTSArnEFKGKVEEIEDLGP 303
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-237 |
2.01e-81 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 248.75 E-value: 2.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMV 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLED--FLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSP 237
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
2.69e-81 |
|
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: 248.02 E-value: 2.69e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGrNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIG 235
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-236 |
5.23e-80 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 247.31 E-value: 5.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMV 80
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGL--EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGS 236
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-282 |
4.88e-79 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 247.06 E-value: 4.88e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRieQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQ 82
Cdd:PRK11607 21 EIR--NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 163 NLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIGSpaMNFL 242
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 494964880 243 EGSFSANGEQFIF---DGL--PFSIDANIGKRHaGQPVALGIRPE 282
Cdd:PRK11607 257 EGVLKERQEDGLVidsPGLvhPLKVDADASVVD-NVPVHVALRPE 300
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-234 |
4.57e-76 |
|
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: 236.00 E-value: 4.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 7 EQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL------EPRERGCAMV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFI 234
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-225 |
8.96e-72 |
|
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: 223.70 E-value: 8.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGCA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAANMGYALKV-AGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 158 DEPLSNLD---AKLRVQMrveIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:COG1127 166 DEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
1.10e-70 |
|
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: 220.05 E-value: 1.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN----PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG--- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 ---CAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMtLADKLVVMYKGNV 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
4.67e-70 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 218.76 E-value: 4.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG----RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---- 75
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 76 ----GcaMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:COG1136 85 rrhiG--FVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 152 PKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQvEAMTLADKLVVMYKGNVE 213
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-235 |
4.64e-69 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 221.26 E-value: 4.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 11 KAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVID-DKVVNQ-----LEPRERGCAMVFQNY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDgENIMKQspvelREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 85 ALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 165 DAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFIG 235
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
3.46e-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: 214.47 E-value: 3.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN----QLEPRERGCAM 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMNVAANMGYAL-KVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 159 EPLSNLDAklrvQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP---RTR 228
Cdd:COG1126 162 EPTSALDP----ELVGEVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPqheRTR 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
3.89e-68 |
|
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: 212.43 E-value: 3.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLE----PRERGCAM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMNVAANMGYAlkvagvpreerdrriketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-216 |
1.95e-67 |
|
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: 211.77 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 28 SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ------LEPRERGCAMVFQNYALYPHMNVAANMGYALK 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 102 VAGvPREERDRrIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHK 181
Cdd:cd03297 102 RKR-NREDRIS-VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 494964880 182 RLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
2.95e-66 |
|
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: 210.04 E-value: 2.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG----RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGC 77
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNY--ALYPHMNVAANMGYALKVAGVPreERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDqVEAMT-LADKLVVMYKGNVEQVGTPLEVYNTPRT 227
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-222 |
8.03e-65 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 205.64 E-value: 8.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNyalyP-----HMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVF 155
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 156 LFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-225 |
1.23e-64 |
|
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: 205.43 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGCA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAANMGYALKVAGV-PREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 158 DEPLSNLD---AKLRVQMrveIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:cd03261 161 DEPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
3.19e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 204.14 E-value: 3.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVID--DKVVNQLEPRERgCAMVF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgeDVARDPAEVRRR-IGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 162 SNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
7.24e-64 |
|
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: 211.69 E-value: 7.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-----GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 -RGCAMVFQN--YALYPHMNVAANMGYALKVAGV-PREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAII 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 150 REPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHD--QVEAMtlADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
1.84e-62 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 200.86 E-value: 1.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYG----RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPrERG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 caMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:COG4525 80 --VVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVM 207
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-210 |
4.08e-62 |
|
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: 198.14 E-value: 4.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ-----LEPRERgCA 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkniNELRQK-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAANMGYAL-KVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 158 DEPLSNLDAklrvQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:cd03262 160 DEPTSALDP----ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-238 |
6.15e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.84 E-value: 6.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN----PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE----- 74
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 155 FLFDEPLSNLDAK-----LRVqmrveIRRLHKRLSATSVFVTHDqveaM----TLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:COG1135 162 LLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|...
gi 494964880 226 RTRFVGSFIGSPA 238
Cdd:COG1135 233 QSELTRRFLPTVL 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-217 |
1.45e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 197.28 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVvhGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-210 |
1.95e-61 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 196.15 E-value: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGR--NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG--CAMV 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNyalyP-HM----NVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVF 155
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 156 LFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
2.86e-61 |
|
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: 196.65 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN----PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE----- 74
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHdQVEAM-TLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-317 |
5.12e-61 |
|
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: 199.94 E-value: 5.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ------LEPRERGCAMVFQNYALYPHMNVAAN 95
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYALKVAgvPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVE 175
Cdd:COG4148 98 LLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 176 IRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNtpRTRFVGSFIGSPAMNFLEGSFSANGEQF-- 253
Cdd:COG4148 176 LERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS--RPDLLPLAGGEEAGSVLEATVAAHDPDYgl 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 254 ---IFDGLPFSIDAniGKRHAGQPVALGIRPEH---ARLVPVGTP--GAVPATVDFVEELGAGRV-IHCDING 317
Cdd:COG4148 254 trlALGGGRLWVPR--LDLPPGTRVRVRIRARDvslALEPPEGSSilNILPGRVVEIEPADGGQVlVRLDLGG 324
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
1.27e-59 |
|
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: 192.34 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY----GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL-----EPRE 74
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQNY--ALYPHMNVAANMGYALKVAGVPR--EERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAII 149
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 150 REPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGN-VEQ 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-198 |
3.07e-59 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.03 E-value: 3.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494964880 158 DEPLSNLDAklrvQMRVEIRRLHKRLSA--TSVFV-THDQ--VEAM 198
Cdd:COG2884 162 DEPTGNLDP----ETSWEIMELLEEINRrgTTVLIaTHDLelVDRM 203
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
4.04e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.11 E-value: 4.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAAN-----MGY--ALKVA--GVPREERDRRIKETARiVGLEDFLDRKPAELSGGQRQRVAMGRAI 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlagrLGRtsTWRSLlgLFPPEDRERALEALER-VGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 149 IREPKVFLFDEPLSNLDAKL-RVQMRVeIRRLHKRLSATSVFVTHdQVE-AMTLADKLVVMYKGNV 212
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
2.67e-57 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 187.17 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGC--AMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARriAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVA--ANMG-YA-LKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:COG1120 82 QEPPAPFGLTVRelVALGrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 158 DEPLSNLDakLRVQMRV--EIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG1120 162 DEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-225 |
1.86e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 184.53 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG----CAM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqeAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMNVAANMGYA-LKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 159 EPLSNLDAKLrvqmRVEIRRLHKRLS---ATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK09493 162 EPTSALDPEL----RHEVLKVMQDLAeegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-221 |
2.52e-56 |
|
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: 184.29 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK-VVNQLEPRERGCAMVFQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 163 NLDAKLRVQMRVEIRRLhKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
6.61e-56 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 190.88 E-value: 6.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDIT---SGEIVIDDKVVNQLEPRERG- 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 -CAMVFQN--YALYPhMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:COG1123 84 rIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
3.54e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.32 E-value: 3.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPhMNVAANMGYALKVAGvpREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494964880 161 LSNLDAKLRVqmRVE--IRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:COG4619 158 TSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
2.87e-52 |
|
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: 173.14 E-value: 2.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDI-----TSGEIVIDDKVVNQLEPRE---- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQNYALYPhMNVAANMGYALKVAGV-PREERDRRIKETARIVGL-EDFLDR-KPAELSGGQRQRVAMGRAIIRE 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 152 PKVFLFDEPLSNLD--AKLRVQMRveIRRLHKRLsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:cd03260 160 PEVLLLDEPTSALDpiSTAKIEEL--IAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
6.73e-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: 171.97 E-value: 6.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQNYALYPHMNVAANMGYALKV 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 103 AGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 494964880 183 LSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-227 |
8.88e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 172.50 E-value: 8.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDD------KVVNQLEPRE-- 74
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQNYALYPHMNVAANMGYA-LKVAGVPREE-RDRRIKETARIvGLEDFLDRKPAELSGGQRQRVAMGRAIIREP 152
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQaREKAMKLLARL-RLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 153 KVFLFDEPLSNLDAKLRVQMrVEIRRLHKRLSATSVFVTHdQVE-AMTLADKLVVMYKGNVEQVGTpLEVYNTPRT 227
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTH-EVEfARKVASQVVYMEKGRIIEQGD-ASHFTQPQT 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-193 |
1.07e-51 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 171.13 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAG-LEDI--TSGEIVIDDKVVNQLEPRERGCAMVF 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMGYALkVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 494964880 162 SNLDAKLRVQMRV----EIRRLHkrLSAtsVFVTHD 193
Cdd:COG4136 162 SKLDAALRAQFREfvfeQIRQRG--IPA--LLVTHD 193
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-193 |
2.00e-51 |
|
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: 170.51 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:TIGR02673 2 IEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 494964880 158 DEPLSNLDAKLRVQ-MRVeIRRLHKRlSATSVFVTHD 193
Cdd:TIGR02673 162 DEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHD 196
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
5.81e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 171.07 E-value: 5.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY--GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV----NQLEPRERgC 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeeNLWEIRKK-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNyalyPHmN------VAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:TIGR04520 80 GMVFQN----PD-NqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 152 PKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAmTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
1.66e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 170.32 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN-----PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN-----QLEPR 73
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ERGCAMVFQnyalYPHM-----NVAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRA 147
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-228 |
4.01e-50 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 167.64 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPrERgcAMVFQNYALYPHMNVAANMGYAL 100
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DR--MVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 101 K--VAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRR 178
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 179 LHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV-YNTPRTR 228
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-236 |
4.55e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 168.44 E-value: 4.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV-------NQLEPRER- 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 76 -------GCAMVFQNYALYPHMNVAANMGYA-LKVAGVPREE-RDRRIKETARiVGLEDFLDRKPAELSGGQRQRVAMGR 146
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEaIERAEALLAK-VGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 147 AIIREPKVFLFDEPLSNLDAKLrVQmrvEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
250
....*....|...
gi 494964880 224 TPRTRFVGSFIGS 236
Cdd:COG4598 244 NPKSERLRQFLSS 256
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-221 |
4.84e-50 |
|
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: 167.74 E-value: 4.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAAN-----MGYALKVAG----VPREERDRRIKETARiVGLEDFLDRKPAELSGGQRQRVAMGRAI 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrLGRRSTWRSlfglFPKEEKQRALAALER-VGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQ-MRVeIRRLHKRLSATSVFVTHdQVE-AMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-212 |
6.45e-50 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 166.51 E-value: 6.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVvhGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQN 83
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-228 |
1.56e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 1.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVI-----------DDKVVNQLEp 72
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIRELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 73 reRGCAMVFQNYALYPHMNVAANMGYA-LKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:PRK11124 82 --RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 152 PKVFLFDEPLSNLDAKLRVQMrVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPlEVYNTPRTR 228
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-225 |
3.01e-49 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 169.14 E-value: 3.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 8 QVRKAYGRnpvvHGVDLNFRS--GEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN------QLEPRERGCAM 79
Cdd:TIGR02142 4 RFSKRLGD----FSLDADFTLpgQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiFLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMNVAANMGYALKVAGVPreERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMKRARPS--ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-232 |
4.21e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 166.01 E-value: 4.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERgcaMVFQNYA 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 86 LYPHMNVAANMGYALKvaGVPREERDRRIKEtariVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PRK11247 92 LLPWKKVIDNVGLGLK--GQWRDAALQALAA----VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 166 AKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGnveQVGTPLEVyNTPRTRFVGS 232
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTV-DLPRPRRRGS 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
1.98e-48 |
|
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: 161.41 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV--NQLEPRERgCAMVF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMgyalkvagvpreerdrriketarivgledfldrkpaELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 162 SNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-233 |
3.18e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 167.90 E-value: 3.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 7 EQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL------EPRERGCAMV 80
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSF 233
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
4.81e-48 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 165.23 E-value: 4.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY----GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED---ITSGEIVIDDKVVNQLEPRE-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 ----RGCAMVFQN-Y-ALYPHMNVAANMGYALKV-AGVPREERDRRIKETARIVGL---EDFLDRKPAELSGGQRQRVAM 144
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 145 GRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHD--QVEAMtlADKLVVMYKGN-VEQvGTPLEV 221
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGRiVEE-GPVEEL 238
|
....*
gi 494964880 222 YNTPR 226
Cdd:COG0444 239 FENPR 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
5.63e-48 |
|
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: 159.72 E-value: 5.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 nyalyphmnvaanmgyalkvagvpreerdrriketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494964880 163 NLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
5.80e-48 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 162.95 E-value: 5.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQlEPRERGcaMVFQN 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERG--VVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494964880 164 LDAKLRVQMRVEIRRLHKRlSATSVF-VTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQE-TGKQVLlITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-212 |
7.13e-48 |
|
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: 160.29 E-value: 7.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERgcamvfqny 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 85 alyphmnvaanmgyALKVAGVPreerdrrikeTA-RIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03214 72 --------------ARKIAYVP----------QAlELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-221 |
2.00e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 171.17 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:COG2274 473 DIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYpHMNVAANMgyALKVAGVPREErdrrIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRA 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENI--TLGDPDATDEE----IIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLrvQMRVeIRRLHKRL-SATSVFVTHDqVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG2274 626 LLRNPRILILDEATSALDAET--EAII-LENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-226 |
1.32e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 161.44 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGCAMVFQN-YA-LYPHMN 91
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKVAGV-PREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:COG4608 114 VGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 170 VQMRVEIRRLHKRLSATSVFVTHD--QVEAMtlADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:COG4608 194 AQVLNLLEDLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-223 |
1.51e-46 |
|
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: 159.00 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVV-HGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:TIGR02315 2 LEVENLSKVYPNGKQAlKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAAN-----MGYALKVAGV----PREERDRRIKETARiVGLEDFLDRKPAELSGGQRQRVAMGRAI 148
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENvlhgrLGYKPTWRSLlgrfSEEDKERALSALER-VGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-236 |
8.68e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 159.97 E-value: 8.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY--GRNPV--VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE----- 74
Cdd:PRK11153 2 IELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTH--DQVEAmtLADKLVVMYKGN-VEQvGTPLEVYNTPRTRFVG 231
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRlVEQ-GTVSEVFSHPKHPLTR 238
|
....*
gi 494964880 232 SFIGS 236
Cdd:PRK11153 239 EFIQS 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-223 |
1.14e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 157.90 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVID-----DKVVNQLEPRERgCAMVFQ--NYALYPHmNVAA 94
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditDKKVKLSDIRKK-VGLVFQypEYQLFEE-TIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 95 NMGYALKVAGVPREERDRRIKETARIVGL--EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQM 172
Cdd:PRK13637 104 DIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 173 RVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK13637 184 LNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-226 |
4.66e-45 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 154.90 E-value: 4.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---GCAMV 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANM--------GYALKVAGVPREERD--RRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR 150
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 151 EPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-193 |
5.21e-45 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 154.10 E-value: 5.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 494964880 158 DEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHD 193
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-236 |
8.03e-45 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 154.60 E-value: 8.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR--------ER 75
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRngplvpadEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 76 GCA-------MVFQNYALYPHMNVAANMGYA-LKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRA 147
Cdd:TIGR03005 81 HLRqmrnkigMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRT 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 494964880 228 RFVGSFIGS 236
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-212 |
1.97e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 152.81 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVFQNYALYPHMNVAANMGYALKV 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 103 AGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKR 182
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|
gi 494964880 183 LSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
2.45e-44 |
|
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: 151.86 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG-CAMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAGVPReeRDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494964880 163 NLDAKlrvqmrvEIRRLHKRLSA------TSVFVTHDQVEA 197
Cdd:COG4133 161 ALDAA-------GVALLAELIAAhlarggAVLLTTHQPLEL 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-227 |
3.16e-44 |
|
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: 159.85 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 10 RKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDiTSGEIVIDDKVVNQLEPRE-----RGCAMVFQN- 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YA-LYPHMNVAANMGYALKV--AGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:COG4172 372 FGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 160 PLSNLDAKLRVQMrVEI-RRLHKRLSATSVFVTHDQ--VEAMtlADKLVVMYKGN-VEQvGTPLEVYNTPRT 227
Cdd:COG4172 452 PTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGKvVEQ-GPTEQVFDAPQH 519
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
3.44e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.55 E-value: 3.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRergCAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMN------VAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:COG1121 81 PQRAEVDWDFPitvrdvVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 155 FLFDEPLSNLDAKLRVQ-MRVeIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQvGTPLEVYN 223
Cdd:COG1121 161 LLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
1.07e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 151.83 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED-----ITSGEIVID-DKVVNQLEPRE 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDtARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RG----CAMVFQNYALYPHMNVAAN-MGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAII 149
Cdd:PRK11264 81 RQlrqhVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 150 REPKVFLFDEPLSNLDAKLRVQMRVEIRRL--HKRlsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP-- 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPqq 237
|
250
....*....|..
