|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-352 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 546.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:COG3839 3 SLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPSMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 241 INDGEVdkEKGVLHIGKLQIPLSiGQLKQLPEGIIRIGMRPEHIALSEEGQ---EVTLQSVEVLGNESILNFAVNGTIWS 317
Cdd:COG3839 241 LLPGTV--EGGGVRLGGVRLPLP-AALAAAAGGEVTLGIRPEHLRLADEGDgglEATVEVVEPLGSETLVHVRLGGQELV 317
|
330 340 350
....*....|....*....|....*....|....*
gi 446493527 318 AKVIGQLLLNKGDKVKLLFSQEKLCFFNENTNERL 352
Cdd:COG3839 318 ARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-352 |
8.46e-165 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 464.70 E-value: 8.46e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPSMN 240
Cdd:PRK11650 162 LSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAMN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 241 INDGEVDKEKGVLHIGK-LQIPLSIGQLKQLPEGIIrIGMRPEHIALSEEGQEVTL--QSVEVLGNESILNFAVNGTIWS 317
Cdd:PRK11650 242 LLDGRVSADGAAFELAGgIALPLGGGYRQYAGRKLT-LGIRPEHIALSSAEGGVPLtvDTVELLGADNLAHGRWGGQPLV 320
|
330 340 350
....*....|....*....|....*....|....*
gi 446493527 318 AKVIGQLLLNKGDKVKLLFSQEKLCFFNENTNERL 352
Cdd:PRK11650 321 VRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-344 |
3.39e-156 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 442.61 E-value: 3.39e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGspSMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 241 INDGEV-DKEKGVLHIGKLQIPLSIGQlKQLPEGIIRIGMRPEHIALSEEGQE----VTLQSVEVLGNESILNFAV-NGT 314
Cdd:COG3842 241 LLPGTVlGDEGGGVRTGGRTLEVPADA-GLAAGGPVTVAIRPEDIRLSPEGPEnglpGTVEDVVFLGSHVRYRVRLgDGQ 319
|
330 340 350
....*....|....*....|....*....|..
gi 446493527 315 IWSAKV--IGQLLLNKGDKVKLLFSQEKLCFF 344
Cdd:COG3842 320 ELVVRVpnRAALPLEPGDRVGLSWDPEDVVVL 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-305 |
1.65e-129 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 375.52 E-value: 1.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYKNAEETavKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVFQN 83
Cdd:PRK11000 6 LRNVTKAYGDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 84 YALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSN 163
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 164 LDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPSMNIND 243
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMNFLP 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 244 GEVDKekgvLHIGKLQIPLSIGQLKQLP---EGIIR-----IGMRPEHIALSEEGqEVTL----QSVEVLGNES 305
Cdd:PRK11000 244 VKVTA----TAIEQVQVELPNRQQVWLPvegRGVQVganmsLGIRPEHLLPSDIA-DVTLegevQVVEQLGNET 312
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-235 |
2.45e-121 |
|
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: 349.61 E-value: 2.45e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIG 235
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
1.35e-119 |
|
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: 344.62 E-value: 1.35e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-341 |
9.73e-119 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 347.52 E-value: 9.73e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN-DLEPKDRNLSMV 80
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGspSMN 240
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 241 INDGEVdkEKGVLHIGKLQIPLSigqlKQLPEGIIRIGMRPEHIALSEEGQ-----EVTLQSVEVLGNESILNFAVNGT- 314
Cdd:COG1118 239 VLRGRV--IGGQLEADGLTLPVA----EPLPDGPAVAGVRPHDIEVSREPEgentfPATVARVSELGPEVRVELKLEDGe 312
|
330 340 350
....*....|....*....|....*....|...
gi 446493527 315 --IWSAKV----IGQLLLNKGDKVKLLFSQEKL 341
Cdd:COG1118 313 gqPLEAEVtkeaWAELGLAPGDPVYLRPRPARV 345
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
2.53e-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: 328.32 E-value: 2.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-331 |
5.18e-108 |
|
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: 320.45 E-value: 5.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:TIGR03265 5 LSIDNIRKRFGAF--TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:TIGR03265 83 QSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGspSMNI 241
Cdd:TIGR03265 163 SALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 242 NDGEVDKEkGVLHIGKLQipLSIGQLKQLPEGIIRIGMRPEHIALSEEGQE-----VTLQSVEVLGNESILNFAVNGtIW 316
Cdd:TIGR03265 241 LPGTRGGG-SRARVGGLT--LACAPGLAQPGASVRLAVRPEDIRVSPAGNAanlllARVEDMEFLGAFYRLRLRLEG-LP 316
|
330
....*....|....*
gi 446493527 317 SAKVIGQLLLNKGDK 331
Cdd:TIGR03265 317 GQALVADVSASEVER 331
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-248 |
3.33e-107 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 318.81 E-value: 3.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGspSMNI 241
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINI 250
|
....*..
gi 446493527 242 NDGEVDK 248
Cdd:PRK09452 251 FDATVIE 257
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-289 |
2.76e-105 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 313.47 E-value: 2.76e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEET--AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND-----LEPKD 74
Cdd:NF040933 3 VRVENVTKIFKKGKKEvvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:NF040933 83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFI 234
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 235 GspSMNINDGEVdKEKGVLHIGKLQIPLSIGQLKqlpEGIIRIGMRPEHIALSEE 289
Cdd:NF040933 243 G--DINLLEGKV-EEEGLVDGNDLKIPLPNPKLE---AGEVIIGIRPEDIDISES 291
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-303 |
2.94e-102 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 305.49 E-value: 2.94e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:PRK11432 7 VVLKNITKRFGSN--TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPsmNI 241
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NI 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 242 NDGEVDkeKGVLHIGKLQIPLSIGQLKQLPEGIIRIGMRPEHIALSEEG---QEVTLQSVEVLGN 303
Cdd:PRK11432 243 FPATLS--GDYVDIYGYRLPRPAAFAFNLPDGECTVGVRPEAITLSEQGeesQRCTIKHVAYMGP 305
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
7.84e-97 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 288.14 E-value: 7.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY--KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKDRNLS 78
Cdd:COG1116 7 ALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMD 158
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493527 159 EPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-289 |
9.18e-97 |
|
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: 290.55 E-value: 9.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 34 LVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKR 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 114 LMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 194 QIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPSM-NINDGEVDKEKGVLHiGKLQIPLSIGQLKQLPE 272
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVfEATVIERKSEQVVLA-GVEGRRCDIYTDVPVEK 239
|
250
....*....|....*...
gi 446493527 273 GI-IRIGMRPEHIALSEE 289
Cdd:TIGR01187 240 DQpLHVVLRPEKIVIEEE 257
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-236 |
1.13e-93 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 281.98 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:COG1125 1 MIEFENVTKRYPDGT-VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGL--KEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGS 236
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
2.08e-93 |
|
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: 278.84 E-value: 2.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQ----KEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGS 236
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-289 |
3.22e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 271.95 E-value: 3.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKnaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:NF040840 1 MIRIENLSKDWK---EFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:NF040840 78 YQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPsmN 240
Cdd:NF040840 158 LSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--N 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446493527 241 INDGEVDKEKG--VLHIGKLQIPLSIGQlkqlpEGIIRIGMRPEHIALSEE 289
Cdd:NF040840 236 IIEGVAEKGGEgtILDTGNIKIELPEEK-----KGKVRIGIRPEDITISTE 281
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-234 |
8.42e-89 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 272.36 E-value: 8.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY-KNAEET---------------------AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSG 58
Cdd:COG4175 3 KIEVRNLYKIFgKRPERAlklldqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 59 DLIINERVANDLEPKD------RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPG 132
Cdd:COG4175 83 EVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 133 QLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRI 242
|
250 260
....*....|....*....|..
gi 446493527 213 QQVGTPLDIYNEPANEFVASFI 234
Cdd:COG4175 243 VQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-215 |
2.62e-88 |
|
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: 265.10 E-value: 2.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEE--TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKdrnLSM 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNK--GSIQQV 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-289 |
8.10e-88 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 269.40 E-value: 8.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:PRK11607 19 LLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGspSMN 240
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG--SVN 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 241 INDGeVDKEKG----VLHIGKLQIPLSIGQLKQLPEGI-IRIGMRPEHIALSEE 289
Cdd:PRK11607 255 VFEG-VLKERQedglVIDSPGLVHPLKVDADASVVDNVpVHVALRPEKIMLCEE 307
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
2-235 |
5.59e-86 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 260.12 E-value: 5.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:TIGR00968 1 IEIANISKRF--GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIG 235
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-237 |
9.36e-84 |
|
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: 254.53 E-value: 9.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGL--KEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSP 237
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-234 |
2.13e-82 |
|
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: 251.79 E-value: 2.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVY-KNAEET---------------------AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGD 59
Cdd:cd03294 1 IKIKGLYKIFgKNPQKAfkllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 60 LIINERVANDLEPKD------RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQ 133
Cdd:cd03294 81 VLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 134 LSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQ 213
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|.
gi 446493527 214 QVGTPLDIYNEPANEFVASFI 234
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFF 261
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-235 |
1.61e-80 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 245.71 E-value: 1.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetaVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIG 235
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-301 |
2.00e-80 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 249.62 E-value: 2.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKV----RKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGsp 237
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG-- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 238 SMNINDGEVdkEKGVLHIGKLQIPLSIGQLKQlpeGIIRIGMRPEHIALSEEGQEVTLQSVEVL 301
Cdd:PRK10851 239 EVNRLQGTI--RGGQFHVGAHRWPLGYTPAYQ---GPVDLFLRPWEVDISRRTSLDSPLPVQVL 297
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
3.04e-76 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.55 E-value: 3.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYK--NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR--- 75
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 ---NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:COG1136 84 rrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 153 PICLMDEPLSNLDAKLRAQ-MRIeIREIQQRLGITMIYVTHDQiEAMTMGDRIMVLNKGSI 212
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
17-299 |
2.72e-75 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 236.81 E-value: 2.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 17 TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEIS--SGDLIINERVANDLEPKDRNLSMVFQNYALYPHLSVEE 94
Cdd:TIGR03258 19 TVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHAPPHKRGLALLFQNYALFPHLKVED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 95 NILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRI 174
Cdd:TIGR03258 99 NVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 175 EIREIQQRL-GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPSM--------NINDGE 245
Cdd:TIGR03258 179 EIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIlpaialgiTEAPGL 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 246 VDKEKGVLHIGKLQIPLSIGQLKQLpegiiriGMRPEHIALSE----EGQ-EVTLQSVE 299
Cdd:TIGR03258 259 VDVSCGGAVIFAFGDGRHDGRDKLA-------CIRPEHLALTPrpagEGRfHATIASVE 310
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
7.95e-75 |
|
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: 229.38 E-value: 7.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLE----PKDRNL 77
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGlkvrkvqkeerqkrlmeaiemvglkeyvkmkpgqLSGGQRQRVALARAIVSQAPICLM 157
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
4.36e-74 |
|
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: 228.91 E-value: 4.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEET--AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR---- 75
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 --NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQiEAMTMGDRIMVLNKGSI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-235 |
3.33e-73 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 226.95 E-value: 3.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAvkgvSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVR-KVQKEERQkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGlKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIG 235
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
1.14e-71 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 222.62 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----R 75
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 156 LMDEPLSNLDAKLRAQ-MRIeIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:COG2884 160 LADEPTGNLDPETSWEiMEL-LEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-235 |
1.55e-69 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 222.03 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVAND-----LEPKDRNLSMVFQNYALYPHLS 91
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDgENIMKQspvelREVRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQ 171
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 172 MRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIG 235
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-234 |
3.04e-69 |
|
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: 217.15 E-value: 3.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----R 75
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVR-KVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 155 CLMDEPLSNLDAKLRAqmRIE--IREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPaNEFVAS 232
Cdd:COG1127 163 LLYDEPTAGLDPITSA--VIDelIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
..
gi 446493527 233 FI 234
Cdd:COG1127 240 FL 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-235 |
1.73e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 212.55 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKDRNLS-- 78
Cdd:COG1126 1 MIEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE---DLTDSKKDINkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 -----MVFQNYALYPHLSVEENILFGL-KVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:COG1126 76 rrkvgMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 153 PICLMDEPLSNLDAKLRAqmriEIREIQQRL---GITMIYVTHDqieamtMG------DRIMVLNKGSIQQVGTPLDIYN 223
Cdd:COG1126 156 KVMLFDEPTSALDPELVG----EVLDVMRDLakeGMTMVVVTHE------MGfarevaDRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|..
gi 446493527 224 EPANEFVASFIG 235
Cdd:COG1126 226 NPQHERTRAFLS 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-236 |
4.37e-67 |
|
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: 211.97 E-value: 4.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE--TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RN 76
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNY--ALYPHLSVEENILFGLKVRKVQkeERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEAMT-MGDRIMVLNKGSIQQVGTPLDIYNEPANEFVAS 232
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRE 237
|
....
gi 446493527 233 FIGS 236
Cdd:COG1124 238 LLAA 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
6.02e-67 |
|
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: 219.77 E-value: 6.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY---KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--- 74
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 --RNLSMVFQN--YALYPHLSVEENILFGLKVRKVQ-KEERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALARAI 148
Cdd:COG1123 340 lrRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEAM-TMGDRIMVLNKGSIQQVGTPLDIYNEPAN 227
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
.
gi 446493527 228 E 228
Cdd:COG1123 499 P 499
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-216 |
1.03e-65 |
|
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: 207.15 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 28 KGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND------LEPKDRNLSMVFQNYALYPHLSVEENILFGLK 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 102 vRKVQKEERQkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQ 181
Cdd:cd03297 102 -RKRNREDRI-SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 446493527 182 RLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
5.68e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 209.55 E-value: 5.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY--KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---- 74
Cdd:COG1135 1 MIELENLSKTFptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:COG1135 81 rRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 154 ICLMDEPLSNLDAK-------LraqmrieIREIQQRLGITMIYVTHDqieamtMG------DRIMVLNKGSIQQVGTPLD 220
Cdd:COG1135 161 VLLCDEATSALDPEttrsildL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLD 227
|
250
....*....|....*..
gi 446493527 221 IYNEPANEFVASFIGSP 237
Cdd:COG1135 228 VFANPQSELTRRFLPTV 244
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
1.19e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 205.30 E-value: 1.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER--VANDLEPKdRNLSM 79
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvARDPAEVR-RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRlGITMIYVTH--DQIEAMTmgDRIMVLNKGSIQQVGTPLDI 221
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAE-GKTVLLSTHylEEAERLC--DRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
1.15e-62 |
|
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: 199.87 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyP-----HLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:COG1122 80 VFQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-212 |
2.05e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 199.90 E-value: 2.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----R 75
Cdd:COG3638 2 MLELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFG-------LK--VRKVQKEERQkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALAR 146
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQ-MRIeIREIQQRLGITMIYVTHdQIE-AMTMGDRIMVLNKGSI 212
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
3.85e-62 |
|
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: 198.50 E-value: 3.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY--KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNL- 77
Cdd:cd03257 1 LLEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 ----SMVFQNY--ALYPHLSVEENILFGLKVRKVQ--KEERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALARAI 148
Cdd:cd03257 81 rkeiQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEAM-TMGDRIMVLNKGSIQQVG 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAGKIVEEG 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-308 |
4.30e-62 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 202.64 E-value: 4.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 33 VLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND------LEPKDRNLSMVFQNYALYPHLSVEENILFGLKVRKvq 106
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRGNLLYGRKRAP-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 107 KEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGIT 186
Cdd:COG4148 107 RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 187 MIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPAneFVASFIGSPSMNINDGEV---DKEKGVLHIGKLQIPLS 263
Cdd:COG4148 187 ILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEAGSVLEATVaahDPDYGLTRLALGGGRLW 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446493527 264 IGQLKQLPEGIIRIGMRPEHIALSeegqevtLQSVEVLgneSILN 308
Cdd:COG4148 265 VPRLDLPPGTRVRVRIRARDVSLA-------LEPPEGS---SILN 299
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-234 |
1.14e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 197.62 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNL--- 77
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 -SMVFQNYALYPHLSVEENILFG-LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK09493 79 aGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 156 LMDEPLSNLDAKLRAqmriEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVAS 232
Cdd:PRK09493 159 LFDEPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
..