gi 494964880 226 -RTR-FVGSFIG 235
Cdd:PRK11264 238 pRTRqFLEKFLL 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
1.17e-43 |
|
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: 148.18 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVFQNYALYPHMNVAANM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 GYALKVAGVPREERDRRIKETARIVGLEDFLDRK----PAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-220 |
3.78e-43 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 149.19 E-value: 3.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG--RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK-VVNQLEPRERGCAMV 80
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSAtsVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLE 220
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
3.79e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.91 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGR--NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAM 79
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNyalyPH-----MNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:PRK13632 88 IFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAmTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-194 |
6.35e-43 |
|
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: 148.15 E-value: 6.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP-------RERgCA 78
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfrREK-LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 494964880 159 EPLSNLDAKLRvQMRVEIRRLHKRLSATSVFVTHDQ 194
Cdd:TIGR03608 160 EPTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-210 |
1.01e-42 |
|
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: 146.37 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG--RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAM 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYpHMNVAANMgyalkvagvpreerdrriketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRlsATSVFVTHDqVEAMTLADKLVVMYKG 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAKG--KTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-218 |
1.80e-42 |
|
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: 155.69 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALyPHMNVAANMGYALKVAGvpreerDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRA 147
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHDQvEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTH 555
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-194 |
2.61e-42 |
|
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: 147.58 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN--PVV--HGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL--EPRERGC 77
Cdd:COG4181 9 IELRGLTKTVGTGagELTilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdeDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AM----VFQNYALYPHMNVAANMGYALKVAGVpREERDRRIKETARiVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:COG4181 89 ARhvgfVFQSFQLLPTLTALENVMLPLELAGR-RDARARARALLER-VGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQ 194
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-220 |
7.50e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 154.17 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAM 79
Cdd:COG1132 339 EIEFENVSFSYPGDrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYpHMNVAANMGYALKvaGVPREErdrrIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAI 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGRP--DATDEE----VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 149 IREPKVFLFDEPLSNLDAK--LRVQMRveIRRLHKRlsATSVFVTH--DQVEAmtlADKLVVMYKGNVEQVGTPLE 220
Cdd:COG1132 492 LKDPPILILDEATSALDTEteALIQEA--LERLMKG--RTTIVIAHrlSTIRN---ADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-222 |
9.10e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 147.47 E-value: 9.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAE--IRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ---LEPR 73
Cdd:PRK13635 1 MKEeiIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ERgCAMVFQNyalyPH-----MNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAI 148
Cdd:PRK13635 81 RQ-VGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTlADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
1.29e-41 |
|
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: 145.21 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQlEPRE--RGCAMVF 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 162 SNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLE 220
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-228 |
2.38e-41 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 146.10 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 12 AYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGCAMVFQNY-- 84
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 85 ALYPHMNVAANMGYALK-VAGVPREERDRRIKETARIVGLE-DFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 163 NLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV--EQVGTPLEVYNTPRTR 228
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFKHPAGR 247
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
3.26e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 146.32 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNP-----VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN------QLE 71
Cdd:PRK13634 2 DITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 72 PRERGCAMVFQnyalYP-HM----NVAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMG 145
Cdd:PRK13634 82 PLRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
1.77e-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: 142.12 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNP----VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQlEPRE--RGC 77
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 158 DEPLSNLDAKLRVQMRVEIRRLhKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
3.29e-40 |
|
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: 141.42 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---GCAMV 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANmgyaLKVAGVPREERDRRiKETARIVG----LEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:cd03224 81 PEGRRIFPELTVEEN----LLLGAYARRRAKRK-ARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRRLhKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-210 |
6.67e-40 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 140.43 E-value: 6.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK-VVNQLEPRERGCAMVfQ 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsYQKNIEALRRIGALI-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAGVpreeRDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 163 NLDAKLRVQMRVEIRRLHKrlSATSVFV-THDQVEAMTLADKLVVMYKG 210
Cdd:cd03268 156 GLDPDGIKELRELILSLRD--QGITVLIsSHLLSEIQKVADRIGIINKG 202
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-210 |
7.15e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 140.56 E-value: 7.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNP----VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG--- 76
Cdd:TIGR02211 2 LKCENLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 ---CAMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDqveaMTLA---DKLVVMYKG 210
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAkklDRVLEMKDG 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-234 |
1.44e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.26 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAE--IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV----------- 67
Cdd:PRK10619 1 MSEnkLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 68 ----NQLEPRERGCAMVFQNYALYPHMNVAAN-MGYALKVAGVPREE-RDRRIKETARIVGLEDFLDRKPAELSGGQRQR 141
Cdd:PRK10619 81 vadkNQLRLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEaRERAVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 142 VAMGRAIIREPKVFLFDEPLSNLDAKLrvqmRVEIRRLHKRLS---ATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*.
gi 494964880 219 LEVYNTPRTRFVGSFI 234
Cdd:PRK10619 237 EQLFGNPQSPRLQQFL 252
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-222 |
1.01e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 139.48 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 16 NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV---NQLEPReRGCAMVFQNyalyPH--- 89
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteeNVWDIR-HKIGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 90 --MNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK 167
Cdd:PRK13650 95 vgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 168 LRVQMRVEIRRLHKRLSATSVFVTHDqVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-228 |
2.53e-38 |
|
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: 136.90 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---GCAMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 161 LSNLDAKlRVQmrvEIRRLHKRLSAT--SVFVT-HDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTR 228
Cdd:cd03218 161 FAGVDPI-AVQ---DIQKIIKILKDRgiGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-226 |
2.35e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.16 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDI-----TSGEIVID-----DKVVNQLEPR 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDgediyDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ER-GcaMVFQNYALYPhMNVAANMGYALKVAGV-PREERDRRIKETARIVGL----EDFLDRKPAELSGGQRQRVAMGRA 147
Cdd:COG1117 92 RRvG--MVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 148 IIREPKVFLFDEPLSNLD----AKlrvqmrVE--IRRLHKRLsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpistAK------IEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
....*
gi 494964880 222 YNTPR 226
Cdd:COG1117 241 FTNPK 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
2.53e-37 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 132.17 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQnyalyphmnvaanmgyalkvagvpreerdrriketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVeqVGT 217
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV--VGT 163
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
2.84e-37 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 134.83 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNyalyPHMNVAanmgyaLKVA------------GVPREErDRRIKETA-RIVGLEDFLDRKPAELSGGQRQR--VAMgr 146
Cdd:COG4604 82 QE----NHINSR------LTVRelvafgrfpyskGRLTAE-DREIIDEAiAYLDLEDLADRYLDELSGGQRQRafIAM-- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 147 AIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-228 |
2.99e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 135.20 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 9 VRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGCAMVFQN 83
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 Y--ALYPHMNVAANMGYALK-VAGVPREERDRRIKETARIVGLED-FLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:PRK10419 98 SisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV--EQVGTPLEVYNTPRTR 228
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSPAGR 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-212 |
4.97e-37 |
|
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: 133.04 E-value: 4.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRergCAMVFQNY 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 85 ALYPHMNVAAN----MG--YALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:cd03235 78 SIDRDFPISVRdvvlMGlyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHkRLSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-226 |
8.60e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 135.60 E-value: 8.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCA-----MVFQN--YALYPHMN 91
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKV--AGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKL 168
Cdd:PRK15079 117 IGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 169 RVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-207 |
8.78e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.00 E-value: 8.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAAN--MGYALKVAGVPREERDRRikETARI---VGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVF 155
Cdd:COG1129 85 HQELNLVPNLSVAENifLGREPRRGGLIDWRAMRR--RARELlarLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 156 LFDEPLSNLDAKlrvqmrvEIRRLHK---RLSA---TSVFVTHDQVEAMTLADKLVVM 207
Cdd:COG1129 163 ILDEPTASLTER-------EVERLFRiirRLKAqgvAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
1.30e-36 |
|
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: 131.63 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLE-------PRERG 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 camvfqnyaLYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:cd03269 81 ---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRRLhKRLSATSVFVTH--DQVEAMtlADKLVVMYKGNVEQVG 216
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEEL--CDRVLLLNKGRAVLYG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.47e-36 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 131.55 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVvILGPSGCGKSTLLRMIAGLEDITSGEIVIDD-KVVNQLEPRERGCAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGqDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 163 NLDaklrVQMRVEIRRLHKRLSATSVFV--TH--DQVEAMtlADKLVVMYKGNVEQVG 216
Cdd:cd03264 160 GLD----PEERIRFRNLLSELGEDRIVIlsTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
1.84e-36 |
|
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: 132.03 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---GC 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANmgyaLKVAGVPREERDRRIKETARIVG----LEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:COG0410 81 GYVPEGRRIFPSLTVEEN----LLLGAYARRDRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRlsATSVFVthdqVE-----AMTLADKLVVMYKGNVEQVGTPLEVYNTPRTR 228
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNRE--GVTILL----VEqnarfALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
3.12e-36 |
|
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: 138.36 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAY--GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGC 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYpHMNVAANmgyaLKVAgvpREE-RDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMG 145
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRLA---RPDaTDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlsATSVFVTHDQVeAMTLADKLVVMYKGNVEQVGTPLE 220
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEE 555
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-207 |
6.42e-36 |
|
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: 137.03 E-value: 6.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP--RERGCAM 79
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHmNVAANMGYALKVAGvpreerDRRIKETARIVGLEDF-----------LDRKPAELSGGQRQRVAMGRAI 148
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDAS------DAEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlsATSVFVTHDqVEAMTLADKLVVM 207
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
5.23e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.23 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLE-------PRERG 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 camvfqnyaLYPHMNVAANMGY--ALKvaGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:COG4152 82 ---------LYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 155 FLFDEPLSNLD---AKLrvqMRVEIRRLHKRlSATSVFVTH--DQVEAmtLADKLVVMYKGNV 212
Cdd:COG4152 151 LILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRK 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-210 |
1.07e-34 |
|
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: 126.94 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAY--GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYP---HMNVAANMGYAlkvagvpreeRDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAM 144
Cdd:cd03245 82 YVPQDVTLFYgtlRDNITLGAPLA----------DDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 145 GRAIIREPKVFLFDEPLSNLDaklrvqMRVEiRRLHKRLSA-----TSVFVTHDQVeAMTLADKLVVMYKG 210
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMD------MNSE-ERLKERLRQllgdkTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
1.84e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 133.00 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-----GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGE--IVIDDKVVNQLEPR--E 74
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGpdG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCA-----MVFQNYALYPHMNVAANMGYALKVAgVPREERDRRIKETARIVGLED-----FLDRKPAELSGGQRQRVAM 144
Cdd:TIGR03269 360 RGRAkryigILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 145 GRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-226 |
3.31e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.54 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP-----RERGCAMVFQN-YA-LYPHMN 91
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqklLRQKIQIVFQNpYGsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKV-AGVPREERDRRIKETARIVGLE-DFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:PRK11308 111 VGQILEEPLLInTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 170 VQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-225 |
3.42e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 129.22 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 34 ILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLE------PRERGCAMVFQNYALYPHMNVAANMGYAlkVAGVPR 107
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYG--MAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 108 EERDRRIKetarIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATS 187
Cdd:PRK11144 107 AQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPI 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 494964880 188 VFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK11144 183 LYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-226 |
4.73e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 126.28 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQN--------------YALYPHMNVAANMGyalkvagvpreERDRRIKETA-RIVGLEDFLDRKPAELSGGQRQRVAMG 145
Cdd:PRK11231 82 PQHhltpegitvrelvaYGRSPWLSLWGRLS-----------AEDNARVNQAmEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 146 RAIIREPKVFLFDEPLSNLDaklrVQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD----INHQVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
....
gi 494964880 223 nTPR 226
Cdd:PRK11231 227 -TPG 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-226 |
8.73e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 125.61 E-value: 8.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGC--AMVF 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARrrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYAL---YPHMNVAAnMGyaLKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAII-------RE 151
Cdd:COG4559 82 QHSSLafpFTVEEVVA-LG--RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 152 PKVFLFDEPLSNLDakLRVQMRVeiRRLHKRLSA--TSVF-VTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:COG4559 159 PRWLFLDEPTSALD--LAHQHAV--LRLARQLARrgGGVVaVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
9.00e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.97 E-value: 9.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGR-----NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP--RERG 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 CAMVFQNYAL--YPHMNVAANMGYALK-------VAGVPREERDRRIKETARI-VGLEDFLDRKPAELSGGQRQRVAMGR 146
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLALAYRrgkrrglRRGLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 147 AIIREPKVFLFDEPLSNLDAKlRVQMRVEI-RRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
1.99e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 124.37 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLE--------- 71
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 72 ---PRErgcAMVFQNyalyphMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAI 148
Cdd:COG1137 81 gylPQE---ASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 149 IREPKVFLFDEPLSNLDAkLRVQmrvEIRRLHKRLSAT--SVFVT-HDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP-IAVA---DIQKIIRHLKERgiGVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
...