gi 446493527 233 FI 234
Cdd:PRK09493 235 FL 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-225 |
3.65e-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: 196.26 E-value: 3.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNA--EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHdQIEAM-TMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-210 |
4.22e-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: 195.38 E-value: 4.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSMV 80
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNyalyP-----HLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:cd03225 81 FQN----PddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
1.14e-60 |
|
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: 194.29 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNL---- 77
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGL-KVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 157 MDEPLSNLDaklrAQMRIEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03262 159 FDEPTSALD----PELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-233 |
3.49e-60 |
|
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: 193.87 E-value: 3.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----RN 76
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHLSVEENILFGLKV-RKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPaNEFVASF 233
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
2-212 |
2.77e-59 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 191.88 E-value: 2.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKN--AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPkDRnlSM 79
Cdd:NF040729 2 LKIQNISKTFINnkKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP-DR--GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVL--NKGSI 212
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.28e-58 |
|
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: 197.05 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEIS---SGDLIINERVANDLEPKDR-- 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQN--YALYPhLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
3.16e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 186.99 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY--KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERV-----Andlepk 73
Cdd:COG4525 3 MLTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 DRnlSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVL 207
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-210 |
6.20e-57 |
|
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: 184.76 E-value: 6.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----R 75
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA-ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 156 LMDEPLSNLDAKLRAQ-MRIeIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:TIGR02673 160 LADEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-228 |
2.50e-56 |
|
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: 183.92 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----RN 76
Cdd:cd03256 1 IEVENLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHLSVEENILFGLKVRK---------VQKEERQKRLmEAIEMVGLKEYVKMKPGQLSGGQRQRVALARA 147
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 148 IVSQAPICLMDEPLSNLDAKL-RAQMRIeIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
..
gi 446493527 227 NE 228
Cdd:cd03256 238 DE 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-221 |
1.47e-55 |
|
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: 182.55 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGLK-----VRKVQKEERQKrLMEAIEMVGLKEYvKMKP-GQLSGGQRQRVALARAIVSQA 152
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYphlglFGRPSAEDREA-VEEALERTGLEHL-ADRPvDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 153 PICLMDEPLSNLDakLRAQMRI--EIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:COG1120 157 PLLLLDEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-212 |
4.70e-55 |
|
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: 179.61 E-value: 4.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 23 SVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVFQNYALYPHLSVEENILFGLKV 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 103 RKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQR 182
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|
gi 446493527 183 LGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-193 |
2.13e-54 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 178.06 E-value: 2.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL--EEIS-SGDLIINERVANDLEPKDRNL 77
Cdd:COG4136 1 MLSLENLT--ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLkVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHD 193
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-224 |
7.27e-54 |
|
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: 178.39 E-value: 7.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINervanDLEPKD------- 74
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTLDeenlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -RNLSMVFQNyalyPH-----LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAI 148
Cdd:TIGR04520 76 rKKVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-210 |
4.66e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.62 E-value: 4.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGLKVRKVQ-KEERQKRLMEAiemVGLKEYVKMKP-GQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRERKfDRERALELLER---LGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 158 DEPLSNLDAKLRAqmRIE--IREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:COG4619 155 DEPTSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
1.08e-52 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 174.66 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR-NLSM 79
Cdd:COG4555 1 MIEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANE 228
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-226 |
2.36e-52 |
|
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: 176.01 E-value: 2.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEET--AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE---ISSGDLIINERVANDLEPKD- 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -----RNLSMVFQN-Y-ALYPHLSVEENILFGLKV-RKVQKEERQKRLMEAIEMVGL---KEYVKMKPGQLSGGQRQRVA 143
Cdd:COG0444 81 rkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 144 LARAIVSQAPICLMDEPLSNLDAKLRAQMrIE-IREIQQRLGITMIYVTHDqieamtMG------DRIMVLNKGSIQQVG 216
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQI-LNlLKDLQRELGLAILFITHD------LGvvaeiaDRVAVMYAGRIVEEG 233
|
250
....*....|
gi 446493527 217 TPLDIYNEPA 226
Cdd:COG0444 234 PVEELFENPR 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
2.82e-52 |
|
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: 173.64 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----R 75
Cdd:TIGR02315 1 MLEVENLSKVYPNGK-QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVRK--VQ------KEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARA 147
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHGRLGYKptWRsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-218 |
4.29e-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: 172.75 E-value: 4.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKnaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEI-----SSGDLIINERVANDLEPKD-- 74
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 --RNLSMVFQNYALYPhLSVEENILFGLKVRKVQKEERQKRLME-AIEMVGLKEYVK--MKPGQLSGGQRQRVALARAIV 149
Cdd:cd03260 79 lrRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWDEVKdrLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 150 SQAPICLMDEPLSNLDAklRAQMRIE--IREIQQRlgITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:cd03260 158 NEPEVLLLDEPTSALDP--ISTAKIEelIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-221 |
1.55e-51 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 171.11 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPkDRnlSMVFQNYALYPHLSVEENILF 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DR--MVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 99 GLK--VRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEI 176
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446493527 177 REIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-212 |
2.23e-51 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 170.92 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETavkgVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMV 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFG----LKVRKVQKEERQKRLmeaiEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGLGlnpgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
2.78e-51 |
|
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: 170.38 E-value: 2.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER-VANDLEPKDRNLSMV 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQM-RIEIREIQQRlgiTMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPL 219
Cdd:cd03263 161 TSGLDPASRRAIwDLILEVRKGR---SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-212 |
4.72e-51 |
|
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: 169.51 E-value: 4.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----RN 76
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-280 |
5.84e-51 |
|
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: 173.76 E-value: 5.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 34 LVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND------LEPKDRNLSMVFQNYALYPHLSVEENILFGLKvrKVQK 107
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK--RARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 108 EERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITM 187
Cdd:TIGR02142 106 SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 188 IYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASfigSPSMNINDGEVDKEKGVLHIGKLQIPlsiGQL 267
Cdd:TIGR02142 186 LYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR---EDQGSLIEGVVAEHDQHYGLTALRLG---GGH 259
|
250
....*....|...
gi 446493527 268 KQLPEGIIRIGMR 280
Cdd:TIGR02142 260 LWVPENLGPTGAR 272
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-214 |
1.47e-50 |
|
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: 168.77 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE--TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKD---- 74
Cdd:COG4181 8 IIELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -----RNLSMVFQNYALYPHLSVEENILFGLKVRkvQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIV 149
Cdd:COG4181 85 arlraRHVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 150 SQAPICLMDEPLSNLDAKLRAQMrIE-IREIQQRLGITMIYVTHDQIEAmTMGDRIMVLNKGSIQQ 214
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQI-IDlLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-226 |
3.00e-50 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 171.07 E-value: 3.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----RNLSMVFQN-YA-LYPHL 90
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVRKVQ-KEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:COG4608 113 TVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 169 RAQMRIEIREIQQRLGITMIYVTHD-----QIeamtmGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:COG4608 193 QAQVLNLLEDLQDELGLTYLFISHDlsvvrHI-----SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-218 |
4.00e-50 |
|
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: 178.49 E-value: 4.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPHL---SVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALA 145
Cdd:COG2274 554 VLQD----VFLfsgTIRENITLG------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTH 693
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-233 |
2.26e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 170.60 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 12 KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINE------RVANDLEPKDRNLSMVFQNYA 85
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakiSDAELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 86 LYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLD 165
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 166 AKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASF 233
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
2.96e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 165.65 E-value: 2.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKDRNLSMV 80
Cdd:COG1121 6 AIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPH--LSVEENILFGLK-----VRKVQKEERQkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 154 ICLMDEPLSNLDAKLRAQ-MRIeIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQvGTPLDIYNEPA 226
Cdd:COG1121 160 LLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
1.47e-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: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVANDLEPKDRNLSMV 80
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLgKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENIlfglkvrkvqkeerqkrlmeaiemvglkeyvkmkpgQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-218 |
1.64e-48 |
|
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: 171.86 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYkNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG4988 337 IELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPHL---SVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALA 145
Cdd:COG4988 416 VPQN----PYLfagTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTH 555
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
1.68e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 164.93 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVY-KN--AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---- 74
Cdd:TIGR04521 1 IKLKNVSYIYqPGtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -RNLSMVFQnyalYPH-----LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKE-YVKMKPGQLSGGQRQRVALARA 147
Cdd:TIGR04521 81 rKKVGLVFQ----FPEhqlfeETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
1.97e-48 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.08 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRnlsMVFQN 83
Cdd:PRK11247 15 LNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 84 YALYPHLSVEENILFGLKvrkvqkEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSN 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493527 164 LDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
2.83e-48 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 162.34 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 23 SVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVFQNYALYPHLSVEENILFGLKV 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 103 RKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 446493527 183 LGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
3.55e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 164.03 E-value: 3.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPH-----LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTmGDRIMVLNKGSIQQVGTPLDIY 222
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
4.44e-48 |
|
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: 161.49 E-value: 4.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVANDLEPKDRNLSM 79
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERqkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITmIYVTHDQIEA 197
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAV-LLTTHQPLEL 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-236 |
6.48e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 165.36 E-value: 6.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNA--EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---- 74
Cdd:PRK11153 1 MIELKNISKVFPQGgrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:PRK11153 81 rRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTH--DQIEAMTmgDRIMVLNKGSIQQVGTPLDIYNEPANEFVA 231
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKRIC--DRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
....*
gi 446493527 232 SFIGS 236
Cdd:PRK11153 239 EFIQS 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-210 |
8.52e-48 |
|
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: 159.47 E-value: 8.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENIlfglkvrkvqkeerqkrlmeaiemvglkeyvkmkpgqLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHDqIEAMTMGDRIMVLNKG 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-207 |
1.22e-47 |
|
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: 160.47 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN------L 77
Cdd:TIGR03608 1 LKNISKKFGD--KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrrekL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493527 158 DEPLSNLDAKLRaQMRIEIREIQQRLGITMIYVTHDQiEAMTMGDRIMVL 207
Cdd:TIGR03608 159 DEPTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-234 |
9.82e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 9.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER---VANDLEPKD---- 74
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAirel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -RNLSMVFQNYALYPHLSVEEN-ILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:PRK11124 81 rRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQrLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPlDIYNEPANEFVAS 232
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAFKN 238
|
..
gi 446493527 233 FI 234
Cdd:PRK11124 239 YL 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-234 |
1.71e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.94 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-----------NERVANDL 70
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsqkpSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 71 EpkdRNLSMVFQNYALYPHLSVEENILFG-LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIV 149
Cdd:COG4161 81 R---QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 150 SQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTpLDIYNEPANEF 229
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEA 235
|
....*
gi 446493527 230 VASFI 234
Cdd:COG4161 236 FAHYL 240
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-218 |
1.88e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.80 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG1132 340 IEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALARAI 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 149 VSQAPICLMDEPLSNLDAklraqmRIEiREIQQRL-----GITMIYVTH--DQIEAMtmgDRIMVLNKGSIQQVGTP 218
Cdd:COG1132 492 LKDPPILILDEATSALDT------ETE-ALIQEALerlmkGRTTIVIAHrlSTIRNA---DRILVLDDGRIVEQGTH 558
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-210 |
2.95e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 154.23 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINervANDLEPKDRNLSMVFQ 82
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF---GKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 83 NYAL---YPhLSVEENILFGL-----KVRKVQKEERQKrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-218 |
6.24e-45 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 162.24 E-value: 6.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPHL---SVEENILFGlkvRKVQKEErqkRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALA 145
Cdd:COG4987 414 VPQR----PHLfdtTLRENLRLA---RPDATDE---ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREI-QQRlgiTMIYVTHDQiEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAlAGR---TVLLITHRL-AGLERMDRILVLEDGRIVEQGTH 553
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
6.46e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 155.66 E-value: 6.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYK-NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN--ERVANDLEPKDRNL 77
Cdd:PRK13650 4 IIEVKNLTFKYKeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNyalyPH-----LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:PRK13650 84 GMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGTPLDIY 222
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-226 |
1.15e-44 |
|
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: 153.36 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---LS 78
Cdd:cd03219 1 LEVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGLKVR--------KVQKEERQ--KRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAI 148
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARtgsglllaRARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
1.25e-44 |
|
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: 150.86 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSMV 80
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQnyalyphlsveenilfglkvrkvqkeerqkrlmeaiemvglkeyvkmkpgqLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
3.78e-44 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 152.89 E-value: 3.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---L 77
Cdd:COG0411 4 LLEVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFG-------------LKVRKVQKEERQ--KRLMEAIEMVGLKEYVKMKPGQLSGGQRQRV 142
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEREarERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 143 ALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEA-MTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVLDFGRVIAEGTPAEV 240
|
....*
gi 446493527 222 YNEPA 226
Cdd:COG0411 241 RADPR 245
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
5.27e-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: 146.25 E-value: 5.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSMVFQNYALYPHLSVEENI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 97 LFGLKVRKVQKEERQKRLMEAIEMVGL----KEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-212 |
1.22e-42 |
|
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: 147.88 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEET--AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR--- 75
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 ---NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:TIGR02211 81 rnkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMgDRIMVLNKGSI 212
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-236 |
2.59e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 148.45 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKN-------AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandLEPKD 74
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---LEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -----RNLSMVFQ--NYALYPHLSVEENILFGLKVR-KVQKEERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALA 145
Cdd:COG4167 82 ykyrcKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqieamtMG------DRIMVLNKGSIQQVGTPL 219
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH------LGivkhisDKVLVMHQGEVVEYGKTA 235
|
250
....*....|....*..
gi 446493527 220 DIYNEPANEFVASFIGS 236
Cdd:COG4167 236 EVFANPQHEVTKRLIES 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-228 |
3.91e-42 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 154.07 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEiSSGDLI-----INERVANDLEPKDRNLSMVFQN-YA-LYPHL 90
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRfdgqdLDGLSRRALRPLRRRMQVVFQDpFGsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVRKVQ--KEERQKRLMEAIEMVGLKE-----YvkmkPGQLSGGQRQRVALARAIVSQAPICLMDEPLSN 163
Cdd:COG4172 380 TVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLDPaarhrY----PHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 164 LDAKLRAQMrIEI-REIQQRLGITMIYVTHDQ--IEAMTmgDRIMVLNKGSIQQVGTPLDIYNEPANE 228
Cdd:COG4172 456 LDVSVQAQI-LDLlRDLQREHGLAYLFISHDLavVRALA--HRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-210 |
6.54e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 147.15 E-value: 6.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDlEPKDRnlSMV 80
Cdd:PRK11248 1 MLQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
7.31e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 145.59 E-value: 7.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEET--AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN--ERVANDLEPKdRN 76
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEAR-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREiQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-236 |
3.77e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.94 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVA------NDLEPK 73
Cdd:COG4598 8 ALEVRDLHKSFGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgEEIRlkpdrdGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 DR--------NLSMVFQNYALYPHLSVEENILFG-LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVAL 144
Cdd:COG4598 86 DRrqlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 145 ARAIVSQAPICLMDEPLSNLDAKLRAQ----MRIEIREiqqrlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLD 220
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEvlkvMRDLAEE-----GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
250
....*....|....*.