gi 494964880 226 RTR 228
Cdd:COG1137 228 LVR 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-210 |
2.07e-33 |
|
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: 123.14 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNP-VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEpRERGCAMVFQN 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 --YALYPHmNVAANMGYALKVAGvpreERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494964880 162 SNLDAKlrvQMRvEIRRLHKRLSA--TSVFV-THDQVEAMTLADKLVVMYKG 210
Cdd:cd03226 155 SGLDYK---NME-RVGELIRELAAqgKAVIViTHDYEFLAKVCDRVLLLANG 202
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-212 |
2.58e-33 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 131.14 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:TIGR03375 463 EIEFRNVSFAYPGQetPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYpHMNVAANMgyALKVAGVpreeRDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRA 147
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNI--ALGAPYA----DDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 148 IIREPKVFLFDEPLSNLDAklRVQMRVeIRRLhKRLSA--TSVFVTHdQVEAMTLADKLVVMYKGNV 212
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDN--RSEERF-KDRL-KRWLAgkTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
3.15e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 124.18 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDIT-----SGEIVIDDKV-----VNQLEPR 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiyspdVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ERgCAMVFQNYALYPHMNVAANMGYALKVAGV--PREERDRRI----KETARIVGLEDFLDRKPAELSGGQRQRVAMGRA 147
Cdd:PRK14267 85 RE-VGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-217 |
5.27e-33 |
|
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: 123.02 E-value: 5.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---GCAMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANmgyaLKVAGVPREERDRRIKET--ARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:TIGR03410 82 QGREIFPRLTVEEN----LLTGLAALPRRSRKIPDEiyELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-212 |
6.02e-33 |
|
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: 120.78 E-value: 6.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG--RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG--CAM 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHmNVAANMgyalkvagvpreerdrriketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHdQVEAMTLADKLVVMYKGNV 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-204 |
1.33e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.85 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL------EPRERGCAMVFQNYALYPHMN 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|...
gi 494964880 172 MRVEIRRLHKRLSATSVFVTHDqveaMTLADKL 204
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-225 |
2.59e-32 |
|
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: 120.94 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED----ITSGEIVIDDKVVNQLEPRERGCAMVFQN--YALYPHMNV 92
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 93 AANMGYALKVAGVPREERDRRIKETARIVGLED---FLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 170 VQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-193 |
2.88e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 120.75 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-----RGC 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 494964880 158 DEPLSNLDAKLrvqmRVEIRRLHK---RLSATSVFVTHD 193
Cdd:PRK10908 162 DEPTGNLDDAL----SEGILRLFEefnRVGVTVLMATHD 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-222 |
6.23e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 121.35 E-value: 6.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 15 RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDD----KVVNQLEPRERgCAMVFQNyalyPHM 90
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLWDIRNK-AGMVFQN----PDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 NVAA-----NMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PRK13633 97 QIVAtiveeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 166 AKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTlADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-221 |
1.44e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 118.87 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAYGR-NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:cd03254 1 GEIEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHmNVAANMGYAlkvagvpREE-RDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGR 146
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG-------RPNaTDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 147 AIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-221 |
1.98e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.49 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVF 81
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QnyalyphmnvAANMGYALKVAGV---------PREERDRRIKETA-RIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR- 150
Cdd:PRK13548 83 Q----------HSSLSFPFTVEEVvamgraphgLSRAEDDALVAAAlAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 151 -----EPKVFLFDEPLSNLDakLRVQMRV-EI-RRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALD--LAHQHHVlRLaRQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
3.44e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.48 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL-----EDITSGEIVIDDKVVNQLEPRE- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 -RGCAMVFQNYALYPHMNVAANMGYALKVAGVPR-----EERDRRIKETARIVG-LEDFLDRKPAELSGGQRQRVAMGRA 147
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKskkelQERVRWALEKAQLWDeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-221 |
3.74e-31 |
|
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: 118.26 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIViddkvvnQLEPRERGCAMVF-- 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV-------RLFGERRGGEDVWel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 -----------QNYaLYPHMNVAaNM----GYAlkVAGVPRE--ERDR-RIKETARIVGLEDFLDRKPAELSGGQRQRVA 143
Cdd:COG1119 77 rkriglvspalQLR-FPRDETVL-DVvlsgFFD--SIGLYREptDEQReRARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 144 MGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHdQVE--------AMTLADKLVVmYKGNVEQV 215
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH-HVEeippgithVLLLKDGRVV-AAGPKEEV 230
|
250
....*....|....*.
gi 494964880 216 ----------GTPLEV 221
Cdd:COG1119 231 ltsenlseafGLPVEV 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-217 |
9.20e-31 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 116.95 E-value: 9.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG--RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAM 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYpHMNVAANMGYalkvaGVPREERDrRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAI 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY-----GRPGATRE-EVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlsATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAH-RLSTIENADRIVVLEDGKIVERGT 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
9.98e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.79 E-value: 9.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 12 AYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIddkvvnqlePRERGCAMVFQNYALYPHMN 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR---------AGGARVAYVPQRSEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 V----AANMGYALKVAGVPREER-DRRIKETA-RIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:NF040873 72 LtvrdLVAMGRWARRGLWRRLTRdDRAAVDDAlERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494964880 166 AKLRVQMRVEIRRLHKRlSATSVFVTHDqVEAMTLADKLVVM 207
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-220 |
1.85e-30 |
|
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: 116.18 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG-RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN--QLEPRERGCAMV 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYpHMNVAANMGYALKVAGvpreerDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAII 149
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRPDAT------DEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 150 REPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHDQVEAMTlADKLVVMYKGNVEQVGTPLE 220
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-223 |
2.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.77 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ--LEPRERGCAMVFQNyalyPHMN-----VAA 94
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQN----PDNQfvgsiVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 95 NMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRV 174
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 175 EIRRLHKRLSATSVFVTHDQVEAMTlADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-225 |
3.56e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL---EDITSGEIVIDDKVVNQ---LEPRERgCAMVFQNyalyPH- 89
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktvWDIREK-VGIVFQN----PDn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 90 ----MNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PRK13640 96 qfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 166 AKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAmTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-217 |
7.73e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGrnPVV--HGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCA 78
Cdd:COG3845 6 LELRGITKRFG--GVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAAN--MGY-ALKVAGVPREERDRRIKETARIVGLE-DfLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:COG3845 84 MVHQHFMLVPNLTVAENivLGLePTKGGRLDRKAARARIRELSERYGLDvD-PDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 155 FLFDEPLSNLDAKlrvqmrvEIRRLH---KRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNVeqVGT 217
Cdd:COG3845 163 LILDEPTAVLTPQ-------EADELFeilRRLAAegkSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-261 |
8.15e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.99 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNP-----VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN------QLEP 72
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 73 RERGCAMVFQnyalYPHMN-----VAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGR 146
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQlfeetVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 147 AIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNtpR 226
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ--E 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 494964880 227 TRFVGSF-IGSPAMNFLEGSFSANGeQFIFDGLPFS 261
Cdd:PRK13643 235 VDFLKAHeLGVPKATHFADQLQKTG-AVTFEKLPIT 269
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-221 |
8.59e-30 |
|
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: 120.24 E-value: 8.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQV--RKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAM 79
Cdd:COG4618 329 GRLSVENLtvVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VF--QNYALYPHmNVAAN---MGyalkvagvprEERDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVA 143
Cdd:COG4618 409 GYlpQDVELFDG-TIAENiarFG----------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 144 MGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQvEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-229 |
1.17e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.42 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKST----LLRMIAglediTSGEIVIDDKVVNQLEPRE----- 74
Cdd:PRK15134 287 IRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvr 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAMVFQ--NYALYPHMNVAANMGYALKV--AGVPREERDRRIKETARIVGLE-DFLDRKPAELSGGQRQRVAMGRAII 149
Cdd:PRK15134 362 HRIQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 150 REPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRF 229
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-221 |
1.76e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 118.99 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQV--RKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMV 80
Cdd:TIGR01842 316 HLSVENVtiVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 F--QNYALYPHmNVAANmgyalkVAGVPREERDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRA 147
Cdd:TIGR01842 396 YlpQDVELFPG-TVAEN------IARFGENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-234 |
5.09e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 113.22 E-value: 5.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 34 ILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV---------VNQLEPRERgCAMVFQNYALYPHMNVAANMGYALKVAG 104
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqIDAIKLRKE-VGMVFQQPNPFPHLSIYDNIAYPLKSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 105 VPREERDRRI-KETARIVGL----EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRL 179
Cdd:PRK14246 120 IKEKREIKKIvEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 180 HKRLsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVGSFI 234
Cdd:PRK14246 200 KNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-220 |
5.89e-29 |
|
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: 112.25 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GR--NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:cd03249 1 IEFKNVSFRYpSRpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPhMNVAANMGYALKvaGVPREErdrrIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRA 147
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKP--DATDEE----VEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 148 IIREPKVFLFDEPLSNLDAK--LRVQMRVEirRLHKrlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLE 220
Cdd:cd03249 154 LLRNPKILLLDEATSALDAEseKLVQEALD--RAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-224 |
1.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK--VVNQLEPRERGCAMVFQNY-ALYPHMNVAAN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 176 IRRLHKRLSATSVFVTHDQVEAMTlADKLVVMYKGNVEQVGTPLEVYNT 224
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
1.13e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 112.05 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDItSGEIVIDDKV-------------VNQL 70
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerrvnLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 71 EpreRGCAMVFQNYALYPhMNVAANMGYALKVAG-VPREERDRRIKETARIVGLEDFLDRK----PAELSGGQRQRVAMG 145
Cdd:PRK14258 87 R---RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADkLVVMYKGNVEQVGTPLE----- 220
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD-FTAFFKGNENRIGQLVEfgltk 241
|
250
....*....|..
gi 494964880 221 -VYNTP---RTR 228
Cdd:PRK14258 242 kIFNSPhdsRTR 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-227 |
1.42e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ-----LEPRERgCAMVFQN-----YALY 87
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkkslLEVRKT-VGIVFQNpddqlFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 88 PHMNVA---ANMGyalkvagVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:PRK13639 96 VEEDVAfgpLNLG-------LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 165 DAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRT 227
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-216 |
1.52e-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: 110.70 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPrergcamvfqN 83
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL----------G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03220 93 GGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494964880 164 LDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-212 |
1.65e-28 |
|
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: 109.95 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED--ITSGEIVIDDKVVNQLEPRERgCAMVFQNYALYPHMNVAA 94
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 95 NMGYALKVAGvpreerdrriketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRV 174
Cdd:cd03213 102 TLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 494964880 175 EIRRLHKrLSATSVFVTHD-QVEAMTLADKLVVMYKGNV 212
Cdd:cd03213 153 LLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-225 |
4.11e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 110.65 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDkvvNQLE-----PRERGCAMVFQN--YALYPHMN 91
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHfgdysYRSQRIRMIFQDpsTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKV-AGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:PRK15112 106 ISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 170 VQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-193 |
4.80e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.48 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERG------CAMVFQNYALYPHMN 91
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANmgyaLKVAGVPREERDRRIKETARI----VGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK 167
Cdd:PRK10584 105 ALEN----VELPALLRGESSRQSRNGAKAlleqLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 494964880 168 LRVQMRVEIRRLHKRLSATSVFVTHD 193
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-231 |
7.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIV---IDDKVVNQLEPRERGCAM 79
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQN-YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDqVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVG 231
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-207 |
7.58e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVF 81
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHmNVAANMGYalkvagvPREERDRRIKETARIVGLEDF------LDRKPAELSGGQRQRVAMGRAIIREPKVF 155
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIF-------PWQIRNQQPDPAIFLDDLERFalpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494964880 156 LFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEaMTLADKLVVM 207
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-297 |
8.71e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.63 E-value: 8.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAA--NMGYALKVAGV-PREERDRRIKETA-RIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQvvEMGRTPHRSRFdTWTETDRAAVERAmERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRfvGSFI 234
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR--AAFD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 235 GSPAMNFLEGSFSANGEQF-IFDGLPFSIDANIGKRHAGQPVALGIRpehaRLVPVG---TPGAVPA 297
Cdd:PRK09536 238 ARTAVGTDPATGAPTVTPLpDPDRTEAAADTRVHVVGGGQPAARAVS----RLVAAGasvSVGPVPE 300
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-225 |
1.45e-27 |
|
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: 114.28 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:TIGR03797 451 AIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYP---HMNVAANMGYALKVAgvpreerdrriKETARIVGLEDFLDRKP-----------AELSGGQRQRVAM 144
Cdd:TIGR03797 531 VVLQNGRLMSgsiFENIAGGAPLTLDEA-----------WEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLI 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 145 GRAIIREPKVFLFDEPLSNLDAklRVQMRVeIRRLhKRLSATSVFVTHDQVEAMTlADKLVVMYKGNVEQVGTPLEVYNT 224
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDN--RTQAIV-SESL-ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMAR 674
|
.