gi 446493527 221 IYNEPANEFVASFIGS 236
Cdd:COG4598 241 VFGNPKSERLRQFLSS 256
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
4.53e-41 |
|
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: 143.50 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPHL---SVEENILFGLKVRKVQkeerqkRLMEAIEMVGLKEYVKMKP----------GQ-LSGGQRQRVALA 145
Cdd:cd03245 83 VPQD----VTLfygTLRDNITLGAPLADDE------RILRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 146 RAIVSQAPICLMDEPLSNLDakLRAQMRIeIREIQQRL-GITMIYVTHdQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMD--MNSEERL-KERLRQLLgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
7.23e-41 |
|
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: 142.74 E-value: 7.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKnaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03268 1 LKTNDLTKTYG--KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVqkeeRQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-216 |
7.41e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.80 E-value: 7.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSMV 80
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQnyalyphlsveenilfglkvrkvqkeerqkrlmeAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 161 LSNLDakLRAQMRI--EIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03214 125 TSHLD--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
2.08e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.59 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNyalyPH-----LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:PRK13632 87 IIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAmTMGDRIMVLNKGSIQQVGTPLDIYNEpaNEFVAS- 232
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN--KEILEKa 239
|
250
....*....|....*.
gi 446493527 233 -----FIGSPSMNIND 243
Cdd:PRK13632 240 kidspFIYKLSKKLKG 255
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-226 |
1.08e-39 |
|
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: 141.48 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY-------KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK 73
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 D-----RNLSMVFQNY--ALYPHLSVEENILFGLK-VRKVQKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVAL 144
Cdd:TIGR02769 82 QrrafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 145 ARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI--QQVGTPLDIY 222
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSF 241
|
....
gi 446493527 223 NEPA 226
Cdd:TIGR02769 242 KHPA 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-224 |
1.66e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 141.72 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINervanDLEPKDRNLS 78
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-----GVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 M---------VFQ--NYALYPHlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLK--EYVKMKPGQLSGGQRQRVALA 145
Cdd:PRK13637 78 LsdirkkvglVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-218 |
2.64e-39 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 139.04 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINervANDL--EPKD--RNL 77
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA---GHDVvrEPREvrRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-226 |
7.32e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.44 E-value: 7.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY-------KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK 73
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 D-----RNLSMVFQNY--ALYPHLSVEENI------LFGLKvrkvqKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQR 139
Cdd:PRK10419 83 QrkafrRDIQMVFQDSisAVNPRKTVREIIreplrhLLSLD-----KAERLARASEMLRAVDLDDSVLDKrPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 140 QRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI--QQVGT 217
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVG 237
|
....*....
gi 446493527 218 PLDIYNEPA 226
Cdd:PRK10419 238 DKLTFSSPA 246
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-225 |
2.55e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.39 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL--------EEISSGDLIINERVANDLEPK 73
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 drnLSMVFQNY-ALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:PRK13640 86 ---VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
3.40e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.19 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE-----ISSGDLIIN-ERVANDLEPKD 74
Cdd:PRK11264 3 AIEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDtARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 RNL----SMVFQNYALYPHLSVEENILFG-LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIV 149
Cdd:PRK11264 81 RQLrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 150 SQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANE- 228
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPr 239
|
250
....*....|
gi 446493527 229 ---FVASFIG 235
Cdd:PRK11264 240 trqFLEKFLL 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
3.78e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 137.58 E-value: 3.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQN-YALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK13648 87 IVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTmGDRIMVLNKGSIQQVGTPLDIYN 223
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
6.12e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.14 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEET----AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEP--KD 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 RNLS-MVFQNyalyPHLS-----VEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALArAI 148
Cdd:PRK13633 84 RNKAgMVFQN----PDNQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA-GI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 149 VSQAPICLM-DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTmGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK13633 159 LAMRPECIIfDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-212 |
6.75e-38 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 143.85 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFGlkVRKVQKEErqkrLMEAIEMVGLKEYVKMKP----------GQ-LSGGQRQRVALARAI 148
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALG--APYADDEE----ILRAAELAGVTEFVRRHPdgldmqigerGRsLSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 149 VSQAPICLMDEPLSNLDAklRAQMRIeIREIQQRL-GITMIYVTHdQIEAMTMGDRIMVLNKGSI 212
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDN--RSEERF-KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
1.04e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.98 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER-VANDLEPK-DR 75
Cdd:COG1101 1 MLELKNLSKTFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYKrAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYAL--YPHLSVEENIL--------FGLKvRKVQKEERQ--KRLMEAIEMvGLKEYVKMKPGQLSGGQRQRVA 143
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLR-RGLTKKRRElfRELLATLGL-GLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 144 LARAIVSQAPICLMDEPLSNLDAKlRAQMRIEI-REIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
1.76e-37 |
|
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: 141.27 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGlkvRKVQKEERqkrLMEAIEMVGLKEYVKMKPGQ-----------LSGGQRQRVALARAI 148
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLA---RPDASDAE---IREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHDqIEAMTMGDRIMVL 207
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-207 |
1.72e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.84 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---RNL 77
Cdd:COG1129 4 LLEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKVRK---VQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 155 CLMDEPLSNLDAKLRAQM-RIeIREIQQRlGITMIYVTHDQIEAMTMGDRIMVL 207
Cdd:COG1129 162 LILDEPTASLTEREVERLfRI-IRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-218 |
4.06e-36 |
|
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: 130.63 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---LS 78
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGLKVRKvqKEERQKRLMEAIEMV-GLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-224 |
6.67e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 130.97 E-value: 6.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE--------------------TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDL 60
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 61 IINERVANDLEpkdrnLSMVFQnyalyPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQ 140
Cdd:COG1134 84 EVNGRVSALLE-----LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 141 RVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHD--QIEAMTmgDRIMVLNKGSIQQVGTP 218
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSmgAVRRLC--DRAIWLEKGRLVMDGDP 230
|
....*....
gi 446493527 219 ---LDIYNE 224
Cdd:COG1134 231 eevIAAYEA 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
2.19e-35 |
|
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: 128.46 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGeFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER-VANDLEPKDRNLSMV 80
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKlraqMRIEIREIQQRLGITMIYV--TH--DQIEAMTmgDRIMVLNKGSIQQVG 216
Cdd:cd03264 158 TAGLDPE----ERIRFRNLLSELGEDRIVIlsTHivEDVESLC--NQVAVLNKGKLVFEG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-210 |
2.98e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 128.45 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-----R 75
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 156 LMDEPLSNLDAKLRAQMrIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK10908 160 LADEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
3.04e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.43 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:COG4604 1 MIEIKNVSKRYGG--KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGlkvR------KVQKEERQKrLMEAIEMVGLKE----YVKmkpgQLSGGQRQRVALARAI 148
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFG---RfpyskgRLTAEDREI-IDEAIAYLDLEDladrYLD----ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-235 |
1.33e-34 |
|
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: 127.10 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE----ISSGDLIINERVANDLEPKDRNLSMVFQN--YALYPHLS 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENILFGLKVRKVQKEERQKRLMEAIEMVGL---KEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 169 RAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIG 235
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-226 |
2.51e-34 |
|
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: 126.25 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---L 77
Cdd:COG0410 3 MLEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKVRKVQKEERqkrlmEAIEMVG-----LKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVR-----ADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-234 |
2.56e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.01 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 6 NVSKVYKN-AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---------- 74
Cdd:PRK10619 7 NVIDLHKRyGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 -----RNLSMVFQNYALYPHLSVEENILFG-LKVRKVQKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQRQRVALARA 147
Cdd:PRK10619 87 lrllrTRLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAqmriEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVG----EVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|
gi 446493527 225 PANEFVASFI 234
Cdd:PRK10619 243 PQSPRLQQFL 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
3.25e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.83 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERV------ANDLEP 72
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 73 KDRNLSMVFQ--NYALYPHlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQRQRVALARAIV 149
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 150 SQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
4.30e-34 |
|
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: 125.09 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvANDLEPKDRnLSMVF 81
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-PLDIAARNR-IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 162 SNLDAKLRAQMRIEIREiQQRLGITMIYVTH--DQIEAMTmgDRIMVLNKGSIQQVG 216
Cdd:cd03269 157 SGLDPVNVELLKDVIRE-LARAGKTVILSTHqmELVEELC--DRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
4.74e-34 |
|
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: 123.31 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---LS 78
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARragIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQnyalyphlsveenilfglkvrkvqkeerqkrlmeaiemvglkeyvkmkpgqLSGGQRQRVALARAIVSQAPICLMD 158
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 159 EPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGsiQQVGT 217
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-234 |
5.17e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 126.18 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEIS-----SGDLIINER--VANDLEPKD 74
Cdd:PRK14247 4 IEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQdiFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 RNLSMVFQNYALYPHLSVEENILFGLKVRKV--QKEERQKRLMEAIEMVGLKEYVKMK----PGQLSGGQRQRVALARAI 148
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANE 228
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*.
gi 446493527 229 FVASFI 234
Cdd:PRK14247 240 LTEKYV 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-234 |
6.84e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 6.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLL----RMIagleeissgDLIINERVANDLEPKDRNL 77
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMN---------DLIPGARVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 --------------SMVFQNYALYPHlSVEENILFGLKVRKV-QKEERQKRLMEAIEMVGLKEYVK---MKPGQ-LSGGQ 138
Cdd:COG1117 81 ydpdvdvvelrrrvGMVFQKPNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDEVKdrlKKSALgLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 139 RQRVALARAIVSQAPICLMDEPLSNLDAKlrAQMRIE--IREIQQRLgiTMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPI--STAKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|....*...
gi 446493527 217 TPLDIYNEPANEFVASFI 234
Cdd:COG1117 236 PTEQIFTNPKDKRTEDYI 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-214 |
7.59e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 125.31 E-value: 7.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 6 NVSKVYK--NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDL------EPKDRNL 77
Cdd:PRK11629 10 NLCKRYQegSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMgDRIMVLNKGSIQQ 214
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-236 |
8.68e-34 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 126.06 E-value: 8.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYK-------NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN--DLE 71
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 72 PKDRNLSMVFQN--YALYPHLSVEENILFGLKVR-KVQKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVALARA 147
Cdd:PRK15112 84 YRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPAN 227
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 243
|
....*....
gi 446493527 228 EFVASFIGS 236
Cdd:PRK15112 244 ELTKRLIAG 252
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-226 |
1.06e-33 |
|
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: 124.58 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR-NLSMV 80
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 F--QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMD 158
Cdd:cd03218 79 YlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 159 EPLSNLDAklraqmrIEIREIQQ------RLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:cd03218 159 EPFAGVDP-------IAVQDIQKiikilkDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-216 |
1.32e-33 |
|
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: 124.18 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVY--------------------KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLI 61
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 62 INERVAndlepkdrnlSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQR 141
Cdd:cd03220 81 VRGRVS----------SLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 142 VALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-263 |
1.76e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 126.62 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER---VANDLEPKD--RNLSMVFQN-YA-LYPHL 90
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllKADPEAQKLlrQKIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVR-KVQKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:PRK11308 110 KVGQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 169 RAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGS-PSMNINDgevD 247
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSAtPRLNPDD---R 266
|
250
....*....|....*.
gi 446493527 248 KEKGVLHiGKLQIPLS 263
Cdd:PRK11308 267 RERIKLT-GELPSPLN 281
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-234 |
6.55e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 123.03 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEIS-----SGDLIINER--VANDLEPKD 74
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRniYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 --RNLSMVFQNYALYPHLSVEENILFGLKVRKV--QKEERQKRLMEAIEMVGLKEYVKMK----PGQLSGGQRQRVALAR 146
Cdd:PRK14267 83 vrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
....*...
gi 446493527 227 NEFVASFI 234
Cdd:PRK14267 241 HELTEKYV 248
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-218 |
6.74e-33 |
|
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: 122.22 E-value: 6.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKST----LLRMIagleEISSGDLIINERVANDLEPKD--R 75
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNyalyPHL---SVEENI-LFGlkvrkvQKEErqKRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQ 140
Cdd:cd03244 79 RISIIPQD----PVLfsgTIRSNLdPFG------EYSD--EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 141 RVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREiqQRLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-212 |
1.37e-32 |
|
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: 122.12 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-------NERVAnDLEPK 73
Cdd:COG1119 3 LLELRNVT-VRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrgGEDVW-ELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 DRNLSMVFQNYaLYPHLSVEENIL------FGLkVRKVQKEERQkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARA 147
Cdd:COG1119 80 IGLVSPALQLR-FPRDETVLDVVLsgffdsIGL-YREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHdQIEAMTMG-DRIMVLNKGSI 212
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH-HVEEIPPGiTHVLLLKDGRV 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-217 |
1.79e-32 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 121.57 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALARAI 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG------RPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-212 |
3.84e-32 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 118.86 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENIlfglkvrkvqkeerqkrlmeaiemvglkeyvkmkpgqLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHdQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-229 |
3.90e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.36 E-value: 3.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 14 AEETAVKGVSVHIKKGEFFVLVGPSGCGKST----LLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVFQ--NYALY 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 88 PHLSVEENILFGLKV--RKVQKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQRQRVALARAIVSQAPICLMDEPLSNL 164
Cdd:PRK15134 377 PRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 165 DAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEF 229
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-212 |
5.36e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 126.76 E-value: 5.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEET--AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---- 74
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 --RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:PRK10535 84 rrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHD-QIEAmtMGDRIMVLNKGSI 212
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDpQVAA--QAERVIEIRDGEI 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
6.86e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 120.89 E-value: 6.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKnaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLeeiSSGDLIINE-------------RVA 67
Cdd:PRK09984 4 IIRVEKLAKTFN--QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGShiellgrtvqregRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 68 NDLEPKDRNLSMVFQNYALYPHLSVEENILFGLK---------VRKVQKEERQkRLMEAIEMVGLKEYVKMKPGQLSGGQ 138
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 139 RQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-217 |
1.40e-31 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 119.18 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAV-KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPhLSVEENILFGLKVRKVQKEERQKRLMEAIEMV-----GLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 154 ICLMDEPLSNLDAKLRAqmrieirEIQQ-----RLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:cd03249 160 ILLLDEATSALDAESEK-------LVQEaldraMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-218 |
1.51e-31 |
|
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: 125.84 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKD-----RN 76
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQ---DLAGLDvqavrRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHlSVEENILFGLKVRkvqkeerQKRLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALA 145
Cdd:TIGR03797 529 LGVVLQNGRLMSG-SIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIA 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQmrieIREIQQRLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQAI----VSESLERLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTY 668
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.71e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.18 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERV----ANDLEPKDRN 76
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQN---YALYPhlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:PRK13639 80 VGIVFQNpddQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-212 |
2.47e-31 |
|
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: 117.74 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYKNAEETaVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANdlePKDR--NLSMV 80
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERrkSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQN--YALYPHlSVEENILFGLKvRKVQKEERQKRLMEAIEMVGLKEyvkMKPGQLSGGQRQRVALARAIVSQAPICLMD 158
Cdd:cd03226 77 MQDvdYQLFTD-SVREELLLGLK-ELDAGNEQAETVLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 159 EPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-225 |
3.56e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 120.58 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR-----NLSMVFQN--YALYPHL 90
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVR--KVQKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAK 167
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 168 LRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-212 |
3.93e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.44 E-value: 3.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKDRNlsmv 80
Cdd:COG4152 1 MLELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 fqN--Y-----ALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:COG4152 72 --RigYlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTH--DQIEAMTmgDRIMVLNKGSI 212
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEELC--DRIVIINKGRK 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-225 |
5.60e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.91 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:COG4559 1 MLEAENLS--VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAI------VSQA 152
Cdd:COG4559 79 VLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 153 PICLM-DEPLSNLDakLRAQ---MRIeIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:COG4559 159 PRWLFlDEPTSALD--LAHQhavLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-218 |
7.29e-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: 116.94 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFG---LKVRKVQKEERQKRLMEAIEMV--GLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRLGrpnATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTH 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-218 |
8.06e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 8.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PRK13548 2 MLEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYAL-YPhLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIV------SQ 151
Cdd:PRK13548 80 VLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 152 APICLMDEPLSNLDakLRAQ---MRIeIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:PRK13548 159 PRWLLLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
8.76e-31 |
|
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: 122.47 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:TIGR02868 335 LELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPHL---SVEENILFGLKvrKVQKEErqkrLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALA 145
Cdd:TIGR02868 414 CAQD----AHLfdtTVRENLRLARP--DATDEE----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMrieIREIQQRL-GITMIYVTHD 193
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
1.45e-30 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 115.74 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKdrnLSMV 80
Cdd:PRK13539 2 MLEGEDLA-CVRG-GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA---EACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 F---QNyALYPHLSVEENILFGLKVRKvqkeERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK13539 77 YlghRN-AMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 446493527 158 DEPLSNLDAklRAQMRIEiREIQQRL--GITMIYVTH 192
Cdd:PRK13539 152 DEPTAALDA--AAVALFA-ELIRAHLaqGGIVIAATH 185
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-226 |
1.55e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.21 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 36 GPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLE------PKDRNLSMVFQNYALYPHLSVEENILFGLKvrkvqkEE 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMA------KS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 110 RQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIY 189
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 446493527 190 VTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-222 |
1.74e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.50 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKN-VSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERV-ANDLEPKDRNL 77
Cdd:PRK13642 4 ILEVENlVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgELLtAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNY-ALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTmGDRIMVLNKGSIQQVGTPLDIY 222
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-211 |
3.17e-30 |
|
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: 114.49 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETA---VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAndlepkdrnls 78
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 mvfqnY-ALYPHL---SVEENILFGlkvrkvqKEERQKRLMEAIEMVGLKEYVKMKPGQ-----------LSGGQRQRVA 143
Cdd:cd03250 70 -----YvSQEPWIqngTIRENILFG-------KPFDEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 144 LARAIVSQAPICLMDEPLSNLDAKLRAQmrieIRE--IQQRL--GITMIYVTHdQIEAMTMGDRIMVLNKGS 211
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRH----IFEncILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-207 |
6.52e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 17 TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLiinERVAndlepkDRNLSMVFQNYAL---YPhLSVE 93
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---RRAG------GARVAYVPQRSEVpdsLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 94 ENILFGL-----KVRKVQKEERqKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:NF040873 76 DLVAMGRwarrgLWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446493527 169 RAQMRIEIREIQQRlGITMIYVTHDqIEAMTMGDRIMVL 207
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-192 |
1.03e-29 |
|
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: 113.22 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 15 EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK-DRNLSMVFQNYALYPHLSVE 93
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 94 ENILFglkVRKVQKEErQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMR 173
Cdd:TIGR01189 92 ENLHF---WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
170
....*....|....*....
gi 446493527 174 IEIREIQQRLGITMIyVTH 192
Cdd:TIGR01189 168 GLLRAHLARGGIVLL-TTH 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-224 |
1.06e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.60 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKG---VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN------DLE 71
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 72 PKDRNLSMVFQnyalYPHLSV-EENIL----FGLKVRKVQKEERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALA 145
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESQLfEETVLkdvaFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-217 |
2.17e-29 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 119.05 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGlKVRKVQKEerqkRLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALARAI 148
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRA----EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGT 550
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-226 |
3.11e-29 |
|
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: 118.25 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 17 TAVKGVSVHIKKGEFFVLVGPSGCGKS----TLLRMIAGLEEISSGDLIINERVANDLEPKD------RNLSMVFQN--Y 84
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQEpmT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 85 ALYPHLSVEENILFGLKV-RKVQKEERQKRLMEAIEMVGLKE-------YvkmkPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:COG4172 104 SLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperrldaY----PHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDqieaMT----MGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
3.40e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.95 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVY---KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL----------EEISSGDLIINERVA 67
Cdd:PRK13631 21 ILRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 68 NDLEPKD--------RNLSMVFQ--NYALYPHlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKE-YVKMKPGQLSG 136
Cdd:PRK13631 101 TNPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 137 GQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|
gi 446493527 217 TPLDIYNEPA 226
Cdd:PRK13631 259 TPYEIFTDQH 268
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-233 |
3.68e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 114.80 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE-------------------TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLi 61
Cdd:COG4586 1 IIEVENLSKTYRVYEKepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 62 ineRVaNDLEP-KDR-----NLSMVF-QNYALYPHLSVEENilFGL--KVRKVQKEERQKRLMEAIEMVGLKEYVKmKP- 131
Cdd:COG4586 80 ---RV-LGYVPfKRRkefarRIGVVFgQRSQLWWDLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLD-TPv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 132 GQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHD--QIEAMTmgDRIMVLNK 209
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmdDIEALC--DRVIVIDH 230
|
250 260
....*....|....*....|....
gi 446493527 210 GSIqqvgtpldIYNEPANEFVASF 233
Cdd:COG4586 231 GRI--------IYDGSLEELKERF 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-218 |
4.27e-29 |
|
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: 112.32 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYkNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVAN-DLEPKDRNLSM 79
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDIREvTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFG-LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQ----LSGGQRQRVALARAIVSQAPI 154
Cdd:cd03253 80 VPQDTVLF-NDTIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 155 CLMDEPLSNLDAKLRaqmrieiREIQQRL-----GITMIYVTHDQIEAMTmGDRIMVLNKGSIQQVGTP 218
Cdd:cd03253 159 LLLDEATSALDTHTE-------REIQAALrdvskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTH 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
4.85e-29 |
|
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: 117.60 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE---TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLiiNERVAND------LE 71
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV--NVRVGDEwvdmtkPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 72 PKDRN-----LSMVFQNYALYPHLSVEENILFGLKVrKVQKEERQKRLMEAIEMVGL-----KEYVKMKPGQLSGGQRQR 141
Cdd:TIGR03269 357 PDGRGrakryIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 142 VALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 446493527 222 YNE 224
Cdd:TIGR03269 516 VEE 518
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
5.08e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.43 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEpkdrNLSM- 79
Cdd:COG1137 3 TLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DIT----HLPMh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 ---------------VFQNyalyphLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLkEYVKMKPG-QLSGGQRQRVA 143
Cdd:COG1137 74 krarlgigylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKAySLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 144 LARAIVSQAPICLMDEPLSNLDAklraqmrIEIREIQQ---RL---GITmIYVT-HDQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDP-------IAVADIQKiirHLkerGIG-VLITdHNVRETLGICDRAYIISEGKVLAEG 218
|
....*....
gi 446493527 217 TPLDIYNEP 225
Cdd:COG1137 219 TPEEILNNP 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-226 |
5.45e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.16 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLE--PKDRNL- 77
Cdd:PRK13644 1 MIRLENVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQN-YALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALArAIVSQAPICL 156
Cdd:PRK13644 80 GIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA-GILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 157 M-DEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:PRK13644 159 IfDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-193 |
6.96e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.79 E-value: 6.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE--TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII--------NERVANDL 70
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 71 epKDRNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVS 150
Cdd:PRK10584 86 --RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493527 151 QAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHD 193
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
1.22e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.85 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPHL---SVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKPG----------QLSGGQRQRVALAR 146
Cdd:PRK11160 419 VSQR----VHLfsaTLRDNLLLA------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-210 |
2.74e-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: 109.18 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 13 NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL--EEISSGDLIINERVANDLEPKDRnLSMVFQNYALYPHL 90
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVRkvqkeerqkrlmeaiemvglkeyvkmkpgQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRA 170
Cdd:cd03213 98 TVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493527 171 QMRIEIREIQQrLGITMIYVTHD-QIEAMTMGDRIMVLNKG 210
Cdd:cd03213 149 QVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-225 |
2.78e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.11 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 15 EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERV----ANDLEPKDRNLSMVFQN-YA-LY 87
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgQRIdtlsPGKLQALRRDIQFIFQDpYAsLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 88 PHLSVEENILFGLKVRKV-QKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLD 165
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 166 AKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
8.26e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.28 E-value: 8.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-NERVAN-DLEPKDRNLS 78
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKeNIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQN---YALYPhlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK13652 82 LVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-234 |
9.54e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.37 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 6 NVSKVYKNAEETAV-KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERV---ANDLEPKD-----RN 76
Cdd:PRK14246 12 NISRLYLYINDKAIlKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfGKDIFQIDaiklrKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLME-AIEMVGLKEYVKMK----PGQLSGGQRQRVALARAIVSQ 151
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 152 APICLMDEPLSNLDAKLRAQMRIEIREIQQRlgITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVA 231
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
...
gi 446493527 232 SFI 234
Cdd:PRK14246 250 KYV 252
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-221 |
1.12e-27 |
|
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: 113.60 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENIL-FGlkvRKVQKEE--RQKRLMEAIEMV-----GLKEYVKMKPGQLSGGQRQRVALARAIVSQ 151
Cdd:TIGR01842 397 LPQDVELFPG-TVAENIArFG---ENADPEKiiEAAKLAGVHELIlrlpdGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 152 APICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
1.90e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNyalypHLSVEenilfGLKVRKV--------------QKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVAL 144
Cdd:PRK11231 80 LLPQH-----HLTPE-----GITVRELvaygrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 145 ARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
1.96e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.79 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-------------ER 65
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 66 VANDLEPKD-------------RNLSMVFQ--NYALYPHlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKE-YVKM 129
Cdd:PRK13651 83 VLEKLVIQKtrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 130 KPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDaklrAQMRIEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMV 206
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD----PQGVKEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIF 237
|
250 260
....*....|....*....|...
gi 446493527 207 LNKGSIQQVGTPLDIYNEpaNEF 229
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD--NKF 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-213 |
4.77e-27 |
|
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: 107.03 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVY-------------------KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII 62
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 63 NERVANDLEPKD-RNLSMVF-QNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQ 140
Cdd:cd03267 81 AGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 141 RVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHD--QIEAMTmgDRIMVLNKGSIQ 213
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmkDIEALA--RRVLVIDKGRLL 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-217 |
8.53e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-RNL-- 77
Cdd:COG3845 5 ALELRGITKRFGGV--VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKVRKVQ----KEERqKRLMEAIEMVGLK----EYVkmkpGQLSGGQRQRVALARAIV 149
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGrldrKAAR-ARIRELSERYGLDvdpdAKV----EDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 150 SQAPICLMDEPLSNLD-----------AKLRAQmrieireiqqrlGITMIYVTHDQIEAMTMGDRIMVLNKGSIqqVGT 217
Cdd:COG3845 158 RGARILILDEPTAVLTpqeadelfeilRRLAAE------------GKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-234 |
9.87e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.79 E-value: 9.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEeissgDLIINERV------------AND 69
Cdd:PRK14243 11 LRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN-----DLIPGFRVegkvtfhgknlyAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 70 LEPKD--RNLSMVFQNYALYPHlSVEENILFGLKVRKVQ---KEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVAL 144
Cdd:PRK14243 84 VDPVEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 145 ARAIVSQAPICLMDEPLSNLDAKlrAQMRIE--IREIQQRLgiTMIYVTHDQIEAMTMGDRIMVLN---------KGSIQ 213
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPI--STLRIEelMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLV 238
|
250 260
....*....|....*....|.
gi 446493527 214 QVGTPLDIYNEPANEFVASFI 234
Cdd:PRK14243 239 EFDRTEKIFNSPQQQATRDYV 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-224 |
1.08e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 110.64 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR---NL 77
Cdd:PRK09700 5 YISMAGIGKSFGPV--HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFG-LKVRKV------QKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVS 150
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGrHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 151 QAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-245 |
1.23e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.38 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDL-IINERVANDLEPKDRNLSMV 80
Cdd:PRK13536 42 IDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENIL-----FGLKVRKVQKEerqkrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLvfgryFGMSTREIEAV-----IPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEpanefvasFIG 235
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE--------HIG 265
|
250
....*....|
gi 446493527 236 SPSMNINDGE 245
Cdd:PRK13536 266 CQVIEIYGGD 275
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-224 |
1.32e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN------DLEP 72
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 73 KDRNLSMVFQnyalYPHLSV-EENIL----FGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQRQRVALAR 146
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLfEETVLkdvaFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-217 |
1.36e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 110.70 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLeeIS-SGDLIINERVANDLEPKD--RNLSMVFQNYALyPHLSVEENILF 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 99 GlkvrKVQKEERQkrLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAK 167
Cdd:PRK11174 446 G----NPDASDEQ--LQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493527 168 L-RAQMRIEIREIQQRlgiTMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PRK11174 520 SeQLVMQALNAASRRQ---TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-235 |
2.22e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.81 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDL-IINERVANDLEPKDRNLSMV 80
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENIL-----FGLKVRKVqkeerQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLvfgryFGLSAAAA-----RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPldiynepaNEFVASFIG 235
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP--------HALIESEIG 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-225 |
2.62e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKG---VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDL------IINERVANDLEP 72
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 73 KDRNLSMVFQnyalYPHL-----SVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMK-PGQLSGGQRQRVALAR 146
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQMrIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-224 |
2.80e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.02 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND------LEP 72
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 73 KDRNLSMVFQnyalYPHL-----SVEENILFGLKVRKVQKEERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALAR 146
Cdd:PRK13646 83 VRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-223 |
4.21e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 104.16 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 28 KGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANdlePKDRNLSMVFQNYAL---YPhLSVEENILFGlKVRK 104
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQRHEFawdFP-ISVAHTVMSG-RTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 105 VQKEERQKR-----LMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMrIEIREI 179
Cdd:TIGR03771 80 IGWLRRPCVadfaaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446493527 180 QQRLGITMIYVTHDQIEAMTMGDRIMVLNkGSIQQVGTPLDIYN 223
Cdd:TIGR03771 159 LAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
5.41e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.62 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHLSVEENILFGL---KVRKVQKEERQKRLME-AIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRtphRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 155 CLMDEPLSNLDaklrAQMRIEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:PRK09536 161 LLLDEPTASLD----INHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-223 |
6.62e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNA---EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINE-RVANDL----EPK 73
Cdd:PRK13645 7 IILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyAIPANLkkikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 D--RNLSMVFQ--NYALYPHlSVEENILFGLKVRKVQKEERQKRLMEAIEMVGL-KEYVKMKPGQLSGGQRQRVALARAI 148
Cdd:PRK13645 87 RlrKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYN 223
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-225 |
8.73e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.46 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVA----NDLEPKDR 75
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgENIPamsrSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVRKVQKEE-RQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPlLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-217 |
1.06e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.99 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR---NLSM 79
Cdd:TIGR03410 2 EVSNLNVYY--GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMvgLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
1.28e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.96 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISS-----------GDLIINERVanDL 70
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrvegrveffNQNIYERRV--NL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 71 EPKDRNLSMVFQNYALYPhLSVEENILFGLKVRKVQKEERQKRLME-AIEMVGLKEYVKMK----PGQLSGGQRQRVALA 145
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVEsALKDADLWDEIKHKihksALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 146 RAIVSQAPICLMDEPLSNLDAKlrAQMRIE--IREIQQRLGITMIYVTHDQIEAMTMGDRIMVL--NKGSIQQV---GTP 218
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPI--ASMKVEslIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLT 240
|
250 260
....*....|....*....|.