gi 494964880 225 P 225
Cdd:TIGR03797 675 E 675
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-228 |
1.65e-27 |
|
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: 113.24 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKS----TLLRMIAGLEDITSGEIVIDDKVVNQLEPRE----RG--CAMVFQN 83
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 --YALYPHMNVAANMGYALKV-AGVPREERDRRIKETARIVGL---EDFLDRKPAELSGGQRQRV--AMgrAIIREPKVF 155
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVmiAM--ALANEPDLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 156 LFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQ--VEAMtlADKLVVMYKGNVEQVGTPLEVYNTPR---TR 228
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGEIVEQGPTAELFAAPQhpyTR 254
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-222 |
1.95e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.45 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN------QLEPRERGCAMVFQnyalYPHM 90
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 N-----VAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:PRK13649 97 QlfeetVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 165 DAKLRVQMRVEIRRLHkRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK13649 177 DPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-212 |
2.03e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.95 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL--EDITSGEIV--------IDDKVVNQLEPR 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIellgrtvqREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ERGCAMVFQNYALYPHMNVAAN-----MG----YALKVAGVPREERDRRIKETARiVGLEDFLDRKPAELSGGQRQRVAM 144
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENvligaLGstpfWRTCFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 145 GRAIIREPKVFLFDEPLSNLDAKlrvQMRVEIRRLH--KRLSATSVFVTHDQVE-AMTLADKLVVMYKGNV 212
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPE---SARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-228 |
4.00e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.31 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL------EPRERgC 77
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsrlyTVRKR-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKV-AGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 157 FDEPLSNLDAklrVQMRV---EIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTR 228
Cdd:PRK11831 167 FDEPFVGQDP---ITMGVlvkLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-223 |
4.00e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.56 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDD-------KVVNQLEPRERGCAMVFQ--NYALYPHmNVA 93
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 94 ANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQM 172
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 173 RVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK13645 190 INLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-217 |
6.40e-27 |
|
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: 106.80 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNP--VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVID--DKVVNQLEPRERGCAM 79
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYpHMNVAANMgyALKVAGVPREerdrRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAI 148
Cdd:cd03252 81 VLQENVLF-NRSIRDNI--ALADPGMSME----RVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 149 IREPKVFLFDEPLSNLDAKlrvQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:cd03252 154 IHNPRILIFDEATSALDYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
1.58e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL----------EDITSGEIVIDDKVVNQLEPRE--------RGCAM 79
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQ--NYALYPHmNVAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 157 FDEPLSNLDAKLRVQMrVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK13631 200 FDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-218 |
2.55e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.15 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED--ITSGEIVIDDKVVNQLEPRER---GCAMVFQnyalYP--- 88
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQ----YPvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 89 -------HMNVAANmgyALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAE-LSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:COG0396 90 pgvsvsnFLRTALN---ARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 160 PLSNLDA-KLRVqMRVEIRRLHKRLSATsVFVTH-----DQVEamtlADKLVVMYKGNVEQVGTP 218
Cdd:COG0396 167 TDSGLDIdALRI-VAEGVNKLRSPDRGI-LIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-223 |
2.60e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.16 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 10 RKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPrergcAMVFQnyalyPH 89
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLEL-----GAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 90 MNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 170 VQMRVEIRRLHKRlSATSVFVTHD--QVEamTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:COG1134 183 KKCLARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-233 |
4.46e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.81 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP------RERGCAMVFQNYALYPHMN 91
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 172 MRVEIRRLHKRlSATSVFVTHD-QVEAMtlADKLVVMYKGNV----------EQVGTPLEVYNTPRT--RFVGSF 233
Cdd:PRK10535 183 VMAILHQLRDR-GHTVIIVTHDpQVAAQ--AERVIEIRDGEIvrnppaqekvNVAGGTEPVVNTASGwrQFVSGF 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-230 |
7.58e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.82 E-value: 7.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL---EPRERGC 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHMNVAANMGYALKV-AGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRrlHKRLSATSVFVT-HDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFV 230
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIE--HLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-212 |
7.80e-26 |
|
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: 103.70 E-value: 7.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNP---VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR--ERGCA 78
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHmNVAANMGYALkvAGVPREerdrRIKETARIVGLEDFL-----------DRKPAELSGGQRQRVAMGRA 147
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGL--QSCSFE----CVKEAAQKAHAHSFIselasgydtevGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlsaTSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-225 |
1.36e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 32 VVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVFQN---YALYPhmNVAANMGYALKVAGVP 106
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNpddQIFSP--TVEQDIAFGPINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 107 REERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSAT 186
Cdd:PRK13652 111 EETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMT 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 494964880 187 SVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK13652 191 VIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-217 |
2.20e-25 |
|
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: 107.49 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAMVFQNYALYPHmNVAA 94
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 95 NMGYAlKVAGVPREerdrRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:TIGR02203 425 NIAYG-RTEQADRA----EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494964880 164 LDAKLRVQMRVEIRRLHKrlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:TIGR02203 500 LDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGT 550
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-212 |
3.56e-25 |
|
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: 101.58 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED---ITSGEIVIDDKVVNQLEPRERgCAMVFQNYALYPHMNVAA 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 95 NMGYALKVAGvPREERDRRIKETARIVGLEDFLDRKPAE-----LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:cd03234 101 TLTYTAILRL-PRKSSDAIRKKRVEDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494964880 170 VQMRVEIRRLHKRLSAtsVFVTHDQ--VEAMTLADKLVVMYKGNV 212
Cdd:cd03234 180 LNLVSTLSQLARRNRI--VILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-263 |
4.35e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.99 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNF--RSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN------QLEPRERGCAMVFQnyalYPHMN--- 91
Cdd:PRK13641 25 NISFelEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAQlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 --VAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKL 168
Cdd:PRK13641 101 ntVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 169 RVQMrVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTrFVGSFIGSPAMNFLEGSFSA 248
Cdd:PRK13641 181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEW-LKKHYLDEPATSRFASKLEK 258
|
250
....*....|....*
gi 494964880 249 NGeqFIFDGLPFSID 263
Cdd:PRK13641 259 GG--FKFSEMPLTID 271
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
9.35e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.58 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER---GCA 78
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNyaLYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:PRK13537 86 PQFDN--LDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-225 |
2.14e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 13 YGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDI-----TSGEIVIDDKvvNQLEPR------ERGCAMVF 81
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGH--NIYSPRtdtvdlRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPhMNVAANMGYALKVAGVPREER-----DRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVldeavEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 157 FDEPLSNLDAKlrVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK14239 172 LDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-221 |
3.00e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.06 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAM 79
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYAL--------------YPHMNVAANMgyalkvagvpREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMG 145
Cdd:PRK10253 86 LAQNATTpgditvqelvargrYPHQPLFTRW----------RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-167 |
9.57e-24 |
|
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: 97.04 E-value: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP-RERGCAMVFQNYALYPHMNV 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 93 AANMGYALKVAGvpreERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK 167
Cdd:TIGR01189 91 LENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-207 |
9.75e-24 |
|
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: 97.89 E-value: 9.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK--VVN--QLEPRErgcaMVfqnyALYPHMnv 92
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggWVDlaQASPRE----IL----ALRRRT-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 93 aanMGY------------ALKV-------AGVPREERDRRIKETARIVGLEDFL-DRKPAELSGGQRQRVAMGRAIIREP 152
Cdd:COG4778 95 ---IGYvsqflrviprvsALDVvaeplleRGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 153 KVFLFDEPLSNLDAKLRVQMRVEIRRLhKRLSATSVFVTHDQvEAM-TLADKLVVM 207
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDE-EVReAVADRVVDV 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-222 |
1.01e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 13 YGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ-----LEPRERgCAMVFQNyaly 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrglLALRQQ-VATVFQD---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 88 P-----HMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:PRK13638 86 PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 163 NLDAKLRVQMRVEIRRLHKRLSATsVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-222 |
1.09e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.29 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEI-VIDDKVVNQLEPRERGCAMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 163 NLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNV-----------EQVGTP-LEVY 222
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKiaegrphalidEHIGCQvIEIY 272
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-193 |
1.23e-23 |
|
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: 102.05 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-RGCAMVF 81
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 qnyALYPHMnVAANMGYALKVA--GVPREErdrrIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAI 148
Cdd:TIGR02868 415 ---AQDAHL-FDTTVRENLRLArpDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMrveirrLHKRLSATS----VFVTHD 193
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADEL------LEDLLAALSgrtvVLITHH 529
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-226 |
1.32e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMVFQNYALYPHMNVAAN 95
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYA-------------LKVAGVPREERD--RRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:PRK11300 101 LLVAqhqqlktglfsglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 161 LSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
2.12e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.88 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE-RG-CAMVFQN-----YALYPHMNVA 93
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQDpddqvFSSTVWDDVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 94 ---ANMGYAlkvagvpREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRV 170
Cdd:PRK13647 103 fgpVNMGLD-------KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494964880 171 QMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
2.17e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ------LEPRERGCAMVFQnyalYPHM-- 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 ---NVAANMGYALKVAGVPREErdrrIKETARIVGLE-----DFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:PRK13646 99 fedTVEREIIFGPKNFKMNLDE----VKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 163 NLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-192 |
2.65e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIE--QVRKAYGRnPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIddkvvnqlePRERGCAM 79
Cdd:COG4178 361 GALALEdlTLRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQN-Y--------AL-YPHMnvaanmgyalkvagvPREERDRRIKETARIVGLEDFLDRKPAE------LSGGQRQRVA 143
Cdd:COG4178 431 LPQRpYlplgtlreALlYPAT---------------AEAFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLA 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494964880 144 MGRAIIREPKVFLFDEPLSNLDAKLRVQMrveIRRLHKRL-SATSVFVTH 192
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
2.83e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV----VNQleprergcam 79
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVkigyFDQ---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 vfQNYALYPHMNVAANMgyalkvagvpREERDRRIKETARIVgLEDFL---DR--KPAE-LSGGQRQRVAMGRAIIREPK 153
Cdd:COG0488 386 --HQEELDPDKTVLDEL----------RDGAPGGTEQEVRGY-LGRFLfsgDDafKPVGvLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 154 VFLFDEPLSNLDaklrVQMRvEIrrLHKRLSA---TSVFVTHDQ--VEamTLADKLVVMYKGNVE 213
Cdd:COG0488 453 VLLLDEPTNHLD----IETL-EA--LEEALDDfpgTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
4.75e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVI---DDKVVNQLEPRE-------------------- 74
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEkvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 ---RGCAMVFQ--NYALYpHMNVAANMGYALKVAGVPREERDRRIKETARIVGL-EDFLDRKPAELSGGQRQRVAMGRAI 148
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-206 |
5.99e-23 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 96.32 E-value: 5.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 25 NFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN----QLEPRERGCAMVFqnyaLYPHMNVAANMGYAl 100
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRDL----LSSITKDFYTHPYF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 101 kvagvpreerdrrIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLH 180
Cdd:cd03237 96 -------------KTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*.
gi 494964880 181 KRLSATSVFVTHDQVEAMTLADKLVV 206
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-226 |
8.91e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 8.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPV-----------VHGVD---LNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIV-----IDDKV 66
Cdd:PRK10261 313 ILQVRNLVTRFPLrsgllnrvtreVHAVEkvsFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 67 VNQLEPRERGCAMVFQN-YA-LYPHMNVAANMGYALKVAGV-PREERDRRIKETARIVGLE-DFLDRKPAELSGGQRQRV 142
Cdd:PRK10261 393 PGKLQALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 143 AMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
....
gi 494964880 223 NTPR 226
Cdd:PRK10261 553 ENPQ 556
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-217 |
1.12e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 99.43 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR--ERGCAM 79
Cdd:TIGR01846 456 ITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHmNVAANMgyALKVAGVPREerdrRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAI 148
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNI--ALCNPGAPFE----HVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 149 IREPKVFLFDEPLSNLDAKlrvQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYE---SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGR 674
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-225 |
1.64e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.03 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 16 NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR--ERGCAMVFQNYALYPHmNVA 93
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 94 ANMGYALKVAgvPREErdrrIKETARIVGLEDFL-----------DRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:TIGR00958 573 ENIAYGLTDT--PDEE----IMAAAKAANAHDFImefpngydtevGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 163 NLDAklrvQMRVEIRRLHKRLSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:TIGR00958 647 ALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-217 |
1.66e-22 |
|
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: 98.74 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCA 78
Cdd:COG5265 356 GEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYphmN--VAANMGYALkvAGVPREErdrrIKETARIVGLEDFLDRKPA-----------ELSGGQRQRVAMG 145
Cdd:COG5265 436 IVPQDTVLF---NdtIAYNIAYGR--PDASEEE----VEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHK---------RLSAtsvfVTHdqveamtlADKLVVMYKGN-VEQv 215
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARgrttlviahRLST----IVD--------ADEILVLEAGRiVER- 573
|
..
gi 494964880 216 GT 217
Cdd:COG5265 574 GT 575
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-210 |
1.72e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 94.71 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 9 VRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIViddkvVNQLEPRERG------CAMVF- 81
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPWKRRkkflrrIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAAnmGYAL--KVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:cd03267 102 QKTQLWWDLPVID--SFYLlaAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
1.74e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV----VNQlEPRERGCAMVF 81
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QN--------YALYPHMNvAANMGYALKVAGVPREER-------------DRRIKETARIVGL-EDFLDRKPAELSGGQR 139
Cdd:COG0488 80 DTvldgdaelRALEAELE-ELEAKLAEPDEDLERLAElqeefealggweaEARAEEILSGLGFpEEDLDRPVSELSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 140 QRVAMGRAIIREPKVFLFDEPLSNLDAklrvqmrvE-IRRLHKRLSA---TSVFVTHD 193
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDL--------EsIEWLEEFLKNypgTVLVVSHD 208
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-226 |
1.96e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.77 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRnPVVHGVDLNFRSGEFVVILGPSGCGKS----TLLRMI-AGLEDiTSGEIVIDDKVVNQLEPRERGCA 78
Cdd:PRK10418 5 IELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQN--YALYPHMNVAANMGYALKVAGVPReeRDRRIKETARIVGLED---FLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:PRK10418 83 TIMQNprSAFNPLHTMHTHARETCLALGKPA--DDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 154 VFLFDEPLSNLDakLRVQMRV--EIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK10418 161 FIIADEPTTDLD--VVAQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-223 |
2.22e-22 |
|
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: 94.15 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 29 GEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKvvnQLEPRERGCAMVFQNYAL---YPhMNVAANM--GYALKVA 103
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVmsGRTGHIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 104 GVPREERD--RRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMrVEIRRLHK 181
Cdd:TIGR03771 82 WLRRPCVAdfAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFIELA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494964880 182 RLSATSVFVTHDQVEAMTLADKlVVMYKGNVEQVGTPLEVYN 223
Cdd:TIGR03771 161 GAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQD 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-223 |
3.37e-22 |
|
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: 97.57 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDI--TSGEIVID------------------ 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 64 --DKVVNQLEPRE---------------RGCAMVFQ-NYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLED 125
Cdd:TIGR03269 81 pcPVCGGTLEPEEvdfwnlsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 126 FLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLV 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 494964880 206 VMYKGNVEQVGTPLEVYN 223
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
9.23e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR---ERGCAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANM--GYAL--KVAGVP----REERdRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREP 152
Cdd:PRK09700 86 YQELSVIDELTVLENLyiGRHLtkKVCGVNiidwREMR-VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 153 KVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATsVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAI-VYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-222 |
1.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ-----LEPRErGCAMVFQ--NYALYPhMNVA 93
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkglMKLRE-SVGMVFQdpDNQLFS-ASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 94 ANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMR 173
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 174 VEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-166 |
1.26e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.47 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 15 RNPVVHGVDLNFR--SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERgCAMVFQNYALYPHMNV 92
Cdd:PRK13539 12 RGGRVLFSGLSFTlaAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 93 AANMGYALKVAGvpreERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDA 166
Cdd:PRK13539 91 AENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-210 |
1.44e-21 |
|
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: 90.57 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERgcamvfqnyalyphmnVAANMG 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA----------------IRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 98 YalkvagVPrEERDRRiketarivGLedFLDRKPAE-------LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDaklrV 170
Cdd:cd03215 79 Y------VP-EDRKRE--------GL--VLDLSVAEnialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----V 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494964880 171 QMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:cd03215 138 GAKAEIYRLIRELADagkAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-210 |
1.64e-21 |
|
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: 90.99 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 15 RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV--VNQlEP-------RErgcamvfqnya 85
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVSQ-EPwiqngtiRE----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 86 lyphmNVaanmgyalkVAGVPREERdrRIKETARIVGLEDFLDRKPA-------E----LSGGQRQRVAMGRAIIREPKV 154
Cdd:cd03250 85 -----NI---------LFGKPFDEE--RYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 155 FLFDEPLSNLDAKLRVQMrveIRRL---HKRLSATSVFVTHdQVEAMTLADKLVVMYKG 210
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHI---FENCilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-203 |
1.89e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDI-----TSGEIVIDDKVVN--QLEPRE- 74
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYapDVDPVEv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 -RGCAMVFQNYALYPHmNVAANMGYALKVAGVP---REERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR 150
Cdd:PRK14243 90 rRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 151 EPKVFLFDEPLSNLD--AKLRVQMRveIRRLHKRLsaTSVFVTHDQVEAMTLADK 203
Cdd:PRK14243 169 QPEVILMDEPCSALDpiSTLRIEEL--MHELKEQY--TIIIVTHNMQQAARVSDM 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
2.99e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP----RErG 76
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimRE-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 CAMVFQNYALYPHMNVAANMgyALKVAGVPREERDRRIKetaRIVGLEDFLDRKPAE----LSGGQRQRVAMGRAIIREP 152
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENL--AMGGFFAERDQFQERIK---WVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 153 KVFLFDEPLSNLDAKLRVQMRVEIRRLhkRLSATSVF-VTHDQVEAMTLADKLVVMYKGNV--EQVGTPLEVYNTPRTRF 229
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQL--REQGMTIFlVEQNANQALKLADRGYVLENGHVvlEDTGDALLANEAVRSAY 234
|
..
gi 494964880 230 VG 231
Cdd:PRK11614 235 LG 236
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-226 |
3.28e-21 |
|
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: 91.43 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL------EPRERGC 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlsEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 A-----MVFQNYALYPHMNVAA--NMGYALKVAGVpreERDRRIKETA----RIVGLE-DFLDRKPAELSGGQRQRVAMG 145
Cdd:TIGR02323 84 MrtewgFVHQNPRDGLRMRVSAgaNIGERLMAIGA---RHYGNIRATAqdwlEEVEIDpTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
.
gi 494964880 226 R 226
Cdd:TIGR02323 241 Q 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-226 |
3.46e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 92.88 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 29 GEFVVILGPSGCGKSTLLRMIAGLED----ITSGEIVIDDKVVNQLEPRER------GCAMVFQN--YALYPHMNVAANM 96
Cdd:PRK11022 33 GEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 GYALKV-AGVPREERDRRIKETARIVGLED---FLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQM 172
Cdd:PRK11022 113 MEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494964880 173 RVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK11022 193 IELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-225 |
4.82e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKS----TLLRMI--AGLEdITSGEI--------VIDDKVVNQLEPRE-RGC- 77
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMllrrrsrqVIELSEQSAAQMRHvRGAd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 -AMVFQN--YALYPHMNVAANMGYALKV-AGVPREE---RDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR 150
Cdd:PRK10261 106 mAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEamvEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 151 EPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-212 |
5.13e-21 |
|
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: 89.51 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED--ITSGEIVIDDKVVNQLEPRER---GCA 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQnyalYPhmnvaanmgyalkvagvpreerdrriketARIVG--LEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:cd03217 81 LAFQ----YP-----------------------------PEIPGvkNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 157 FDEPLSNLDAK-LRVQMRVeIRRLHKRLSATSVfVTH-----DQVEamtlADKLVVMYKGNV 212
Cdd:cd03217 128 LDEPDSGLDIDaLRLVAEV-INKLREEGKSVLI-ITHyqrllDYIK----PDRVHVLYDGRI 183
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-226 |
5.36e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.14 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVID--DKVVNQL----EPRERGCA 78
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrDGQLRDLyalsEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 -----MVFQNYALYPHMNVAA--NMGYALKVAGvpreERD-RRIKETA-----RIVGLEDFLDRKPAELSGGQRQRVAMG 145
Cdd:PRK11701 88 rtewgFVHQHPRDGLRMQVSAggNIGERLMAVG----ARHyGDIRATAgdwleRVEIDAARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 146 RAIIREPKVFLFDEPLSNLDakLRVQMRV--EIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYN 223
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLD--VSVQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLD 241
|
...
gi 494964880 224 TPR 226
Cdd:PRK11701 242 DPQ 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-194 |
7.66e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.50 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVvnqleprergcamvfqn 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 yalyphmnvaaNMGYalkvagvpreerdrriketarivgledFldrkpAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:cd03221 64 -----------KIGY---------------------------F-----EQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|.
gi 494964880 164 LDAKLRVQMRVEIrrlhKRLSATSVFVTHDQ 194
Cdd:cd03221 101 LDLESIEALEEAL----KEYPGTVILVSHDR 127
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-225 |
1.03e-20 |
|
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: 93.85 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGR--NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLePRER---GC 77
Cdd:TIGR03796 477 YVELRNITFGYSPlePPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSV 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYpHMNVAANMgyALKVAGVPREE-----RDRRIKE--TARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR 150
Cdd:TIGR03796 556 AMVDQDIFLF-EGTVRDNL--TLWDPTIPDADlvracKDAAIHDviTSRPGGYDAELAEGGANLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 151 EPKVFLFDEPLSNLDAKLRVQMRVEIRRlhkRlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDDNLRR---R-GCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
1.12e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEP---RERGCAMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYPHMNVAANMGYalkvaGVPREERD-RRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILF-----GLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 160 PLSNLDAklrvqmrVEIRRLHKRLSATS------VFVTHDQVEAMTLADKLVVMYKGNVEQVGtPLEVYNT 224
Cdd:PRK15439 167 PTASLTP-------AETERLFSRIRELLaqgvgiVFISHKLPEIRQLADRISVMRDGTIALSG-KTADLST 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-235 |
1.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.54 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSG-----EIVIDDKVV----NQLEPRERgCAMVFQNYALYP 88
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrDVLEFRRR-VGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 89 hMNVAANMGYALKVAG-VPREE----RDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEfrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLsaTSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR----TRFVGSFIG 235
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKhaetARYVAGLSG 267
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-210 |
4.02e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMVFQN---YALY 87
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 88 PHMNVAANMGYA----LKVAGV--PREERDR--------RIKeTARIvgledflDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:COG1129 343 LDLSIRENITLAsldrLSRGGLldRRRERALaeeyikrlRIK-TPSP-------EQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 154 VFLFDEPLSNLD--AKlrvqmrVEIRRLHKRLSA--TSV-FVTHDQVEAMTLADKLVVMYKG 210
Cdd:COG1129 415 VLILDEPTRGIDvgAK------AEIYRLIRELAAegKAViVISSELPELLGLSDRILVMREG 470
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-218 |
8.76e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 20 HGVDLNFRSGEFVVILGPSGCGKSTLLRMIA-----GLEdiTSGEIVIDDKVVNQLEPRERgCAMVFQNYALYPHMNVAA 94
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVK--GSGSVLLNGMPIDAKEMRAI-SAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 95 NMGYALKV---AGVPREERDRRIKETARIVGLEDFLDRK---PAE---LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 166 AKlrvqMRVEIRRLHKRL--SATSVFVTHDQ--VEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:TIGR00955 199 SF----MAYSVVQVLKGLaqKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSP 251
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
1.99e-19 |
|
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: 84.67 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEpRERGCAMVF 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYAlyPHMnvaanmgyalkVAGVPREERDRRiketarivgledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:cd03247 80 LNQR--PYL-----------FDTTLRNNLGRR--------------------FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 162 SNLDAKLRVQ-MRVEIRRLHKRlsaTSVFVTHdQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:cd03247 127 VGLDPITERQlLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-220 |
3.11e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.92 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAY-GRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN--QLEPRERGCA 78
Cdd:PRK11176 341 DIEFRNVTFTYpGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYpHMNVAANMGYAlkvagvpREERDRR--IKETAR-------IVGLEDFLDRKPAE----LSGGQRQRVAMG 145
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYA-------RTEQYSReqIEEAARmayamdfINKMDNGLDTVIGEngvlLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 146 RAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLE 220
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
6.95e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIViddkvVNQLEP-RERgcamvfQNYAlyphMNVAANMG 97
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPfKRR------KEFA----RRIGVVFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 98 --------------YAL--KVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQR--VAMgrAIIREPKVFLFDE 159
Cdd:COG4586 103 qrsqlwwdlpaidsFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 160 PLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHD--QVEAmtLADKLVVMYKGNV 212
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-229 |
1.06e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.15 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 8 QVRKAYGRnPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK-VVNQLEPRERGCAMVFQNYAL 86
Cdd:TIGR01257 936 KIFEPSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 87 YPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDA 166
Cdd:TIGR01257 1015 FHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 167 KLRVQMRVEIrrLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRF 229
Cdd:TIGR01257 1095 YSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGF 1155
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-218 |
1.11e-18 |
|
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: 83.70 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKST----LLRMIagleDITSGEIVIDDKVVNQLEPRE-R 75
Cdd:cd03244 2 DIEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 76 GC-AMVFQNYALYPHmNVAANMGyalkvagvPREER-DRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRV 142
Cdd:cd03244 78 SRiSIIPQDPVLFSG-TIRSNLD--------PFGEYsDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 143 AMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRrlHKRLSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-167 |
1.87e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 20 HGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPrERGCAMVF---QNyALYPHMNVAANM 96
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYlghQP-GIKTELTALENL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 97 GYALKVAGVPREERDRRIKETariVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK 167
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQ---VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-217 |
3.94e-18 |
|
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: 85.95 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEpreRGCAMVF 81
Cdd:TIGR01193 473 DIVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNY-ALYPHMNVAANMGYALKVA--GVPREErdrrIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRA 147
Cdd:TIGR01193 550 INYlPQEPYIFSGSILENLLLGAkeNVSQDE----IWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMrveIRRLHKRLSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-217 |
4.02e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.53 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 15 RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL---EPRERgCAMVFQNYALYPHmN 91
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSWRSR-LAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMgyALKVAGVPREErdrrIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:PRK10789 405 VANNI--ALGRPDATQQE----IEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 161 LSNLDAKLRVQMRVEIRRL-HKRlsatSVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWgEGR----TVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-225 |
8.97e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR--ERGCAMVFQNYALYPHMNV--- 92
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVrel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 93 AANMGY----ALKVAGVprEERdRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKL 168
Cdd:PRK10575 106 VAIGRYpwhgALGRFGA--ADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 169 RVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-225 |
9.40e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNF--RSGEFVVILGPSGCGKSTLLRMIAGL---EDITSG-------EIV-IDDKVVNQLepRERGCAMVFQN--YALY 87
Cdd:PRK09473 34 DLNFslRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGsatfngrEILnLPEKELNKL--RAEQISMIFQDpmTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 88 PHMNVAANMGYALKV-AGVPREERdrrIKETARIvgledfLD-------RK-----PAELSGGQRQRVAMGRAIIREPKV 154
Cdd:PRK09473 112 PYMRVGEQLMEVLMLhKGMSKAEA---FEESVRM------LDavkmpeaRKrmkmyPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-236 |
1.01e-17 |
|
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: 84.49 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 11 KAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL--EDITSGEIVIDD---KVVNQLEPRERGCAMVFQNYA 85
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGsplKASNIRDTERAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 86 LYPHMNVAAN--MGYALKVAG--VPREERDRRIKETARIVGLEDFLDRKP-AELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:TIGR02633 89 LVPELSVAENifLGNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 161 LSNLDAKlRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGnvEQVGT-PLEVYNTPR--TRFVGSFIGS 236
Cdd:TIGR02633 169 SSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVATkDMSTMSEDDiiTMMVGREITS 244
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-221 |
1.23e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 26 FRSGEFVVILGPSGCGKSTLLRMIAGLEDiTSGEIVIDDKVVNQLEPRE----RGC---------AM-VFQNYALYPHmn 91
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhRAYlsqqqsppfAMpVFQYLALHQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 vaanmgyalkvAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR-------EPKVFLFDEPLSNL 164
Cdd:COG4138 96 -----------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 165 DaklrVQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:COG4138 165 D----VAQQAALDRLLRELCQqgiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-214 |
1.59e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 2 AEIRIEQVRKAY--GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL-EPRERGC- 77
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAALRQAi 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHmNVAANMGYALKVAGvpreerDRRIKETARIVGLEDFLDRKPA----------ELSGGQRQRVAMGRA 147
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPNAS------DEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRL--HKrlsaTSVFVTHdQVEAMTLADKLVVMYKGN-VEQ 214
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNK----TVLMITH-RLTGLEQFDRICVMDNGQiIEQ 554
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-192 |
2.61e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.35 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 16 NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIddkvvnqlePRERGCAMVFQNyalyPHMnvaan 95
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 mgyalkVAGVPREerdrriketARIVGLEDfldrkpaELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDaklrVQMRVE 175
Cdd:cd03223 76 ------PLGTLRE---------QLIYPWDD-------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDR 129
|
170
....*....|....*..
gi 494964880 176 IRRLHKRLSATSVFVTH 192
Cdd:cd03223 130 LYQLLKELGITVISVGH 146
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-165 |
2.84e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.51 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 12 AYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEpRERGCAMVFQNYALYPH 89
Cdd:PRK13543 18 AFSRNeePVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 90 MNVAANMGYALKVAGvpreERDRRIKETA-RIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PRK13543 97 LSTLENLHFLCGLHG----RRAKQMPGSAlAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-173 |
4.71e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR-ERGCAMVFQNYALYPHMNVAANM 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 GYALKVAGvpreerDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD----AKLRVQM 172
Cdd:cd03231 95 RFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAM 168
|
.
gi 494964880 173 R 173
Cdd:cd03231 169 A 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-217 |
4.93e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 24 LNF--RSGEFVVILGPSGCGKSTLLRMIAGLEDITsGEIVIDDKVVNQLEPRE--RGCAMVFQNYALyPHMNVAANMGYA 99
Cdd:PRK11174 369 LNFtlPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 100 LKVAGvpreerDRRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAkl 168
Cdd:PRK11174 447 NPDAS------DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA-- 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494964880 169 RVQMRVeIRRLHK-RLSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:PRK11174 519 HSEQLV-MQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-165 |
6.76e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.30 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLE--DITSGEIVIDDKVVNQLEPRER---GCAMV 80
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQnyalyphmnvaanmgYALKVAGVPREE------RDRR----------------IKETARIVGLED-FLDRKPAE-LSG 136
Cdd:CHL00131 90 FQ---------------YPIEIPGVSNADflrlayNSKRkfqglpeldplefleiINEKLKLVGMDPsFLSRNVNEgFSG 154
|
170 180
....*....|....*....|....*....