gi 446493527 219 LDIYNEPAN----EFVASFIG 235
Cdd:PRK14258 241 KKIFNSPHDsrtrEYVLSRLG 261
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-212 |
1.81e-25 |
|
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: 102.55 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAV-KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK--DRNLS 78
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHlSVEENILFGL------KVRKVQKEERQKRLMEAIEMvGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLqscsfeCVKEAAQKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHdQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
2.56e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER----VANDLEPKDRN 76
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQ--NYALYPhLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLkEYVKMKPGQ-LSGGQRQRVALARAIVSQAP 153
Cdd:PRK13636 84 VGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-217 |
2.76e-25 |
|
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: 106.76 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERvanDLEPKDRNlsmvf 81
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA---DLSQWDRE----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 qnyALYPHL------------SVEENI-LFG-LKVRKVqkeerqkrlMEAIEMVGLKEYVKMKP-----------GQLSG 136
Cdd:COG4618 403 ---ELGRHIgylpqdvelfdgTIAENIaRFGdADPEKV---------VAAAKLAGVHEMILRLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 137 GQRQRVALARAIVSQAPICLMDEPLSNLD----AKLRAQmrieIREIQQRlGITMIYVTHDQiEAMTMGDRIMVLNKGSI 212
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDdegeAALAAA----IRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRV 544
|
....*
gi 446493527 213 QQVGT 217
Cdd:COG4618 545 QAFGP 549
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
3.10e-25 |
|
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: 100.47 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYalyPHLsveenilFGLKVRkvqkeerqkrlmeaiEMVGLkeyvkmkpgQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03247 81 NQR---PYL-------FDTTLR---------------NNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 162 SNLDAKLRAQMrieIREIQQRL-GITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVG 216
Cdd:cd03247 127 VGLDPITERQL---LSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-207 |
3.49e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PRK10247 7 LLQLQNVG--YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHlSVEENILFGLKVRKVQKEErqKRLMEAIEMVGLKEYVKMKP-GQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEaMTMGDRIMVL 207
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-217 |
6.58e-25 |
|
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: 105.98 E-value: 6.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK--DRNLSM 79
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGLKVRKVQKEERQKRLMEAIEMV-----GLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAKLAGAHDFIselpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPRI 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR01846 615 LIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGR 674
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
7.50e-25 |
|
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: 106.64 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER-VANDLEPKDRNLSMVFQ 82
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 83 NYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLS 162
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 163 NLDAKLRAQMRIEIreIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYN 223
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-193 |
7.66e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIInervandlePKDRNLSMVFQN 83
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 84 YALYPHLSVEENILFGLK-VRKVQKE---------------ERQKRLMEAIE--------------MVGLK---EYVKMK 130
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAeLRALEAEleeleaklaepdedlERLAELQEEFEalggweaearaeeiLSGLGfpeEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 131 PGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDakLRAQMRIEiREIQQRLGiTMIYVTHD 193
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LESIEWLE-EFLKNYPG-TVLVVSHD 208
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-217 |
1.04e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 105.41 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLePKDR---NLS 78
Cdd:TIGR03796 478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHlSVEENI-LFGLKVRkvqkeerQKRLMEAIEMVGLKEYVKMKPGQ-----------LSGGQRQRVALAR 146
Cdd:TIGR03796 557 MVDQDIFLFEG-TVRDNLtLWDPTIP-------DADLVRACKDAAIHDVITSRPGGydaelaegganLSGGQRQRLEIAR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 147 AIVSQAPICLMDEPLSNLDAKLRAQMRIEIReiqqRLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR03796 629 ALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-234 |
1.64e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLeeissGDLIINERVANDLEPKDRNL--- 77
Cdd:PRK14239 5 ILQVSDLS-VYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM-----NDLNPEVTITGSIVYNGHNIysp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 -----------SMVFQNYALYPhLSVEENILFGLKVRKVQKEERqkrLMEAIE--MVG------LKEYVKMKPGQLSGGQ 138
Cdd:PRK14239 78 rtdtvdlrkeiGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEksLKGasiwdeVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 139 RQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
250
....*....|....*.
gi 446493527 219 LDIYNEPANEFVASFI 234
Cdd:PRK14239 232 KQMFMNPKHKETEDYI 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-192 |
2.03e-24 |
|
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: 99.10 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 15 EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK-DRNLSMVFQNYALYPHLSVE 93
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 94 ENILFglkVRKVQKEERqkrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMR 173
Cdd:cd03231 92 ENLRF---WHADHSDEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*....
gi 446493527 174 IEIREIQQRLGItMIYVTH 192
Cdd:cd03231 166 EAMAGHCARGGM-VVLTTH 183
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-225 |
2.08e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.80 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAV-KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK--DRNLS 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHlSVEENILFGLkvRKVQKEERQKRLMEA------IEMV-GLKEYVKMKPGQLSGGQRQRVALARAIVSQ 151
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAAnahdfiMEFPnGYDTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 152 APICLMDEPLSNLDAKLRaQMRIEIREIQQRlgiTMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:TIGR00958 636 PRVLILDEATSALDAECE-QLLQESRSRASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
4.46e-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: 98.66 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYK-----NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN-DL---E 71
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvDLaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 72 PKD------RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKE-----YvkmkPGQLSGGQRQ 140
Cdd:COG4778 84 PREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErlwdlP----PATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 141 RVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDqIEAM-TMGDRIMVLNKGS 211
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
6.08e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD-RN-LSM 79
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNyalyPH-----LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:PRK13647 84 VFQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 155 CLMDEPLSNLDAKLRAqmriEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:PRK13647 160 IVLDEPMAYLDPRGQE----TLMEILDRLhnqGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-228 |
9.86e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 98.62 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKStlLRMIAGLEEISSGDLIINERVANDLEP------KDRNLSMVFQN--YALYPHL 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPvapcalRGRKIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVRKVQKEERQkrLMEAIEMVGLKE---YVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDak 167
Cdd:PRK10418 97 TMHTHARETCLALGKPADDAT--LTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 168 LRAQMRI--EIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANE 228
Cdd:PRK10418 173 VVAQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-224 |
1.71e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.66 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 5 KNVSKVYKnaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDL---EPKDRNLSMVF 81
Cdd:PRK10895 7 KNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRK----VQKEERQKRLMEAIEMVGLKEYVkmkpGQ-LSGGQRQRVALARAIVSQAPICL 156
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDdlsaEQREDRANELMEEFHIEHLRDSM----GQsLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 157 MDEPLSNLDAKlraqMRIEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:PRK10895 161 LDEPFAGVDPI----SVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-225 |
1.76e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.75 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVANDLEPKDRNLSMV--FQNYALYPHLSVEE 94
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgQHIEGLPGHQIARMGVVrtFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 95 NILFG-------------LKVRKVQKEERQK--RLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:PRK11300 100 NLLVAqhqqlktglfsglLKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-218 |
2.26e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.28 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 20 KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE---ISSGDLIINERVANDLEPKDRNlSMVFQNYALYPHLSVEENI 96
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 97 LFGLKVR---KVQKEERQKRLMEAIEMVGLKEYVKMKPGQ------LSGGQRQRVALARAIVSQAPICLMDEPLSNLDAk 167
Cdd:TIGR00955 121 MFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS- 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 168 LRAQMRIEI-REIQQRlGITMIYVTHD-QIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:TIGR00955 200 FMAYSVVQVlKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-203 |
3.71e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 95.64 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 21 GVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPkDRNLSMVF---QNyALYPHLSVEENIL 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYlghQP-GIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 98 FGLKVRKVQKEERqkrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIR 177
Cdd:PRK13538 97 FYQRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
170 180
....*....|....*....|....*.
gi 446493527 178 EIQQRLGITmIYVTHDQIEAMTMGDR 203
Cdd:PRK13538 174 QHAEQGGMV-ILTTHQDLPVASDKVR 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-236 |
8.70e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 8.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKS----TLLRMI--AGlEEISSGDLIINERVANDLEPKDR-----------NLSMV 80
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAG-GLVQCDKMLLRRRSRQVIELSEQsaaqmrhvrgaDMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQN--YALYPHLSVEENILFGLKVRK-VQKEE---RQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQgASREEamvEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 155 CLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFI 234
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALL 269
|
..
gi 446493527 235 GS 236
Cdd:PRK10261 270 AA 271
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-245 |
9.10e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.32 E-value: 9.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 14 AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL-EEIS----SGDLIINERVA---NDLEPKDRNLSMVFQNYA 85
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIfnyRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 86 LYPhLSVEENILFGLKVRKV--QKEER---QKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:PRK14271 112 PFP-MSIMDNVLAGVRAHKLvpRKEFRgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSPSMN 240
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGD 268
|
....*
gi 446493527 241 INDGE 245
Cdd:PRK14271 269 VKDAK 273
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-192 |
9.67e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.50 E-value: 9.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIInervandlePKDRNLSMV 80
Cdd:COG4178 362 ALALEDLT-LRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNyalyPHL---SVEENILFGLKVRKVQKEErqkrLMEAIEMVGLKEYVKM------KPGQLSGGQRQRVALARAIVSQ 151
Cdd:COG4178 432 PQR----PYLplgTLREALLYPATAEAFSDAE----LREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446493527 152 APICLMDEPLSNLDAKLRAQMrieIREIQQRL-GITMIYVTH 192
Cdd:COG4178 504 PDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-212 |
1.11e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.97 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---L 77
Cdd:PRK15439 11 LLCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGLKvrkvQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQrLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-253 |
1.23e-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: 99.11 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEI--SSGDLIIN-------------ERV 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 67 A-------NDLEPKD----------------RNLSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGL 123
Cdd:TIGR03269 79 GepcpvcgGTLEPEEvdfwnlsdklrrrirkRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 124 KEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTH--DQIEAMTmg 201
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIEDLS-- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446493527 202 DRIMVLNKGSIQQVGTPLdiynepanEFVASFIGSPSMNINDGEVDKEKGVL 253
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPD--------EVVAVFMEGVSEVEKECEVEVGEPII 280
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-212 |
1.46e-22 |
|
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: 94.65 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 12 KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE---ISSGDLIINERVANDLEPKDRnLSMVFQNYALYP 88
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 89 HLSVEENILFGLKVR---KVQKEERQKRLME------AIEMVGlKEYVKmkpgQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:cd03234 95 GLTVRETLTYTAILRlprKSSDAIRKKRVEDvllrdlALTRIG-GNLVK----GISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-225 |
2.77e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 12 KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE----ISSGDLIINERVANDLEPKDR------NLSMVF 81
Cdd:PRK11022 16 ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QN--YALYPHLSVEENILFGLKVRKV-QKEERQKRLMEAIEMVGLKE---YVKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK11022 96 QDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEP 225
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-217 |
4.36e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.72 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:PRK13657 335 VEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFGlkvRKVQKEERqkrLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALARAI 148
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVG---RPDATDEE---MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-222 |
5.24e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.92 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 11 YKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN----DLEPKDRNLSMVFQNyal 86
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 87 yP-----HLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYvKMKPGQ-LSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:PRK13638 86 -PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIY 222
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-226 |
9.56e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 17 TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL---EEISSGDLIINERVANDLEPKDRN------LSMVFQN--YA 85
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKELNklraeqISMIFQDpmTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 86 LYPHLSVEENILFGL----KVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:PRK09473 110 LNPYMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPA 226
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-217 |
1.16e-21 |
|
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: 92.16 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINervANDLEPKD-----RN 76
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVD---GHDLALADpawlrRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYpHLSVEENILFGLKVRKVQKEERQKRLMEAIEMV-----GLKEYVKMKPGQLSGGQRQRVALARAIVSQ 151
Cdd:cd03252 78 VGVVLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 152 APICLMDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-165 |
1.60e-21 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 91.45 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 25 HIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEpKDRNLSMVFQNYALYPHLSVEENILF--GLKV 102
Cdd:PRK13543 33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLENLHFlcGLHG 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 103 RKVQKEERQkrlmeAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLD 165
Cdd:PRK13543 112 RRAKQMPGS-----ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-213 |
2.45e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERV-----ANDLEpkdr 75
Cdd:COG0488 315 VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVkigyfDQHQE---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 nlsmvfqnyALYPHLSVEENIlfglkvRKVQKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVALARAIVSQAPI 154
Cdd:COG0488 389 ---------ELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 155 CLMDEPLSNLDaklraqmrIEIREI-QQRL----GiTMIYVTHDQ--IEAMTmgDRIMVLNKGSIQ 213
Cdd:COG0488 454 LLLDEPTNHLD--------IETLEAlEEALddfpG-TVLLVSHDRyfLDRVA--TRILEFEDGGVR 508
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-217 |
3.92e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.70 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND--LEPKDRNLSM 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFGLKVRKVQKE-ERQKRLMEAIEMVGlkeyvKMKPG----------QLSGGQRQRVALARAI 148
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYARTEQYSREQiEEAARMAYAMDFIN-----KMDNGldtvigengvLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGT 561
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-218 |
4.14e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.81 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 17 TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGD--LIINERVANDLEPKDRNLSMVfQNYALYPHLSVEE 94
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFGQPVDAGDIATRRRVGYMS-QAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 95 NI-----LFGLKvrkvqKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLR 169
Cdd:NF033858 359 NLelharLFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493527 170 AQM-RIEIrEIQQRLGITmIYV-THDQIEAMTMgDRIMVLNKGSIQQVGTP 218
Cdd:NF033858 434 DMFwRLLI-ELSREDGVT-IFIsTHFMNEAERC-DRISLMHAGRVLASDTP 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
5.94e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.70 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDlepkdrNLSMV 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFG-------LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIqQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-217 |
1.08e-20 |
|
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: 93.86 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAndlepkdrnlsMVF 81
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA-----------YVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNyALYPHLSVEENILFGlkvrKVQKEERQKRLMEA------IEMV--GLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:TIGR00957 706 QQ-AWIQNDSLRENILFG----KALNEKYYQQVLEAcallpdLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRL-GITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGS 844
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
2.27e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.78 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD---RNL 77
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENI-LFGLKVRKVQKEERQKRLMEAIEMvgLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLaMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-193 |
2.44e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANdlEPKDRNL-SMV 80
Cdd:PRK15056 7 IVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKNLvAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYAL---YPHLsVEENILFG----LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:PRK15056 84 PQSEEVdwsFPVL-VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHD 193
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-225 |
2.47e-20 |
|
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: 89.12 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDL------EPKD 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlsEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 RNLSMVFQNYalyphlsVEENILFGLKVRKVQKEERQKRLMEaiemVGLKEYVKM--------------------KPGQL 134
Cdd:TIGR02323 81 RRLMRTEWGF-------VHQNPRDGLRMRVSAGANIGERLMA----IGARHYGNIrataqdwleeveidptriddLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 135 SGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQ 214
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250
....*....|.
gi 446493527 215 VGTPLDIYNEP 225
Cdd:TIGR02323 230 SGLTDQVLDDP 240
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-234 |
3.00e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.11 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLepkDRNLSMVFQNY-ALYPHL---SVEENIL 97
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsgSILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 98 FGLKvRKVQKEErqkrLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDA 166
Cdd:TIGR01193 570 LGAK-ENVSQDE----IWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 167 KLRAQMRIEIREIQQRlgiTMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEpaNEFVASFI 234
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-228 |
3.72e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK--DRNLSMVF 81
Cdd:PRK10575 14 LRNVS--FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGL-----KVRKVQKEERQKrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALArAIVSQAPIC- 155
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIGRypwhgALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIA-MLVAQDSRCl 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANE 228
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-212 |
3.92e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.72 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR-NLSMVF-----QNYALYPHLS 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENILFGLkvrkvqkeerqkrlmeaiemvglkeyvkmkpgQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQ 171
Cdd:cd03215 95 VAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493527 172 MRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:cd03215 143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-243 |
4.23e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 17 TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSMVFQNYALYPHLSVEE 94
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 95 NILFG------LKVRkvQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:PRK10253 101 LVARGryphqpLFTR--WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 169 RAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEpanEFVASFIGSPSMNIND 243
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA---ELIERIYGLRCMIIDD 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-243 |
6.80e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINE---RVANDLEPKDRNLSM 79
Cdd:PRK11288 6 SFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemRFASTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLSVEENILFG-LKVRK--VQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:PRK11288 84 IYQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 157 MDEPLSNLDAKLRAQ-MRIeIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGsiQQVGTPLDIYNEPANEFVASFIG 235
Cdd:PRK11288 164 FDEPTSSLSAREIEQlFRV-IRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG--RYVATFDDMAQVDRDQLVQAMVG 239
|
....*...
gi 446493527 236 SpsmNIND 243
Cdd:PRK11288 240 R---EIGD 244
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
2-217 |
8.79e-20 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 90.72 E-value: 8.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEEtAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:TIGR01192 335 VEFRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESlrKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALARAI 148
Cdd:TIGR01192 414 VFQDAGLFNR-SIRENIRLG------REGATDEEVYEAAKAAAAHDFILKRSngydtlvgergNRLSGGERQRLAIARAI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLgiTMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDALRKNR--TTFIIAH-RLSTVRNADLVLFLDQGRLIEKGS 552
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-210 |
1.45e-19 |
|
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: 84.04 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandlepkdrnlsmvf 81
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 qNYALYPhlsveenilfglkvrkvqkeerqkrlmeaiemvglkeyvkmkpgQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:cd03221 64 -KIGYFE--------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493527 162 SNLDAKLRAQMRIEIREIQQrlgiTMIYVTHDQ--IEAMTmgDRIMVLNKG 210
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG----TVILVSHDRyfLDQVA--TKIIELEDG 143
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-210 |
2.28e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE--TAVKGVSVHIKKGEFFVLVGPSGCGKS----TLLRMI-AGLEEISSGDLIIN-ERVANDLEP 72
Cdd:PRK15134 5 LLAIENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHgESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 73 KDR-----NLSMVFQN--YALYPHLSVEENILFGLKV-RKVQKEERQKRLMEAIEMVGLKEYVKMK---PGQLSGGQRQR 141
Cdd:PRK15134 85 TLRgvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 142 VALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-192 |
5.26e-19 |
|
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: 82.97 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSkVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIInervandlePKDRNLSMVF 81
Cdd:cd03223 1 IELENLS-LATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNyalyPHLSveenilfglkvrkvqkeerQKRLMEAI----EMVglkeyvkmkpgqLSGGQRQRVALARAIVSQAPICLM 157
Cdd:cd03223 71 QR----PYLP-------------------LGTLREQLiypwDDV------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 446493527 158 DEPLSNLDAKLRAQMrieiREIQQRLGITMIYVTH 192
Cdd:cd03223 116 DEATSALDEESEDRL----YQLLKELGITVISVGH 146
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
5.53e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.36 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 5 KNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINER--VANDL----EPKDRNLS 78
Cdd:PRK11701 10 RGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLyalsEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 -----MVFQNYA--LYPHLSVEENIlfglkvrkvqkeerQKRLMEaiemVGLKEYVKMK--------------------P 131
Cdd:PRK11701 88 rtewgFVHQHPRdgLRMQVSAGGNI--------------GERLMA----VGARHYGDIRatagdwlerveidaariddlP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 132 GQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGS 211
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
....*
gi 446493527 212 IQQVG 216
Cdd:PRK11701 230 VVESG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-188 |
2.32e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.31 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-NERVANDLEPKDRNLSMVFQNYALYPHLSVEENILFGL 100
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 101 KVRKVQKEerqkrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQ 180
Cdd:PRK13540 100 HFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHR 174
|
....*...
gi 446493527 181 QRLGITMI 188
Cdd:PRK13540 175 AKGGAVLL 182
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-217 |
2.36e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.30 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 11 YKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSMVFQNYALYP 88
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 89 HlSVEENILFGLKVRKVQKEERQKRLMEAIEMV-----GLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSN 163
Cdd:PRK10789 403 D-TVANNIALGRPDATQQEIEHVARLASVHDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 164 LDAKLRAQMRIEIReiQQRLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PRK10789 482 VDGRTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGN 532
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-255 |
2.44e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.47 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 15 EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISS--GDLIINERVANdlEPKDRNLSMVFQNYALYPHLSV 92
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 93 EENILFGLKVRKVQKEERQKRLMEA---IEMVGLKEYVKMKPGQ-----LSGGQRQRVALARAIVSQAPICLMDEPLSNL 164
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAesvISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 165 DAKLRAQMRIEIREIQQRlGITMIYVTHD-QIEAMTMGDRIMVLNKGSIQQVGTPLDIYnepaneFVASFIG-SPS--MN 240
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSDAM------AYFESVGfSPSfpMN 310
|
250
....*....|....*
gi 446493527 241 INDGEVDKEKGVLHI 255
Cdd:PLN03211 311 PADFLLDLANGVCQT 325
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-214 |
3.12e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-NERV-ANDLEPKDRNLSM 79
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVtAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHLsveenilfglkvRKVQKEERQKRLMEA-IEMVGLKEYVKMKPG-----QLSGGQRQRVALARAIVSQAP 153
Cdd:PRK10522 402 VFTDFHLFDQL------------LGPEGKPANPALVEKwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 154 ICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQiEAMTMGDRIMVLNKGSIQQ 214
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSE 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-217 |
4.10e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISS--GDLIINE---RVANDLEPKDR 75
Cdd:PRK13549 5 LLEMKNITKTFGGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGeelQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFGLKVRK---VQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQA 152
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGsiQQVGT 217
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG--RHIGT 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-217 |
4.63e-18 |
|
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: 85.26 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISS--GDLIINE---RVANDLEPKDR 75
Cdd:TIGR02633 1 LLEMKGIVKTFGGV--KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGsplKASNIRDTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHLSVEENILFG----LKVRKVQKEERQKRLMEAIEMVGLKEYVKMKP-GQLSGGQRQRVALARAIVS 150
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 151 QAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGsiQQVGT 217
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-217 |
5.67e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 85.26 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYkNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG5265 358 VRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYpHLSVEENILFGlkvrkvQKEERQKRLMEAIEMVGLKEYVKMKPGQ-----------LSGGQRQRVALARAI 148
Cdd:COG5265 437 VPQDTVLF-NDTIAYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 149 VSQAPICLMDEPLSNLDaklraqMRIEiREIQQRL-----GITMIYVTH---DQIEAmtmgDRIMVLNKGSIQQVGT 217
Cdd:COG5265 510 LKNPPILIFDEATSALD------SRTE-RAIQAALrevarGRTTLVIAHrlsTIVDA----DEILVLEAGRIVERGT 575
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-250 |
7.42e-18 |
|
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: 82.07 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 26 IKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-NERVA---NDLEPK-----DRNLSMVFQNYALYPHLSVEenI 96
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSykpQYIKADyegtvRDLLSSITKDFYTHPYFKTE--I 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 97 LFGLKVRKVQkeERQKRlmeaiemvglkeyvkmkpgQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEI 176
Cdd:cd03237 100 AKPLQIEQIL--DREVP-------------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 177 REIQQRLGITMIYVTHDQIEAMTMGDRIMVLN-KGSIQQVGTPLDIYNEPANEFVASF---------IGSPSMNINDGEV 246
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRLIVFEgEPSVNGVANPPQSLRSGMNRFLKNLditfrrdpeTGRPRINKLGSVK 238
|
....
gi 446493527 247 DKEK 250
Cdd:cd03237 239 DREQ 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-217 |
1.44e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.40 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 14 AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLR-MIAGLEEISSGDLIINERVAndLEPKdrnLSMVFqnyalypHLSV 92
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVA--YVPQ---VSWIF-------NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 93 EENILFGLkvrkvqkEERQKRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:PLN03130 696 RDNILFGS-------PFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 162 SNLDAKLRAQM--RIEIREIQQRlgiTMIYVThDQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PLN03130 769 SALDAHVGRQVfdKCIKDELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-249 |
4.59e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.90 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIinervandlepKDRNLSMVFQNyALYPHLSVEENILFGlk 101
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFF-- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 102 vrkvqKEERQKRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRA 170
Cdd:PTZ00243 745 -----DEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 171 QMRIEIreIQQRL-GITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPANEFVASfIGSPSMNINDGEVDKE 249
Cdd:PTZ00243 820 RVVEEC--FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAA-ELKENKDSKEGDADAE 895
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-218 |
6.55e-17 |
|
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: 78.22 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-NERVAN-DLEPKDRNLSM 79
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQnyalyphlsveENILFGLKVRK---VQKEERQKRLMEAIEmvglkeyVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:cd03369 87 IPQ-----------DPTLFSGTIRSnldPFDEYSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 157 MDEPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT--NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-233 |
1.32e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSmv 80
Cdd:PRK09544 4 LVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 fqnyALYPhLSVEENILFGLKVRKvqkeerqKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP 160
Cdd:PRK09544 80 ----TTLP-LTVNRFLRLRPGTKK-------EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 161 LSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNkGSIQQVGTPLDIYNEPanEFVASF 233
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-225 |
1.34e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVskvyknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEiSSGDLIINERVANDLEPKDRNL---- 77
Cdd:PRK03695 1 MQLNDV------AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARhray 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 ---------SM-VFQNYALYPHlsveenilfglkvRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALA-- 145
Cdd:PRK03695 74 lsqqqtppfAMpVFQYLTLHQP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAav 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 146 -----RAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQrLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLD 220
Cdd:PRK03695 141 vlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
....*
gi 446493527 221 IYNEP 225
Cdd:PRK03695 220 VLTPE 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-211 |
1.66e-16 |
|
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: 77.37 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVFQ-NYALY-PHL---SVEENI 96
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAAQkPWLlnaTVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 97 LFGLKVRKvqkeERQKRLMEAIEM--------VGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:cd03290 100 TFGSPFNK----QRYKAVTDACSLqpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446493527 169 RAQ-MRIEIREIQQRLGITMIYVTHdQIEAMTMGDRIMVLNKGS 211
Cdd:cd03290 176 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDGS 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-212 |
2.68e-16 |
|
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: 76.41 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLE--EISSGDLIINERVANDLEPKDR---N 76
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQnyalYPhlsveenilfglkvrkvqkeerqkrlmEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICL 156
Cdd:cd03217 79 IFLAFQ----YP---------------------------PEIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 157 MDEPLSNLDAKlraQMRIEIREIQQ--RLGITMIYVTH-----DQIEAmtmgDRIMVLNKGSI 212
Cdd:cd03217 128 LDEPDSGLDID---ALRLVAEVINKlrEEGKSVLIITHyqrllDYIKP----DRVHVLYDGRI 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-170 |
2.80e-16 |
|
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: 79.98 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandlepkdrNLSMVF 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNY-ALYPHLSVEENILFGLKVRKVQKEERQKRlmeaiemvglkEYV----------KMKPGQLSGGQRQRVALARAIVS 150
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGLDIIKLGKREIPSR-----------AYVgrfnfkgsdqQKKVGQLSGGERNRVHLAKTLKS 460
|
170 180
....*....|....*....|.
gi 446493527 151 QAPICLMDEPLSNLDAK-LRA 170
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVEtLRA 481
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-221 |
2.80e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVskvyknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEiSSGDLIINERVANDLEPKD--RNLSM 79
Cdd:COG4138 1 LQLNDV------AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 ------------VFQNYALYPHLSVEEnilfglkvrkvqkEERQKRLMEAIEMVGLKEYVkMKP-GQLSGGQRQRVALAR 146
Cdd:COG4138 74 lsqqqsppfampVFQYLALHQPAGASS-------------EAVEQLLAQLAEALGLEDKL-SRPlTQLSGGEWQRVRLAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 147 AIV-------SQAPICLMDEPLSNLD-AKLRAQMRIeIREIQQrLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:COG4138 140 VLLqvwptinPEGQLLLLDEPMNSLDvAQQAALDRL-LRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGET 217
|
...