gi 494964880 137 GQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-221 |
1.04e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIV-----IDDKVVnqlepRERGC- 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARH-----RRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 --AMVFQ----NyaLYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:NF033858 77 riAYMPQglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 152 PKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFV-THDQVEAMTLaDKLVVMYKGNVEQVGTPLEV 221
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-210 |
1.21e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 9 VRKAYGRnPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRERGCAMVF------Q 82
Cdd:COG3845 265 VRDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 83 NYALYPHMNVAANMgyALKVAGVPREER-----DRRIKE-TARIVglEDF------LDRKPAELSGGQRQRVAMGRAIIR 150
Cdd:COG3845 344 GRGLVPDMSVAENL--ILGRYRRPPFSRggfldRKAIRAfAEELI--EEFdvrtpgPDTPARSLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 151 EPKVFLFDEPLSNLDAKlrvqmrvEIRRLHKRL------SATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:COG3845 420 DPKLLIAAQPTRGLDVG-------AIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-235 |
2.73e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV---NQLEPRERGCAMVFQNYALYPHMNVAAN-- 95
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELHLVPEMTVAENly 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYALKVAGVPREerdRRIKETARI----VGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK-LRV 170
Cdd:PRK11288 102 LGQLPHKGGIVNR---RLLNYEAREqlehLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQ 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 171 QMRVeIRRLHKRLSATsVFVTHDQVEAMTLADKLVVMYKGnvEQVGTPLEVYNTPRTRFVGSFIG 235
Cdd:PRK11288 179 LFRV-IRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDG--RYVATFDDMAQVDRDQLVQAMVG 239
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-225 |
2.99e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.59 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIddkvvnqleprERGCAMVFQNYALyphMN--VAAN 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQAWI---MNatVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYAlkvagvpREERDRRIKETARIV-----------GLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:PTZ00243 741 ILFF-------DEEDAARLADAVRVSqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 165 DAKL--RVQMRVEIRRLHKRlsaTSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PTZ00243 814 DAHVgeRVVEECFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-226 |
4.21e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 26 FRSGEFVVILGPSGCGKSTLLRMIAGLEDiTSGEIVIDDKVVNQLEPRE----RG---------CAM-VFQNYALYPHmn 91
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLHQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 vaanmgyalkvAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIR-------EPKVFLFDEPLSNL 164
Cdd:PRK03695 96 -----------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 165 DaklrVQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPR 226
Cdd:PRK03695 165 D----VAQQAALDRLLSELCQqgiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-218 |
4.25e-16 |
|
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: 76.30 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ--LEPRERGCA 78
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYphmnvaanMGYALKVAGVPREERDRRIKETARIVGLEDfldrkpaELSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:cd03369 86 IIPQDPTLF--------SGTIRSNLDPFDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 159 EPLSNLDaklrVQMRVEIRR-LHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:cd03369 151 EATASID----YATDALIQKtIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-206 |
4.69e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 27 RSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVvnQLEPrergcamvfQNYALYPHMNVAANMgyalkvAGVP 106
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI--SYKP---------QYIKPDYDGTVEDLL------RSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 107 REERDRRIK-ETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSA 185
Cdd:PRK13409 426 DDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREA 505
|
170 180
....*....|....*....|.
gi 494964880 186 TSVFVTHDQVEAMTLADKLVV 206
Cdd:PRK13409 506 TALVVDHDIYMIDYISDRLMV 526
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-213 |
7.23e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYG------RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLE--DITSGEIVIDDkvvnqlEPRERG 76
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD------NQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 CAMVfqnYALYPHMNVAAnmgyALKVAGvpreerdrriketarIVGLED--FLDRKPAELSGGQRQRVAMGRAIIREPKV 154
Cdd:COG2401 100 ASLI---DAIGRKGDFKD----AVELLN---------------AVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 155 FLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVM--YKGNVE 213
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPE 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-193 |
1.28e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.07 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAG---LEDitsGEIVID-DKVVNQLE---PR 73
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEqDLIVARLQqdpPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 -ERGCamVFqNYalyphmnVA---ANMGYALK--------VAGVPREER-------------------DRRIKETARIVG 122
Cdd:PRK11147 78 nVEGT--VY-DF-------VAegiEEQAEYLKryhdishlVETDPSEKNlnelaklqeqldhhnlwqlENRINEVLAQLG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 123 LEDflDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDaklrvqmrVE-IRRLHKRL---SATSVFVTHD 193
Cdd:PRK11147 148 LDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--------IEtIEWLEGFLktfQGSIIFISHD 212
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-225 |
1.37e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.87 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED----ITSGEIVIDDKVVNQLEPRER------GCAMVFQN 83
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYphMNVAANMGYALKVAgVPREE-----------RDRRIKETARIVGL---EDFLDRKPAELSGGQRQRVAMGRAII 149
Cdd:COG4170 98 PSSC--LDPSAKIGDQLIEA-IPSWTfkgkwwqrfkwRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 150 REPKVFLFDEPLSNLDAKLRVQmrveIRRLHKRL---SATSV-FVTHDqVEAMT-LADKLVVMYKGNVEQVGTPLEVYNT 224
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQ----IFRLLARLnqlQGTSIlLISHD-LESISqWADTITVLYCGQTVESGPTEQILKS 249
|
.
gi 494964880 225 P 225
Cdd:COG4170 250 P 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-210 |
1.45e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.61 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 27 RSGEFVVILGPSGCGKSTLLRMIAGLED----ITSGEIVIDDKVVNQLEPRERG----CAmvfQNYALYPHMNVAANMGY 98
Cdd:TIGR00956 85 KPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGdvvyNA---ETDVHFPHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 99 A-------LKVAGVPREERDRRIKE-TARIVGLEDFLDRKPAE-----LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:TIGR00956 162 AarcktpqNRPDGVSREEYAKHIADvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494964880 166 AKLRVQMrVEIRRLHKRLSATSVFVTHDQV--EAMTLADKLVVMYKG 210
Cdd:TIGR00956 242 SATALEF-IRALKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEG 287
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-206 |
1.63e-15 |
|
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: 77.90 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 27 RSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVvnQLEPRErgcamVFQNYalypHMNVAANMGYALK--VAG 104
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI--SYKPQY-----ISPDY----DGTVEEFLRSANTddFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 105 VPREErdrrikETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLS 184
Cdd:COG1245 433 SYYKT------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRG 506
|
170 180
....*....|....*....|..
gi 494964880 185 ATSVFVTHDQVEAMTLADKLVV 206
Cdd:COG1245 507 KTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-208 |
2.13e-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: 75.10 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 13 YGRNP-VVHGVDLNfRSGEFVVILGPSGCGKSTLLRMIAG--------LEDITSGEIVID-------DKVVNQLEPRERG 76
Cdd:cd03236 10 YGPNSfKLHRLPVP-REGQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDefrgselQNYFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 CAMVFQNYALYPHMnVAANMGYALKVAgvprEERDRrIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:cd03236 89 VIVKPQYVDLIPKA-VKGKVGELLKKK----DERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494964880 157 FDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVfVTHDQVEAMTLADKLVVMY 208
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCLY 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-217 |
2.34e-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: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYG--RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVnqleprERGCAMVF 81
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------LTNISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMG--------YAlKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLtgrehlylYA-RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATsVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV-VLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-165 |
2.45e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV--NQLEPRERGCAMVfQNYALYPHMNVAANM 96
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRVGYMS-QAFSLYGELTVRQNL 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 97 GYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-217 |
5.28e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGR-NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR--ERGCAMV 80
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYAlyphmnVAANMGYALKVAGVP-REERDRRIKETARIV--------GLEDFLDRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:PRK10790 421 QQDPV------VLADTFLANVTLGRDiSEEQVWQALETVQLAelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 152 PKVFLFDEPLSNLDA--KLRVQMRVEIRRLHkrlsATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:PRK10790 495 PQILILDEATANIDSgtEQAIQQALAAVREH----TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-208 |
8.49e-15 |
|
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: 75.59 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 27 RSGEFVVILGPSGCGKSTLLRmiagledITSGEIV----IDDKVVNQLEPRERgcamvFQNYALYPHM-NVAANmgyALK 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-------ILSGELKpnlgDYDEEPSWDEVLKR-----FRGTELQDYFkKLANG---EIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 102 VA--------------GVPRE------ERDRrIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:COG1245 162 VAhkpqyvdlipkvfkGTVREllekvdERGK-LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494964880 162 SNLDAKLRVQMRVEIRRLHKRLSATSVfVTHDQveAM--TLADKLVVMY 208
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLV-VEHDL--AIldYLADYVHILY 286
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-192 |
1.10e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYG-RNPVVHGVDLNF--RSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDD----KVVNQLEPR 73
Cdd:PTZ00265 380 IKKIQFKNVRFHYDtRKDVEIYKDLNFtlTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ER-GCA----MVFQN-------YALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVG------------------- 122
Cdd:PTZ00265 460 SKiGVVsqdpLLFSNsiknnikYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGdlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 123 ------------------LEDFLDRKP-----------AELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMR 173
Cdd:PTZ00265 540 nyqtikdsevvdvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250
....*....|....*....
gi 494964880 174 VEIRRLHKRLSATSVFVTH 192
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAH 638
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-225 |
1.61e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 73.68 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED----ITSGEIVIDDKVVNQLEPRER------GCAMVFQNyaly 87
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 88 PH--MNVAANMGYALkVAGVPREE-----------RDRRIKETARIVGLEDFLD---RKPAELSGGQRQRVAMGRAIIRE 151
Cdd:PRK15093 98 PQscLDPSERVGRQL-MQNIPGWTykgrwwqrfgwRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 152 PKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTP 225
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-214 |
1.66e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 10 RKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKS----TLLRMIAGLEDI-TSGEIVIDDK-VVNQLEPRERGC-----A 78
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGEsLLHASEQTLRGVrgnkiA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQN--YALYPHMNVAANMGYALKV-AGVPREERDRRIKETARIVG-------LEDFldrkPAELSGGQRQRVAMGRAI 148
Cdd:PRK15134 96 MIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGirqaakrLTDY----PHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGN-VEQ 214
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQ 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-217 |
1.85e-14 |
|
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: 74.98 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 12 AYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVnqLEPRErgcaMVFQNYALypHMN 91
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA--YVPQQ----AWIQNDSL--REN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAanMGYALKvagvprEERDRRIKETARIVGLEDFL---DR-----KPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:TIGR00957 719 IL--FGKALN------EKYYQQVLEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLS-ATSVFVTHDqVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGS 844
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-231 |
2.18e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 11 KAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL--EDITSGEIVIDDKVV---NQLEPRERGCAMVFQNYA 85
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqasNIRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 86 LYPHMNVAANM--GYALKVAGVPR-EERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:PRK13549 93 LVKELSVLENIflGNEITPGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494964880 163 NLDAKlRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGnvEQVGT-PLEVYNTPR--TRFVG 231
Cdd:PRK13549 173 SLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGTrPAAGMTEDDiiTMMVG 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-193 |
2.93e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVvnqleprerGCAMVFQN 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------RIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 84 YALYPHMNVAANMGYALKvAGVPREErdrrIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLR-PGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|
gi 494964880 164 LDAKLRVQMRVEIRRLHKRLSATSVFVTHD 193
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-193 |
3.91e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 9 VRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV-VNQL--EPR----------- 73
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIkVGYLpqEPQldptktvrenv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ERGCAMVFQNYALYPhmnvAANMGYALkvagvPREERDRRIKETARivgLEDFLD------------------RKP---- 131
Cdd:TIGR03719 90 EEGVAEIKDALDRFN----EISAKYAE-----PDADFDKLAAEQAE---LQEIIDaadawdldsqleiamdalRCPpwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 132 --AELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKlrvqmRVE-IRRLHKRLSATSVFVTHD 193
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-----SVAwLERHLQEYPGTVVAVTHD 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-208 |
4.40e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 13 YGRN-------PVVhgvdlnfRSGEFVVILGPSGCGKSTLLRMIAG--------LEDITSGEIVIDdkvvnqlepRERGC 77
Cdd:PRK13409 83 YGVNgfklyglPIP-------KEGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLK---------RFRGT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMvfQNY--ALYphmnvAANMGYALK---VAGVPR----------EERDRR--IKETARIVGLEDFLDRKPAELSGGQRQ 140
Cdd:PRK13409 147 EL--QNYfkKLY-----NGEIKVVHKpqyVDLIPKvfkgkvrellKKVDERgkLDEVVERLGLENILDRDISELSGGELQ 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 141 RVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHDQVEAMTLADKLVVMY 208
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-217 |
4.73e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAY-GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ--LEPRERGCAM 79
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYpHMNVAANmgyaLKVaGVPrEERDRRIKETARIVGLEDFLDRKPA-----------ELSGGQRQRVAMGRAI 148
Cdd:PRK13657 414 VFQDAGLF-NRSIEDN----IRV-GRP-DATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 149 IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlsATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK---GRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-202 |
6.13e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 13 YGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ-LEPRERGCAMVFQNYALYPHMN 91
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYALKVAGVPREerdrrIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180 190
....*....|....*....|....*....|.
gi 494964880 172 MRVEIRRlhKRLSATSVFVTHDQVEAMTLAD 202
Cdd:PRK13540 166 IITKIQE--HRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-212 |
1.62e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 28 SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQlEPRERGCAMVFQNYAL---YP-------HMNVAANMG 97
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYVPQSEEVdwsFPvlvedvvMMGRYGHMG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 98 YaLKVAgvprEERDRRIKETARI-VGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEI 176
Cdd:PRK15056 111 W-LRRA----KKRDRQIVTAALArVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 494964880 177 RRLHKRlSATSVFVTHDQVEAMTLADkLVVMYKGNV 212
Cdd:PRK15056 186 RELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-215 |
2.17e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKvvnQLEPR------ERGCAMVFQNY---ALYPH 89
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRspldavKKGMAYITESRrdnGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 90 MNVAANMGYA--LKVA------GVPREERDRRIKETAR-IVGLE-DFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDE 159
Cdd:PRK09700 356 FSIAQNMAISrsLKDGgykgamGLFHEVDEQRTAENQReLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 160 PLSNLDaklrVQMRVEIRRLHKRLS---ATSVFVTHDQVEAMTLADKLVVMYKGNVEQV 215
Cdd:PRK09700 436 PTRGID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
4-212 |
2.47e-13 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 71.14 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY----GRNPVVHG-VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQlepRERG-- 76
Cdd:TIGR01194 338 IELKDVHMNPkapeGSEGFALGpIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSA---DSRDdy 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 77 ---CAMVFQNYALYPHMnVAANMGyalKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPK 153
Cdd:TIGR01194 415 rdlFSAIFADFHLFDDL-IGPDEG---EHASLDNAQQYLQRLEIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRP 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 154 VFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQvEAMTLADKLVVMYKGNV 212
Cdd:TIGR01194 491 ILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-224 |
2.64e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 16 NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGleditsgeividdkvvnQLEPRERGCAMVFQNYALYPHM----- 90
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVswifn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 -NVAANMGYALKVAGvprEERDRRIKETARIVGLEDFLDRKPAEL-------SGGQRQRVAMGRAIIREPKVFLFDEPLS 162
Cdd:PLN03232 693 aTVRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 163 NLDAKLRVQ-----MRVEIRrlhkrlSATSVFVThDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNT 224
Cdd:PLN03232 770 ALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-229 |
3.96e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAY--GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ--LEPRERGCAM 79
Cdd:PLN03232 1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHmNVAANMGyalkvagvP-REERDRRIKETARIVGLEDFLDRKPAEL-----------SGGQRQRVAMGRA 147
Cdd:PLN03232 1315 IPQSPVLFSG-TVRFNID--------PfSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARA 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 148 IIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRT 227
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIREEFK--SCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
..
gi 494964880 228 RF 229
Cdd:PLN03232 1463 AF 1464
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-210 |
5.31e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMVFQNY---ALYPHM 90
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 NVAANM-----GYALKVAGvpreerdrRIKETARIVGLEDFLD----RKPA------ELSGGQRQRVAMGRAIIREPKVF 155
Cdd:PRK10762 346 SVKENMsltalRYFSRAGG--------SLKHADEQQAVSDFIRlfniKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 156 LFDEPLSNLDaklrVQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK10762 418 ILDEPTRGVD----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-216 |
5.33e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.89 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED--ITSGEIVIDDKVVNQLEPRER---GCAMV 80
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQnyalYPHMNVAANMGYALKVAgvPREERDRRIKETARIVGLEDFLDRK------PAEL---------SGGQRQRVAMG 145
Cdd:PRK09580 84 FQ----YPVEIPGVSNQFFLQTA--LNAVRSYRGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 146 RAIIREPKVFLFDEPLSNL--DAKLRVQMRVEIRRLHKRlsaTSVFVTHDQ-VEAMTLADKLVVMYKGNVEQVG 216
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLdiDALKIVADGVNSLRDGKR---SFIIVTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-212 |
7.55e-13 |
|
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: 66.90 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 5 RIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDIT---SGEIVIDDKVVNQLEPRERG-CA 78
Cdd:cd03233 7 RNISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGeII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 79 MVFQNYALYPHMNVAANMGYALKVAGvpreerdrriketarivglEDFLdRKpaeLSGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFALRCKG-------------------NEFV-RG---ISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHKRLSATsVFVTHDQ--VEAMTLADKLVVMYKGNV 212
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTT-TFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-169 |
8.29e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 66.43 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 16 NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEprERGCAMVFQNYALYPHMNVAAN 95
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494964880 96 MGYALKVAgvpreERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:PRK13541 91 LKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-165 |
1.11e-12 |
|
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: 69.19 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHgvDLNFR--SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV----VNQLepRErgc 77
Cdd:TIGR03719 323 IEAENLTKAFGDKLLID--DLSFKlpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklayVDQS--RD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 amvfqnyALYPHMNV--AANMGYALKVAGvpreerDRRIKETArIVGLEDFL----DRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:TIGR03719 396 -------ALDPNKTVweEISGGLDIIKLG------KREIPSRA-YVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....
gi 494964880 152 PKVFLFDEPLSNLD 165
Cdd:TIGR03719 462 GNVLLLDEPTNDLD 475
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-208 |
1.21e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 65.67 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 26 FRSGEFVVILGPSGCGKSTLLRMIAGleditsgeividdkvvnQLEPRERgcamvfqnyalyphmnvaanmgyalkvagv 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG-----------------QLIPNGD------------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 106 pREERDRriketARIVGLEDFLDrkpaeLSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSA 185
Cdd:cd03222 55 -NDEWDG-----ITPVYKPQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|...
gi 494964880 186 TSVFVTHDQVEAMTLADKLVVMY 208
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-193 |
1.34e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 9 VRKAYGRN-PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVI----------------DDKVVnqLE 71
Cdd:PRK11819 12 VSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPapgikvgylpqepqldPEKTV--RE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 72 PRERGCAMVFQNYALYphmN-VAANMgyalkvaGVPREERDRRIKETARivgLEDFLD------------------RKP- 131
Cdd:PRK11819 90 NVEEGVAEVKAALDRF---NeIYAAY-------AEPDADFDALAAEQGE---LQEIIDaadawdldsqleiamdalRCPp 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494964880 132 -----AELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK----LRvqmrveiRRLHkRLSATSVFVTHD 193
Cdd:PRK11819 157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLE-------QFLH-DYPGTVVAVTHD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-210 |
1.60e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRSGEFVVILGPSGCGKSTLLRMIAglEDITSGEIVIDDKVVNQlEPR----ERGCAMVFQNYALYPHMNVAANM 96
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNG-RPLdssfQRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 GYALKV---AGVPREERDRRIKETARIVGLEDFLDR---KPAE-LSGGQRQRVAMGRAIIREPKVFLF-DEPLSNLDAkl 168
Cdd:TIGR00956 858 RFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS-- 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494964880 169 rvQMRVEIRRLHKRLSAT--SVFVTHDQVEAMTLA--DKLVVMYKG 210
Cdd:TIGR00956 936 --QTAWSICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-210 |
2.43e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVN---QLEPRERGCAMVFQNYALYPHMNVAANM-- 96
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELNLVLQRSVMDNMwl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 -GYALKVAGVpreERDRRIKETARIVgleDFLD------RKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLR 169
Cdd:PRK10982 97 gRYPTKGMFV---DQDKMYRDTKAIF---DELDididprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494964880 170 VQMRVEIRRLHKRlSATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK10982 171 NHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-159 |
4.84e-12 |
|
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: 67.13 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAY----GRNP-VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVV---NQLEPRE 74
Cdd:COG4615 327 TLELRGVTYRYpgedGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 RGCAmVFQNYALYPHmnvaanmgyalkVAGVPREERDRRIK------ETARIVGLED--FLDRkpaELSGGQRQRVAMGR 146
Cdd:COG4615 407 LFSA-VFSDFHLFDR------------LLGLDGEADPARARellerlELDHKVSVEDgrFSTT---DLSQGQRKRLALLV 470
|
170
....*....|...
gi 494964880 147 AIIREPKVFLFDE 159
Cdd:COG4615 471 ALLEDRPILVFDE 483
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-210 |
1.37e-11 |
|
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: 63.50 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEI-----VIDDKVVNQLEPRERGCAMVFQNYALYPHMN 91
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYalkvaGVPREERdrRIKETARIVGLEDFLDRKP-----------AELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:cd03290 95 VEENITF-----GSPFNKQ--RYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 161 LSNLDAKLRVQ-MRVEIRRLHKRLSATSVFVTHdQVEAMTLADKLVVMYKG 210
Cdd:cd03290 168 FSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-217 |
1.50e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLR-MIAGLEDITSGEIVIDDKVvnqleprergcAMVFQNYALYpHMNVAAN 95
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYalkvaGVPREERdrRIKETARIVGLEDFLDRKPA-----------ELSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:PLN03130 699 ILF-----GSPFDPE--RYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 165 DAKLRVQ-----MRVEIRRlhkrlsATSVFVThDQVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:PLN03130 772 DAHVGRQvfdkcIKDELRG------KTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-221 |
2.56e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGleDIT----------SGEIVIDDKVVNQLEPR 73
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 74 ERGCAMVFQNYALYPHMNVAAN----MG-YALKVAGVPREERDRRIKETA-RIVGLEDFLDRKPAELSGGQRQRVAMGRA 147
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAReivlLGrYPHARRAGALTHRDGEIAWQAlALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 148 I---------IREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
...
gi 494964880 219 LEV 221
Cdd:PRK13547 240 ADV 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-224 |
4.48e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 57 SGEIVIDDKVVNQLEPRE-RGCAMVFQNYALYPHMNVAANMGYAlkvagvpREERDRR-IKETARIVGLEDFLDRKPAE- 133
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATREdVKRACKFAAIDEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 134 ----------LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKRLSATSVFVTHdQVEAMTLADK 203
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|.
gi 494964880 204 LVVMykGNVEQVGTPLEVYNT 224
Cdd:PTZ00265 1428 IVVF--NNPDRTGSFVQAHGT 1446
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
9.66e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 9.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMVFQNY---ALYPHMNVAAN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGYALKVAGVP-------REERDR--------RIKETARivgledflDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:PRK11288 352 INISARRHHLRagclinnRWEAENadrfirslNIKTPSR--------EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 161 LSNLDaklrVQMRVEIRRLHKRLSA---TSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:PRK11288 424 TRGID----VGAKHEIYNVIYELAAqgvAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-283 |
1.06e-10 |
|
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: 56.44 E-value: 1.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 494964880 235 GSPAMNFLEGSFSANGEQFIFDGLPFSIDAN---IGKRHAGQPVALGIRPEH 283
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGGVTLPLPEGqvlALKLYVGKEVILGIRPEH 52
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-240 |
1.28e-10 |
|
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: 61.41 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 16 NPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIviddkvvnqlepRERGCAMVFQNYALYPHMNVAAN 95
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MgyalkVAGVPREERdrRIKETARIVGLEDFLDRKPAE-----------LSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:cd03291 118 I-----IFGVSYDEY--RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 165 DakLRVQMRVEIRRLHKRL-SATSVFVThDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTpRTRFVGSFIGSPAMN 240
Cdd:cd03291 191 D--VFTEKEIFESCVCKLMaNKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSL-RPDFSSKLMGYDTFD 263
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-211 |
1.67e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPV-VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE--RGCAM 79
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 80 VFQNYALYPHMnvaanMGYALKVAGVPREERDRRIKETARIVGLED--FLDRKpaeLSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:PRK10522 402 VFTDFHLFDQL-----LGPEGKPANPALVEKWLERLKMAHKLELEDgrISNLK---LSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 158 DEPLSNLDAKLRvqmRVEIRRLHKRLSAT--SVF-VTHDQvEAMTLADKLVVMYKGN 211
Cdd:PRK10522 474 DEWAADQDPHFR---REFYQVLLPLLQEMgkTIFaISHDD-HYFIHADRLLEMRNGQ 526
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-192 |
1.84e-10 |
|
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: 62.46 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNFR--SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK----VVNQLEPRERGcamVFQNYALYPhmnvaaNM 96
Cdd:TIGR00954 470 SLSFEvpSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgklfYVPQRPYMTLG---TLRDQIIYP------DS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 GYALKVAGVpreeRDRRIKETARIVGLEDFLDRKPA---------ELSGGQRQRVAMGRAIIREPKVFLFDEPLSnldaK 167
Cdd:TIGR00954 541 SEDMKRRGL----SDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS----A 612
|
170 180
....*....|....*....|....*
gi 494964880 168 LRVQMRVEIRRLHKRLSATSVFVTH 192
Cdd:TIGR00954 613 VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-166 |
1.94e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 29 GEFVVILGPSGCGKSTLLRMIAGL--EDITSGEIVIDD-KVVNQLEPRergCAMVFQNYALYPHMNVAANMGYA--LKVA 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNrKPTKQILKR---TGFVTQDDILYPHLTVRETLVFCslLRLP 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 104 -GVPREERDRRIKETARIVGL---------EDFLdrkpAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDA 166
Cdd:PLN03211 171 kSLTKQEKILVAESVISELGLtkcentiigNSFI----RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-210 |
4.52e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNF--RSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRER-GCAMVF-----QNYALYPHMNVA 93
Cdd:PRK15439 280 RNISLevRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 94 ANMgYALKVAGVP---REERDRRIKET-ARIVGLEDFLDRKPAE-LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDakl 168
Cdd:PRK15439 360 WNV-CALTHNRRGfwiKPARENAVLERyRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD--- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494964880 169 rVQMRVEIRRLHKRLSATSV---FVTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK15439 436 -VSARNDIYQLIRSIAAQNVavlFISSDLEEIEQMADRVLVMHQG 479
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-231 |
8.75e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLeprerGCAMVFQNYALYPHMNVAanm 96
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-----GLMDLRKVLGIIPQAPVL--- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 97 gyalkVAGVPR-------EERDRRIKETARIVGLEDFLDRKP----AEL-------SGGQRQRVAMGRAIIREPKVFLFD 158
Cdd:PLN03130 1325 -----FSGTVRfnldpfnEHNDADLWESLERAHLKDVIRRNSlgldAEVseagenfSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 159 EPLSNLDAKLRVQMRVEIRRLHKrlSATSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRFVG 231
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFK--SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-229 |
9.83e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.56 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 8 QVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLL----RMIagleDITSGEIVIDDKVVNQLEPRE--RGCAMVF 81
Cdd:PTZ00243 1315 QMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYP---HMNV-------AANMGYALKVAGVpreeRDRRIKETArivGLEDFLDRKPAELSGGQRQRVAMGRAIIRE 151
Cdd:PTZ00243 1391 QDPVLFDgtvRQNVdpfleasSAEVWAALELVGL----RERVASESE---GIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494964880 152 PKVF-LFDEPLSNLDAKLRVQMRVEIRrlhKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTPRTRF 229
Cdd:PTZ00243 1464 GSGFiLMDEATANIDPALDRQIQATVM---SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-248 |
1.20e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 17 PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV-----VNQLEPRERGCAMVFQ-NYALYPHM 90
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIsfspqTSWIMPGTIKDNIIFGlSYDEYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 NVaanmgyalkVAGVPREERDRRIKETARIVgledfLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDaklrV 170
Cdd:TIGR01271 520 SV---------IKACQLEEDIALFPEKDKTV-----LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----V 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 171 QMRVEI--RRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVYNTpRTRFVGSFIGSPAMNflegSFSA 248
Cdd:TIGR01271 582 VTEKEIfeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK-RPDFSSLLLGLEAFD----NFSA 656
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-213 |
2.67e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 6 IEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAgleditsGEIVIDDKVVNQLEPRERG-CAmvfQNY 84
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKWSENANIGyYA---QDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 85 ALY--PHMNVAANMGYAlkvagvpREERDrriKETA------RIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:PRK15064 392 AYDfeNDLTLFDWMSQW-------RQEGD---DEQAvrgtlgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 157 FDEPLSNLDaklrvqMRvEIRRLHKRL---SATSVFVTHDQVEAMTLA-------DKLVVMYKGNVE 213
Cdd:PRK15064 462 MDEPTNHMD------ME-SIESLNMALekyEGTLIFVSHDREFVSSLAtriieitPDGVVDFSGTYE 521
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-217 |
2.95e-09 |
|
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: 55.79 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 8 QVRKAYGRNpvVHGVDLNFRSGEFVVILGPSGCGKSTLLRmiAGLEditsgeividdkvvnqleprERGCAMVFQNYALY 87
Cdd:cd03238 2 TVSGANVHN--LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--------------------ASGKARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 88 PHMNVAanmgyalkvagvpreerdrRIKETARI--VGLEDF-LDRKPAELSGGQRQRVAMGRAIIREPK--VFLFDEPLS 162
Cdd:cd03238 58 SRNKLI-------------------FIDQLQFLidVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 163 NLDAKLRVQMRVEIRRLhKRLSATSVFVTHDqVEAMTLADKLVVMYKGNVEQVGT 217
Cdd:cd03238 119 GLHQQDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-165 |
3.72e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHgvDLNFR--SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVvnQLeprergcAMVF 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLID--DLSFSlpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV--KL-------AYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNY-ALYPHMNVAanmgyalkvagvprEErdrriketarIVGLEDFLD-----------------------RKPAELSGG 137
Cdd:PRK11819 394 QSRdALDPNKTVW--------------EE----------ISGGLDIIKvgnreipsrayvgrfnfkggdqqKKVGVLSGG 449
|
170 180
....*....|....*....|....*...