gi 446493527 219 LDI 221
Cdd:COG4138 218 AEV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-212 |
4.09e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKvyknaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR-NLSMVF 81
Cdd:COG1129 258 EVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 -----QNYALYPHLSVEENILFGL--KVRK---VQKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVALARAIVS 150
Cdd:COG1129 332 vpedrKGEGLVLDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 151 QAPICLMDEPLSNLD--AKLraqmriEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:COG1129 412 DPKVLILDEPTRGIDvgAKA------EIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-193 |
5.89e-16 |
|
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: 79.07 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEET---AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandLEPKD---- 74
Cdd:COG4615 328 LELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNreay 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 75 RNL-SMVFQNYALYPHlsveeniLFGLkvrkvQKEERQKRLMEAIEMVGLKEYVKMKPG-----QLSGGQRQRVALARAI 148
Cdd:COG4615 405 RQLfSAVFSDFHLFDR-------LLGL-----DGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVAL 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRaqmRIEIREIQQRL---GITMIYVTHD 193
Cdd:COG4615 473 LEDRPILVFDEWAADQDPEFR---RVFYTELLPELkarGKTVIAISHD 517
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-217 |
6.63e-16 |
|
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: 77.20 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandlepkdrnlSMVFQNYALYPHlSVEENILF 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-----------SFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 99 GLKVRKVQKEERQK--RLMEAIEMVGLKEYVKMKPG--QLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMrI 174
Cdd:cd03291 121 GVSYDEYRYKSVVKacQLEEDITKFPEKDNTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI-F 199
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493527 175 EIREIQQRLGITMIYVThDQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:cd03291 200 ESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGT 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-215 |
9.04e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.38 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 15 EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIInervandlepkdrnlsmVFQNYALYPHLSVEE 94
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 95 NIlfGLKVRKVQKeerqkrlMEAIEMVGLKEYVKM--KPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQM 172
Cdd:COG2401 105 AI--GRKGDFKDA-------VELLNAVGLSDAVLWlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446493527 173 RIEIREIQQRLGITMIYVT-HDQIEAMTMGDRIMVLNKGSIQQV 215
Cdd:COG2401 176 ARNLQKLARRAGITLVVAThHYDVIDDLQPDLLIFVGYGGVPEE 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-280 |
9.69e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.25 E-value: 9.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGleeissgdlIINE--RVAND-----------LEPKDR------NLS 78
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---------ITKDnwHVTADrfrwngidllkLSPRERrkiigrEIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQN--YALYPHLSVEENILFGLKVRKVQ------KEERQKRLMEAIEMVGLKEYVK-MK--PGQLSGGQRQRVALARA 147
Cdd:COG4170 93 MIFQEpsSCLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIKDHKDiMNsyPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQmrieIREIQQRL----GITMIYVTHDqIEAMT-MGDRIMVLNKGSIQQVGTPLDIY 222
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQ----IFRLLARLnqlqGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQIL 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 223 NEPANEFVASFIGS-PSMNindgevdkeKGVLHIGKLQ-IPLSIGQLKQLPEGiIRIGMR 280
Cdd:COG4170 248 KSPHHPYTKALLRSmPDFR---------QPLPHKSRLNtLPGSIPPLQHLPIG-CRLGPR 297
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-280 |
1.06e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.15 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEE--TAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLeeisSGDliiNERVAND--------- 69
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV----TKD---NWRVTADrmrfddidl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 70 --LEPKDR------NLSMVFQ--NYALYPHLSVEENILFGL-----KVRKVQK-EERQKRLMEAIEMVGLKEYVKMK--- 130
Cdd:PRK15093 76 lrLSPRERrklvghNVSMIFQepQSCLDPSERVGRQLMQNIpgwtyKGRWWQRfGWRKRRAIELLHRVGIKDHKDAMrsf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 131 PGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 211 SIQQVGTPLDIYNEPANEFVASFIGS-PsmnindgevDKEKGVLHIGKLQ-IPLSIGQLKQLPEGiIRIGMR 280
Cdd:PRK15093 236 QTVETAPSKELVTTPHHPYTQALIRAiP---------DFGSAMPHKSRLNtLPGAIPLLEHLPIG-CRLGPR 297
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-217 |
1.37e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 15 EETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLR-MIAGLEEISSGDLIINERVAndLEPKdrnLSMVFqnyalypHLSVE 93
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVA--YVPQ---VSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 94 ENILFGLKVRKvqkeerqKRLMEAIEMVGLKEYVKMKPGQ-----------LSGGQRQRVALARAIVSQAPICLMDEPLS 162
Cdd:PLN03232 697 ENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 163 NLDAKLRAQ-----MRIEIReiqqrlGITMIYVThDQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PLN03232 770 ALDAHVAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-218 |
5.79e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.56 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 20 KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLE--EISSGDLIINERVANDLEPKDR---NLSMVFQnyalYP------ 88
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQ----YPveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 89 ------HLSVEENILFGLKVRKVQKEerqkrLMEAIEMVGLKE-----YVKMKpgqLSGGQRQRVALARAIVSQAPICLM 157
Cdd:COG0396 93 svsnflRTALNARRGEELSAREFLKL-----LKEKMKELGLDEdfldrYVNEG---FSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 158 DEPLSNLDAklrAQMRIEIREIQQRL--GITMIYVTH-----DQIEAmtmgDRIMVLNKGSIQQVGTP 218
Cdd:COG0396 165 DETDSGLDI---DALRIVAEGVNKLRspDRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGK 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-217 |
5.90e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNaEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPK--DRNLSM 79
Cdd:PRK10790 341 IDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGlkvRKVQKEerqkRLMEAIEMVGLKEYVKMKPG-----------QLSGGQRQRVALARAI 148
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG---RDISEE----QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlgITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-240 |
9.82e-15 |
|
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: 75.72 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandlepkdrnlSMVFQNYALYPHlSVEENILF 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-----------SFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 99 GLKVRKVQKEERQK--RLMEAIEMVGLKEYVKMKPG--QLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAklraqmrI 174
Cdd:TIGR01271 510 GLSYDEYRYTSVIKacQLEEDIALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV-------V 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 175 EIREIQQR------LGITMIYVThDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPAnEFVASFIGSPSMN 240
Cdd:TIGR01271 583 TEKEIFESclcklmSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP-DFSSLLLGLEAFD 652
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-221 |
4.02e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAeeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDL------IINERVANDLEPK-- 73
Cdd:NF033858 2 ARLEGVSHRYGKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdMADARHRRAVCPRia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 ------DRNlsmvfqnyaLYPHLSVEENI-----LFGLKvrkvqKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRV 142
Cdd:NF033858 80 ympqglGKN---------LYPTLSVFENLdffgrLFGQD-----AAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 143 ALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREI-QQRLGITMIYVTHDQIEAMTMgDRIMVLNKGSIQQVGTPLDI 221
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
4.71e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYknAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVandlepkdrNLSMVF 81
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNY-ALYPHLSVEENILFGLKVRKVQKEERQKRlmeaiemvglkEYV----------KMKPGQLSGGQRQRVALARAIVS 150
Cdd:PRK11819 394 QSRdALDPNKTVWEEISGGLDIIKVGNREIPSR-----------AYVgrfnfkggdqQKKVGVLSGGERNRLHLAKTLKQ 462
|
170 180
....*....|....*....|.
gi 446493527 151 QAPICLMDEPLSNLDAK-LRA 170
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVEtLRA 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
9.98e-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: 72.28 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYKNAEETaVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINErvandlepkDRNLSMVFQN 83
Cdd:TIGR03719 7 MNRVSKVVPPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP---------GIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 84 YALYPHLSVEENILFGL-KVRKVQKE-------------------ERQKRLMEAIEMVGL----------KEYVKMKPG- 132
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVaEIKDALDRfneisakyaepdadfdklaAEQAELQEIIDAADAwdldsqleiaMDALRCPPWd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 133 ----QLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRieiREIQQRLGiTMIYVTHD 193
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPG-TVVAVTHD 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-234 |
1.63e-13 |
|
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: 69.55 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN--ERVANDLEPKDRNLSM 79
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgiDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQnyalyphlsveENILFGLKVRKVQKEERQ---KRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVALA 145
Cdd:cd03288 100 ILQ-----------DPILFSGSIRFNLDPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 146 RAIVSQAPICLMDEPLSNLD-AKLRAQMRIEIREIQQRLGITMIYVTHDQIEAmtmgDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDmATENILQKVVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLLAQ 244
|
250
....*....|
gi 446493527 225 PANEFvASFI 234
Cdd:cd03288 245 EDGVF-ASLV 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-228 |
2.20e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAV-KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINErvANDLepKDRNLS-- 78
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND--SHNL--KDINLKww 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 -----MVFQNYALYPHlSVEENI---LFGLK------------------------------------------------V 102
Cdd:PTZ00265 459 rskigVVSQDPLLFSN-SIKNNIkysLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnelieM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 103 RKVQKEERQKRLMEAIEMVGLKEYVKMKP-----------GQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQ 171
Cdd:PTZ00265 538 RKNYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 172 MRIEIREIQQRLGITMIYVTHdQIEAMTMGDRIMVLN---KGSIQQVGTPLDIYNEPANE 228
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAH-RLSTIRYANTIFVLSnreRGSTVDVDIIGEDPTKDNKE 676
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-217 |
2.26e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 56 SSGDLIINERVANDLEPKD-RNL-SMVFQNYALYpHLSVEENILFGlkvRKVQKEERQKRlmeAIEMVGLKEYVKMKPGQ 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG---KEDATREDVKR---ACKFAAIDEFIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 134 -----------LSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHdQIEAMTMGD 202
Cdd:PTZ00265 1348 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1426
|
170 180
....*....|....*....|
gi 446493527 203 RIMVLNK----GS-IQQVGT 217
Cdd:PTZ00265 1427 KIVVFNNpdrtGSfVQAHGT 1446
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-212 |
3.52e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSkVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSMVF- 81
Cdd:COG3845 259 EVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAy 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 -----QNYALYPHLSVEENILFG------------LKVRKVqkEERQKRLMEA--IEMVGLKEYVKMkpgqLSGGQRQRV 142
Cdd:COG3845 338 ipedrLGRGLVPDMSVAENLILGryrrppfsrggfLDRKAI--RAFAEELIEEfdVRTPGPDTPARS----LSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 143 ALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-241 |
5.62e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 68.16 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 27 KKGEFFVLVGPSGCGKSTLLRMIAG--------LEEISSGDLIINERVANDLEP-----KDRNLSMVF--QNYALYPHlS 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNyftklLEGDVKVIVkpQYVDLIPK-A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENILFGLKvrkvQKEERQKrLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQ 171
Cdd:cd03236 103 VKGKVGELLK----KKDERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493527 172 MRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVL-NKGSIQQVGTPLDIYNEPANEFVASFIGSPSMNI 241
Cdd:cd03236 178 AARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLyGEPGAYGVVTLPKSVREGINEFLDGYLPTENMRF 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-210 |
6.28e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAN---DLEPKDRNLSMV 80
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 81 FQNYALYPHLSVEENILFGLKVRK--VQKEERQKRLMEAI-EMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLM 157
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKgmFVDQDKMYRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 158 DEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-221 |
9.27e-13 |
|
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: 69.59 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINE-RVA----NDLEPKdrn 76
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAkiglHDLRFK--- 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNYALYPHlSVEENI-LFGlkvrKVQKEErqkrLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVAL 144
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-SLRMNLdPFS----QYSDEE----VWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCL 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 145 ARAIVSQAPICLMDEPLSNLD--------AKLRAQMR-IEIREIQQRLGITMIYVthdqieamtmgdRIMVLNKGSIQQV 215
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDletdnliqSTIRTQFEdCTVLTIAHRLNTIMDYT------------RVIVLDKGEVAEF 1500
|
....*.
gi 446493527 216 GTPLDI 221
Cdd:TIGR00957 1501 GAPSNL 1506
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-229 |
1.05e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLS 78
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 79 MVFQNYALYPHlSVEENIlfglkvrKVQKEERQKRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVALARA 147
Cdd:PLN03232 1314 IIPQSPVLFSG-TVRFNI-------DPFSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARA 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQMRIEIREiqQRLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNEPAN 227
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
..
gi 446493527 228 EF 229
Cdd:PLN03232 1463 AF 1464
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-215 |
1.19e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGleeissgDLIINERVANDL-----------EPKDRNLSMVFQNYALY 87
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-------RTEGNVSVEGDIhyngipykefaEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 88 PHLSVEENILFGLKVRKvqkeerqkrlmeaiemvglKEYVKmkpgQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAK 167
Cdd:cd03233 96 PTLTVRETLDFALRCKG-------------------NEFVR----GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493527 168 LRAQMRIEIREIQQRLGIT-MIYVTHDQIEAMTMGDRIMVLNKGsiQQV 215
Cdd:cd03233 153 TALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEG--RQI 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-229 |
1.62e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLL----RMIagleEISSGDLIINER--VANDLEPKDR 75
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGReiGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 NLSMVFQNYALYPHlSVEENILFGLkvrkvqkEERQKRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVAL 144
Cdd:PTZ00243 1385 QFSMIPQDPVLFDG-TVRQNVDPFL-------EASSAEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 145 ARAIVSQ-APICLMDEPLSNLDAKLRaqmrieiREIQQRL-----GITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:PTZ00243 1457 ARALLKKgSGFILMDEATANIDPALD-------RQIQATVmsafsAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSP 1528
|
250
....*....|.
gi 446493527 219 LDIYNEPANEF 229
Cdd:PTZ00243 1529 RELVMNRQSIF 1539
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-210 |
2.21e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRN---L 77
Cdd:PRK10762 4 LLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQNYALYPHLSVEENILFGL-KVRKVQKEERQKRLMEA---IEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP 153
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGReFVNRFGRIDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493527 154 ICLMDEPLSNL-DAKLRAQMRIeIREIQ-QRLGItmIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK10762 162 VIIMDEPTDALtDTETESLFRV-IRELKsQGRGI--VYISHRLKEIFEICDDVTVFRDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-218 |
2.49e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RNLSM 79
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYphlsvEENILFGLKVRKvqkEERQKRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVALARAI 148
Cdd:PLN03130 1318 IPQAPVLF-----SGTVRFNLDPFN---EHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 149 VSQAPICLMDEPLSNLDAKLRAQMRIEIREiqQRLGITMIYVTHdQIEAMTMGDRIMVLNKGSIQQVGTP 218
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTP 1456
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-206 |
3.63e-12 |
|
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: 67.50 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 26 IKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVA---NDLEPK-----DRNLSMVfqNYALYPHLSVEENIL 97
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISykpQYISPDydgtvEEFLRSA--NTDDFGSSYYKTEII 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 98 FGLKVrkvqkeerqKRLMEaiemvglkEYVKmkpgQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIR 177
Cdd:COG1245 441 KPLGL---------EKLLD--------KNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|
gi 446493527 178 EIQQRLGITMIYVTHDqIEAMTM-GDRIMV 206
Cdd:COG1245 500 RFAENRGKTAMVVDHD-IYLIDYiSDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-206 |
5.49e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEETAVKGvsvHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVA---NDLEPK---- 73
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykpQYIKPDydgt 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 -DRNLSMVFQNYALYPHlsvEENILFGLKVrkvqkeerqKRLMEaiemvglkEYVKmkpgQLSGGQRQRVALARAIVSQA 152
Cdd:PRK13409 417 vEDLLRSITDDLGSSYY---KSEIIKPLQL---------ERLLD--------KNVK----DLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 153 PICLMDEPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMV 206
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-237 |
1.43e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.02 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEeisSGDLIINERVANDLEPKDRNLSMVF----QNYALYPHLSVEE 94
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFPKKQETFARISgyceQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 95 NILFGLKVR---KVQKEERQK---RLMEAIEMVGLKEYVKMKPG--QLSGGQRQRVALARAIVSQAPICLMDEPLSNLDA 166
Cdd:PLN03140 973 SLIYSAFLRlpkEVSKEEKMMfvdEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 167 KLRAqmrIEIREIQQRL--GITMIYVTH----DQIEAMtmgDRIMVLNKGSIQQVGTPLDIYNEPANEFVASFIGSP 237
Cdd:PLN03140 1053 RAAA---IVMRTVRNTVdtGRTVVCTIHqpsiDIFEAF---DELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVP 1123
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-233 |
1.92e-11 |
|
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: 62.20 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 26 IKKGEFFVLVGPSGCGKSTLLRMIAGleeissgdliinervanDLEPKDRNLSMVFQNYALYPhlsveenilfglkvrkv 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG-----------------QLIPNGDNDEWDGITPVYKP----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 106 qkeerqkrlmeaiemvglkEYVKmkpgqLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGI 185
Cdd:cd03222 68 -------------------QYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493527 186 TMIYVTHDQIEAMTMGDRIMVL-NKGSIQQVGTPLDIYNEPANEFVASF 233
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFeGEPGVYGIASQPKGTREGINRFLRGY 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-210 |
2.27e-11 |
|
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: 62.26 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 20 KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEIS--SGDLIINERvandlePKDRNLS----MVFQNYALYPHLSVE 93
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR------PLDKNFQrstgYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 94 ENILFGLKVRKVQKEERqKRLMEAIEMVGlkeyvkmKPgqlsggqrqrvalaraivsqaPICLMDEPLSNLDaklrAQMR 173
Cdd:cd03232 98 EALRFSALLRGLSVEQR-KRLTIGVELAA-------KP---------------------SILFLDEPTSGLD----SQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493527 174 IEIREIQQRL---GITMIYVTHD-QIEAMTMGDRIMVLNKG 210
Cdd:cd03232 145 YNIVRFLKKLadsGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-221 |
2.37e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAG--LEEISSGDLIINERVANDLEPKDR-NLSMVFQNYALYPH-------LS 91
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRLARLRAVLPQaaqpafaFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENILFGL--KVRKVQKEERQKR--LMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAP---------ICLMD 158
Cdd:PRK13547 100 AREIVLLGRypHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpprYLLLD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 159 EPLSNLDAKLRAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDI 221
Cdd:PRK13547 180 EPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-170 |
2.67e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.20 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 36 GPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKdrNLSMVFQNYALYPHLSVEENILFGLKVRkvqkeERQKRLM 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 116 EAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRA 170
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-165 |
6.62e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEetAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLE--EISSGDLIINERVANDLEPKDRN-- 76
Cdd:CHL00131 7 ILEIKNLHASVNENE--ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 -LSMVFQNYALYPHLSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLK-EYVKMKPGQL--------SGGQRQRVALAR 146
Cdd:CHL00131 85 gIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKlKLVGMDPSFLsrnvnegfSGGEKKRNEILQ 164
|
170
....*....|....*....