gi 494964880 138 QRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-210 |
4.54e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 18 VVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL-EDITSGEIVIDDKVVNQLEPRE---RGCAMVFQN---YALYPHM 90
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 91 NVAANMgyalKVAGVPREERDRRIKETARIVGLEDFLDR----------KPAELSGGQRQRVAMGRAIIREPKVFLFDEP 160
Cdd:PRK13549 357 GVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494964880 161 LSNLDaklrVQMRVEIRRLHKRLSATSV---FVTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK13549 433 TRGID----VGAKYEIYKLINQLVQQGVaiiVISSELPEVLGLSDRVLVMHEG 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-204 |
6.23e-09 |
|
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: 54.30 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 28 SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDkvvnqleprergcamvfqnyalyphmnvaanmgyalkvagvpr 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 108 eerDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIR-----RLHKR 182
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|..
gi 494964880 183 LSATSVFVTHDQVEAMTLADKL 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-212 |
8.37e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCG--KSTLLRMIAGlEDITSGEIVIDDKVVNQLEPRERGCAMVF 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 82 QNYALYPHMNVAANMGYALKVAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPL 161
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 162 SNLDAKLRVQMRVEIRRLhKRLSATSVFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-210 |
1.23e-08 |
|
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: 54.17 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLED--ITSGEIVIDDKVVNQLEPRERGCAMvfQNYALYPHMN 91
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRSTGYVE--QQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VaanmgyalkvagvpREErdrrIKETARIVGledfldrkpaeLSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAklrvQ 171
Cdd:cd03232 96 V--------------REA----LRFSALLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----Q 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494964880 172 MRVEIRRLHKRLSAT--SVFVTHDQVEAMTLA--DKLVVMYKG 210
Cdd:cd03232 143 AAYNIVRFLKKLADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-214 |
1.45e-08 |
|
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: 56.84 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 14 GRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDiTSGEIVIDDKVVNQ--LEPRERGCAMVFQNYALYP--- 88
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvtLQTWRKAFGVIPQKVFIFSgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 89 HMNVAANMGYAlkvagvpreerDRRIKETARIVGLEDFLDRKPAEL-----------SGGQRQRVAMGRAIIREPKVFLF 157
Cdd:TIGR01271 1309 RKNLDPYEQWS-----------DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494964880 158 DEPLSNLDAklrVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQ 214
Cdd:TIGR01271 1378 DEPSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-213 |
2.39e-08 |
|
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: 55.60 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 19 VHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGL-EDITSGEIVIDDKVVNQLEPR---ERGCAMVFQN---YALYPHMN 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 92 VAANMGYAL-----KVAGVPREERDRRIKETARIVGLEDFLDRKP-AELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:TIGR02633 356 VGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494964880 166 aklrVQMRVEIRRLHKRLSATSV---FVTHDQVEAMTLADKLVVMYKGNVE 213
Cdd:TIGR02633 436 ----VGAKYEIYKLINQLAQEGVaiiVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-165 |
3.62e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 13 YGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAG------LEDIT-------SGEIVIDDK-----VVNQLepre 74
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrrgSGETIWDIKkhigyVSSSL---- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 75 rgcamvfqnyalypHMN--VAANM------GYaLKVAGVPREERDRRIKETAR---IVGLEDFLDRKP-AELSGGQRQRV 142
Cdd:PRK10938 346 --------------HLDyrVSTSVrnvilsGF-FDSIGIYQAVSDRQQKLAQQwldILGIDKRTADAPfHSLSWGQQRLA 410
|
170 180
....*....|....*....|...
gi 494964880 143 AMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-218 |
4.34e-08 |
|
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: 53.76 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRN--PVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQL---EPRERgC 77
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 AMVFQNYALYPHmNVAANMGYALKVAgvpreerDRRIKETARIVGLEDFLDRKPAEL-----------SGGQRQRVAMGR 146
Cdd:cd03288 98 SIILQDPILFSG-SIRFNLDPECKCT-------DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 147 AIIREPKVFLFDEPLSNLD-AKLRVQMRVEIRRLHKRlsaTSVFVTHdQVEAMTLADKLVVMYKGNVEQVGTP 218
Cdd:cd03288 170 AFVRKSSILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAH-RVSTILDADLVLVLSRGILVECDTP 238
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-222 |
4.97e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 4 IRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKV------VNQLEprergc 77
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklgyfaQHQLE------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 78 aMVFQNYALYPHMNVAAnmgyalkvagvPREErDRRIKETARIVGLE-DFLDRKPAELSGGQRQRVAMGRAIIREPKVFL 156
Cdd:PRK10636 387 -FLRADESPLQHLARLA-----------PQEL-EQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494964880 157 FDEPLSNLDaklrVQMRVEIRRLHKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEVY 222
Cdd:PRK10636 454 LDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-221 |
1.14e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 3 EIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQ--LEPRERGCAMV 80
Cdd:TIGR00957 1286 EFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 81 FQNYALYP---HMNVAANMGYAlkvagvpreerDRRIKETARIVGLEDFLDRKPAEL-----------SGGQRQRVAMGR 146
Cdd:TIGR00957 1366 PQDPVLFSgslRMNLDPFSQYS-----------DEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 147 AIIREPKVFLFDEPLSNLDAKLRVQMRVEIRrlhKRLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVGTPLEV 221
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIR---TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-165 |
1.64e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRsgefVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVnqleprergcAMVFQNYALyPHMNVAAN-MGYA 99
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR----------MAVFSQHHV-DGLDLSSNpLLYM 595
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 100 LKV-AGVPreerDRRIKETARIVGLEDFLDRKPA-ELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PLN03073 596 MRCfPGVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-212 |
3.42e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 15 RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPRE---RGCAMVFQ---NYALYP 88
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 89 HMNVA-----ANMGYALKVAGVpreERDRRIKETARIVgLEDFLDRKPAE------LSGGQRQRVAMGRAIIREPKVFLF 157
Cdd:PRK10982 340 YLDIGfnsliSNIRNYKNKVGL---LDNSRMKSDTQWV-IDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494964880 158 DEPLSNLDaklrVQMRVEIRRLHKRLSATS---VFVTHDQVEAMTLADKLVVMYKGNV 212
Cdd:PRK10982 416 DEPTRGID----VGAKFEIYQLIAELAKKDkgiIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-193 |
4.12e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 29 GEFVVILGPSGCGKSTLLRMIAGLEDITSGEIviddKVVNQLEprergcAMVFQNY--ALYPHMNVAANMGYALK---VA 103
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLE------VAYFDQHraELDPEKTVMDNLAEGKQevmVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 104 GVPREerdrriketarIVG-LEDFL-----DRKPAE-LSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDaklrvqmrVEI 176
Cdd:PRK11147 415 GRPRH-----------VLGyLQDFLfhpkrAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD--------VET 475
|
170 180
....*....|....*....|.
gi 494964880 177 RRLHKRLSA----TSVFVTHD 193
Cdd:PRK11147 476 LELLEELLDsyqgTVLLVSHD 496
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-164 |
9.93e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITS--GEIVIDDKVV-----NQLEprERGCAMVFQNYALYPHMNVAA 94
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdiRDSE--ALGIVIIHQELALIPYLSIAE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 95 NM--GYALKVAGV-PREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNL 164
Cdd:NF040905 98 NIflGNERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-210 |
1.22e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 21 GVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVVNQLEPR---ERGCAMVFQNYALYPHMNVAAN-- 95
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqEAGIGIIHQELNLIPQLTIAENif 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 96 MGyalkvagvpREERDR--RI----------KETARIvGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSN 163
Cdd:PRK10762 102 LG---------REFVNRfgRIdwkkmyaeadKLLARL-NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494964880 164 L-DAKLRVQMRVeIRRLhKRLSATSVFVTHDQVEAMTLADKLVVMYKG 210
Cdd:PRK10762 172 LtDTETESLFRV-IREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
277-348 |
1.46e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 45.30 E-value: 1.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494964880 277 LGIRPEHARLVpvGTPGAVPATVDFVEELGAGRVIHCDI-NGSSFAVAVANHTSG--ETGQAVALELPRDNIHLF 348
Cdd:pfam08402 1 LAIRPEKIRLA--AAANGLSGTVTDVEYLGDHTRYHVELaGGEELVVRVPNAHARppAPGDRVGLGWDPEDAHVL 73
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-226 |
1.53e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 33 VILGPSGCGKSTLLRMIAGLEDIT---SGEIVIDDKVVNQLEPReRGCAMVFQNYALYPHMNVAANMGYALKVAGV---- 105
Cdd:PLN03140 195 LLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPR-KTSAYISQNDVHVGVMTVKETLDFSARCQGVgtry 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 106 ------PREERDRRI----------KETA--------------RIVGLE---DFL--DRKPAELSGGQRQRVAMGRAIIR 150
Cdd:PLN03140 274 dllselARREKDAGIfpeaevdlfmKATAmegvksslitdytlKILGLDickDTIvgDEMIRGISGGQKKRVTTGEMIVG 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 151 EPKVFLFDEPLSNLDAKLRVQMrveIRRLHK--RLSATSVFVTHDQ--VEAMTLADKLVVMYKGNVeqvgtpleVYNTPR 226
Cdd:PLN03140 354 PTKTLFMDEISTGLDSSTTYQI---VKCLQQivHLTEATVLMSLLQpaPETFDLFDDIILLSEGQI--------VYQGPR 422
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-167 |
1.99e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 26 FRSGEFVVILGPSGCGKSTLLRMIAGLEdiTSGEIVIDDKVVNQLEPRE---RGCAMVFQNYALYPHMNVAANMGYA--L 100
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLAGRK--TGGYIEGDIRISGFPKKQEtfaRISGYCEQNDIHSPQVTVRESLIYSafL 980
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494964880 101 KVAG-VPREERDRRIKETARIVGLEDFLDR-----KPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAK 167
Cdd:PLN03140 981 RLPKeVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-182 |
1.79e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 1 MAEIRIEQVRKAYGRNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVID------------DKVVN 68
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlsfeqlQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 69 Q---------LEPRE----RGCAMVFQNyalyphmnvaanmgyalkvagvprEERDR-RIKETARIVGLEDFLDRKPAEL 134
Cdd:PRK10938 81 DewqrnntdmLSPGEddtgRTTAEIIQD------------------------EVKDPaRCEQLAQQFGITALLDRRFKYL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 494964880 135 SGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLHKR 182
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-209 |
2.66e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 23 DLNFRSGEFVVILGPSGCGKSTLLRMIagleditsgeividdkvvnqleprergCAMVFQNYAlyphmnvaanmgyalkv 102
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAI---------------------------GLALGGAQS----------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 103 AGVPREERDRRIKETARIVGLEDFLDRkpaeLSGGQRQRVAM-----GRAIIREPkVFLFDEPLSNLDakLRVQMRVE-- 175
Cdd:cd03227 51 ATRRRSGVKAGCIVAAVSAELIFTRLQ----LSGGEKELSALalilaLASLKPRP-LYILDEIDRGLD--PRDGQALAea 123
|
170 180 190
....*....|....*....|....*....|....
gi 494964880 176 IRRLHKRlSATSVFVTHDQvEAMTLADKLVVMYK 209
Cdd:cd03227 124 ILEHLVK-GAQVIVITHLP-ELAELADKLIHIKK 155
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-165 |
8.01e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 8.01e-04
10 20 30
....*....|....*....|....*....|....*..
gi 494964880 129 RKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLD 165
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-216 |
9.95e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 22 VDLNFRSGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDKVvnqleprergcAMVFQNYALYPHMNVAANMGYALK 101
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-----------SVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 102 VAGVPREERDRRIKETARIVGLEDFLDRKPAELSGGQRQRVAMGRAIIREPKVFLFDEPLSNLDAKLRVQMRVEIRRLhK 181
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-K 190
|
170 180 190
....*....|....*....|....*....|....*
gi 494964880 182 RLSATSVFVTHDQVEAMTLADKLVVMYKGNVEQVG 216
Cdd:PRK13546 191 EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-65 |
1.48e-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: 39.30 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|....*...
gi 494964880 28 SGEFVVILGPSGCGKSTLLRMIAGLEDITSGEIVIDDK 65
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEISEKLG 121
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
13-50 |
3.42e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 38.38 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 494964880 13 YGRNPVVHGV---------DLNFRSGEFVVILGPSGCGKSTLLRMIA 50
Cdd:cd03243 4 GGRHPVLLALtkgetfvpnDINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-227 |
3.56e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494964880 121 VGLEDF-LDRKPAELSGGQRQRVAMGRAIIREPK--VFLFDEPLSNLDAKLRVQMRVEIRRLhKRLSATSVFVTHDQvEA 197
Cdd:TIGR00630 475 VGLDYLsLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE-DT 552
|
90 100 110
....*....|....*....|....*....|....*.
gi 494964880 198 MTLADKLVVM------YKGNVEQVGTPLEVYNTPRT 227
Cdd:TIGR00630 553 IRAADYVIDIgpgageHGGEVVASGTPEEILANPDS 588
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
31-60 |
5.05e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 37.48 E-value: 5.05e-03
10 20 30
....*....|....*....|....*....|...
gi 494964880 31 FVVILGPSGCGKSTLLRMIA---GLEDITSGEI 60
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEI 34
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-49 |
5.78e-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: 36.74 E-value: 5.78e-03
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
32-64 |
6.66e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 36.70 E-value: 6.66e-03
10 20 30
....*....|....*....|....*....|....*.
gi 494964880 32 VVILGPSGCGKSTLLRMIA---GLEDITSGEIVIDD 64
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAkklGLPYLDTGGIRTEE 37
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
15-50 |
7.15e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.63 E-value: 7.15e-03
10 20 30
....*....|....*....|....*....|....*.
gi 494964880 15 RNPVVHGVDLNFRSGEFVVILGPSGCGKSTLLRMIA 50
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
20-46 |
9.99e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 9.99e-03
10 20
....*....|....*....|....*..
gi 494964880 20 HGVDLNFRSGeFVVILGPSGCGKSTLL 46
Cdd:pfam13476 10 RDQTIDFSKG-LTLITGPNGSGKTTIL 35
|
|
| |