gi 446493527 147 AIVSQAPICLMDEPLSNLD 165
Cdd:CHL00131 165 MALLDSELAILDETDSGLD 183
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-193 |
1.17e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSkvYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLiineRVANDLEpkdrnlSMVFQ 82
Cdd:PRK11147 321 EMENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLE------VAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 83 NY--ALYPHLSVEENILFGLKVRKVQKEERQ------------KRLMEAiemvglkeyVKmkpgQLSGGQRQRVALARAI 148
Cdd:PRK11147 389 QHraELDPEKTVMDNLAEGKQEVMVNGRPRHvlgylqdflfhpKRAMTP---------VK----ALSGGERNRLLLARLF 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493527 149 VSQAPICLMDEPLSNLDaklraqmrIEIREIQQRL-----GiTMIYVTHD 193
Cdd:PRK11147 456 LKPSNLLILDEPTNDLD--------VETLELLEELldsyqG-TVLLVSHD 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
1.32e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGE---FFVLVGpsgCGKSTLLRMIAGLEEISSGDLIIN-ERVAND-----------LEPKDRnlsmvfQNYAL 86
Cdd:PRK11288 272 ISFSVRAGEivgLFGLVG---AGRSELMKLLYGATRRTAGQVYLDgKPIDIRsprdairagimLCPEDR------KAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 87 YPHLSVEENI---------LFGLKVRKVQKEERQKRLMEAIEmvglkeyVK-----MKPGQLSGGQRQRVALARAIVSQA 152
Cdd:PRK11288 343 IPVHSVADNInisarrhhlRAGCLINNRWEAENADRFIRSLN-------IKtpsreQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 153 PICLMDEPLSNLDAKLRAqmriEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKH----EIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-228 |
1.50e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISS--GDLIINERVA-----NDLEpkDRNLSMVFQNYALYPHL 90
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdiRDSE--ALGIVIIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVRK---VQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEP------- 160
Cdd:NF040905 94 SIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPtaalnee 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 161 ----LSNLDAKLRAQmrieireiqqrlGITMIYVTHDQIEAMTMGDRIMVLNKGsiQQVGTpLDIYNEPANE 228
Cdd:NF040905 174 dsaaLLDLLLELKAQ------------GITSIIISHKLNEIRRVADSITVLRDG--RTIET-LDCRADEVTE 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
1.68e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKD--RN----LSMVFQNYALYPHLSV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglANgivyISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 93 EENI------LFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKP-GQLSGGQRQRVALARAIVSQAPICLMDEPLSNLD 165
Cdd:PRK10762 348 KENMsltalrYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 166 --AKlraqmrieiREIQQRL------GITMIYVTHDQIEAMTMGDRIMVLNKGSI 212
Cdd:PRK10762 428 vgAK---------KEIYQLInqfkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-166 |
1.73e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 4 LKNVSKVYKNAEETA----VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGleEISSGDLIINERVA------NDLEPK 73
Cdd:TIGR00956 58 LTRGFRKLKKFRDTKtfdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITydgitpEEIKKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 74 DRNLSM-VFQNYALYPHLSVEENILFGLKVRKVQ-------KEERQKRLME-AIEMVGLKEYVKMKPGQ-----LSGGQR 139
Cdd:TIGR00956 136 YRGDVVyNAETDVHFPHLTVGETLDFAARCKTPQnrpdgvsREEYAKHIADvYMATYGLSHTRNTKVGNdfvrgVSGGER 215
|
170 180
....*....|....*....|....*..
gi 446493527 140 QRVALARAIVSQAPICLMDEPLSNLDA 166
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-224 |
1.86e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 3 ELKNVSKvYKNAEetaVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINervANDLEPKD------RN 76
Cdd:PRK09700 267 EVRNVTS-RDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN---GKDISPRSpldavkKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 77 LSMVFQNY---ALYPHLSVEEN--ILFGLKVRK-------VQKEERQKRLMEAIEMVGLK-EYVKMKPGQLSGGQRQRVA 143
Cdd:PRK09700 340 MAYITESRrdnGFFPNFSIAQNmaISRSLKDGGykgamglFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 144 LARAIVSQAPICLMDEPLSNLDAKLRAqmriEIREIQQRL---GITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLD 220
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKA----EIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
....
gi 446493527 221 IYNE 224
Cdd:PRK09700 496 DMSE 499
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-224 |
2.47e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.64 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISsGDLIINERVANdlepkdrnlSMVF 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWN---------SVPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHLSVEENILFGLKVRK---VQKEERQKRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVALARA 147
Cdd:cd03289 73 QKWRKAFGVIPQKVFIFSGTFRKnldPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 148 IVSQAPICLMDEPLSNLDAKLRAQMRieiREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-193 |
5.80e-10 |
|
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: 60.57 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 27 KKGEFFVLVGPSGCGKSTLLRmiagleeISSGDLIIN-ERVANDLEpKDRNLSMvFQNYALYPHLS--VEENI------- 96
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-------ILSGELKPNlGDYDEEPS-WDEVLKR-FRGTELQDYFKklANGEIkvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 97 -------LFGLKVRKVQK--EERqKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAK 167
Cdd:COG1245 168 yvdlipkVFKGTVRELLEkvDER-GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....*.
gi 446493527 168 LRAQMRIEIREIQQRlGITMIYVTHD 193
Cdd:COG1245 247 QRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-210 |
9.39e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 11 YKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEE---ISSGDLIINERvandlePKD----RNLSMVFQN 83
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGR------PLDssfqRSIGYVQQQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 84 YALYPHLSVEENILFGLKVR---KVQKEERQKRLMEAIEMVGLKEYVKM---KPGQ-LSGGQRQRVALARAIVSQ-APIC 155
Cdd:TIGR00956 845 DLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTIGVELVAKpKLLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 156 LMDEPLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHdQIEAMTMG--DRIMVLNKG 210
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-213 |
1.01e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 13 NAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEIS-SGDLIINERVANDLEPKD---RNLSMVFQN---YA 85
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 86 LYPHLSVEENILFGL-----KVRKVQKEERQKRLMEAIEMVGLKEYVKMKP-GQLSGGQRQRVALARAIVSQAPICLMDE 159
Cdd:TIGR02633 350 IVPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 160 PLSNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQ 213
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-193 |
1.60e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 34 LVGPSGCGKSTLLRMIAGLEEISSGDLiineRVANDL-------EPKdrnlsmvfqnyaLYPHLSVEENILFGLK-VRKV 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEA----RPAPGIkvgylpqEPQ------------LDPEKTVRENVEEGVAeVKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 106 QKE-------------------ERQKRLMEAIEMVGLKEY-----VKM----------KPGQLSGGQRQRVALARAIVSQ 151
Cdd:PRK11819 102 LDRfneiyaayaepdadfdalaAEQGELQEIIDAADAWDLdsqleIAMdalrcppwdaKVTKLSGGERRRVALCRLLLEK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446493527 152 APICLMDEPLSNLDAKLRAQMRieiREIQQRLGiTMIYVTHD 193
Cdd:PRK11819 182 PDMLLLDEPTNHLDAESVAWLE---QFLHDYPG-TVVAVTHD 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-212 |
4.39e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDR-NLSMVF-----QNYALYPHLSVEEN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 96 I------LFGLKVRKVQKEERQKRLMEAIemvGLK-EYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKL 168
Cdd:PRK15439 362 VcalthnRRGFWIKPARENAVLERYRRAL---NIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446493527 169 RAQMRIEIREI-QQRLGITMIYVTHDQIEAMTmgDRIMVLNKGSI 212
Cdd:PRK15439 439 RNDIYQLIRSIaAQNVAVLFISSDLEEIEQMA--DRVLVMHQGEI 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-206 |
4.76e-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: 54.69 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 28 KGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIInervandlepkdrnlsmvfqnyalyphLSVEenilfglkvrkvqk 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------IDGE-------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 108 eerqkRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIR-----EIQQR 182
Cdd:smart00382 40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|....
gi 446493527 183 LGITMIYVTHDQIEAMTMGDRIMV 206
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-192 |
6.25e-09 |
|
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: 57.45 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKVYKNAEeTAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVANDLEPKDRNLSM- 79
Cdd:TIGR00954 451 GIKFENIPLVTPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 80 VFQNYALYPHlSVEENILFGLkvrkvqkeeRQKRLMEAIEMVGLKEYVKMKPG---------QLSGGQRQRVALARAIVS 150
Cdd:TIGR00954 530 TLRDQIIYPD-SSEDMKRRGL---------SDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446493527 151 QAPICLMDEPLSnldaKLRAQMRIEIREIQQRLGITMIYVTH 192
Cdd:TIGR00954 600 KPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-193 |
8.27e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.92 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVsvhikkgefFVLVGPSGCGKSTLlrmIAGLEEISSGDLIINervaNDLEPKDRNL---- 77
Cdd:cd03240 4 LSIRNIRSFHERSEIEFFSPL---------TLIVGQNGAGKTTI---IEALKYALTGELPPN----SKGGAHDPKLireg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 ------SMVFQN-----YALYPHLSVEENILFglkvrkVQKEERQKRLMEAIemvglkeyvkmkpGQLSGGQRQ------ 140
Cdd:cd03240 68 evraqvKLAFENangkkYTITRSLAILENVIF------CHQGESNWPLLDMR-------------GRCSGGEKVlaslii 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493527 141 RVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQRLGI-TMIYVTHD 193
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNfQLIVITHD 182
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-216 |
1.00e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSKvykNAEETAV-KGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLE--EISSGDLIINERVANDLEPKDR-- 75
Cdd:PRK09580 1 MLSIKDLHV---SVEDKAIlRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 76 -NLSMVFQNYALYPHLSVEENILFGLK-VRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQL--------SGGQRQRVALA 145
Cdd:PRK09580 78 eGIFMAFQYPVEIPGVSNQFFLQTALNaVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLtrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 146 RAIVSQAPICLMDEPLSNLDA---KLRAQMRIEIREIQQrlgiTMIYVTHDQ-IEAMTMGDRIMVLNKGSIQQVG 216
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIdalKIVADGVNSLRDGKR----SFIIVTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-210 |
2.08e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 25 HIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII-NERVANDLE---PKDRNLSmVFQNYA-----------LYPH 89
Cdd:PRK11147 25 HIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQqdpPRNVEGT-VYDFVAegieeqaeylkRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 90 LSV-------EENILfglKVRKVQKE-------ERQKRLMEAIEMVGLKEyvKMKPGQLSGGQRQRVALARAIVSQAPIC 155
Cdd:PRK11147 104 ISHlvetdpsEKNLN---ELAKLQEQldhhnlwQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 156 LMDEPLSNLDaklraqmrIE-IREIQQRL----GiTMIYVTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK11147 179 LLDEPTNHLD--------IEtIEWLEGFLktfqG-SIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-193 |
2.10e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 26 IKKGEFFVLVGPSGCGKSTLLRmiagleeISSGDLIIN-ERVANDLEPKDrnlsmVFQNYA---LYPHLS-VEENilfgl 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------ILSGELIPNlGDYEEEPSWDE-----VLKRFRgteLQNYFKkLYNG----- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 101 KVRKVQK----------------------EERqKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMD 158
Cdd:PRK13409 159 EIKVVHKpqyvdlipkvfkgkvrellkkvDER-GKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 446493527 159 EPLSNLDAKLRAQMRIEIREIQQrlGITMIYVTHD 193
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHD 270
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
90-306 |
3.08e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 90 LSVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLR 169
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 170 AQMRIEIREIqQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIqqvgtpldiynepanefvasfigspsmnINDGEVDKE 249
Cdd:NF000106 181 NEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRV----------------------------IADGKVDEL 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 250 KGVLHIGKLQI-PLSIGQLKQLPEGIIRIGMrpEHIALSEEGQEVTLQSVEVLGNESI 306
Cdd:NF000106 232 KTKVGGRTLQIrPAHAAELDRMVGAIAQAGL--DGIAGATADHEDGVVNVPIVSDEQL 287
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-197 |
3.22e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVskVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAG----------------------LEEIS--- 56
Cdd:PRK10938 261 IVLNNG--VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlfgrrrgsgetIWDIKkhi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 57 ---SGDLIINERVANDLepkdRN--LSMVFQNYALYPHLSveenilfglkvrkvqkeERQKRL-MEAIEMVGLKEYVKMK 130
Cdd:PRK10938 339 gyvSSSLHLDYRVSTSV----RNviLSGFFDSIGIYQAVS-----------------DRQQKLaQQWLDILGIDKRTADA 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493527 131 PGQ-LSGGQrQRVAL-ARAIVSQAPICLMDEPLSNLDAKLRAQMR----IEIREIQQRLgitmIYVTHDQIEA 197
Cdd:PRK10938 398 PFHsLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRrfvdVLISEGETQL----LFVSHHAEDA 465
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
11-229 |
4.55e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 11 YKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLiinervandlePKDRNLSMVFQNYALYPHL 90
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 91 SVEENILFGLKVRKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRA 170
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493527 171 QMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDI---YNEPANEF 229
Cdd:PRK13546 181 KCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDF 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-224 |
1.05e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 2 IELKNVSKVYKNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEiSSGDLIINERVANDLepkdrNLSMVF 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSV-----TLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 82 QNYALYPHlsvEENILFGLKVRKVQKEER--QKRLMEAIEMVGLKEYVKMKPGQL-----------SGGQRQRVALARAI 148
Cdd:TIGR01271 1292 KAFGVIPQ---KVFIFSGTFRKNLDPYEQwsDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493527 149 VSQAPICLMDEPLSNLDAklrAQMRIEIREIQQRLGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGTPLDIYNE 224
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-190 |
2.20e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 23 SVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIIN-ERVAN----------DLEPKDRNLSMvfqnyalyphLS 91
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRlsfeqlqklvSDEWQRNNTDM----------LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENIlFGLKVRKVQKEERQK--RLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLR 169
Cdd:PRK10938 93 PGEDD-TGRTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180
....*....|....*....|.
gi 446493527 170 AQMRIEIREIQQRlGITMIYV 190
Cdd:PRK10938 172 QQLAELLASLHQS-GITLVLV 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-217 |
7.02e-07 |
|
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: 48.86 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 14 AEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRmiAGLEEISSgdliinERVANDLEPKDRNLSMVFqnyalyphlsve 93
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGK------ARLISFLPKFSRNKLIFI------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 94 enilfglkvrkvqkeerqKRLMEAIEMvGLkEYvkMKPGQ----LSGGQRQRVALARAIVSQAP--ICLMDEPLSNLDAK 167
Cdd:cd03238 66 ------------------DQLQFLIDV-GL-GY--LTLGQklstLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493527 168 LRAQMRIEIREIQQrLGITMIYVTHDqIEAMTMGDRIMVLNKGSIQQVGT 217
Cdd:cd03238 124 DINQLLEVIKGLID-LGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-284 |
1.10e-06 |
|
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: 45.27 E-value: 1.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 235 GSPSMNINDGEVDKEKGVLHIGKLQIPLSIGQLKQLPEGIIR---IGMRPEHI 284
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGGVTLPLPEGQVLALKLYVGKeviLGIRPEHI 53
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-210 |
1.13e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 1 MIELKNVSkvykNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAND---LEPKDRNL 77
Cdd:PRK10982 250 ILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaNEAINHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 78 SMVFQ---NYALYPHLSVEENILfglkVRKVQKEERQKRLMEAIEMVGLKEYV-----------KMKPGQLSGGQRQRVA 143
Cdd:PRK10982 326 ALVTEerrSTGIYAYLDIGFNSL----ISNIRNYKNKVGLLDNSRMKSDTQWVidsmrvktpghRTQIGSLSGGNQQKVI 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493527 144 LARAIVSQAPICLMDEPLSNLDAKLRAQMRIEIREIQQR-LGITMIyvTHDQIEAMTMGDRIMVLNKG 210
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIII--SSEMPELLGITDRILVMSNG 467
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-165 |
4.13e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 34 LVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAndlepkdrnlSMVFQNYALyPHLSVEENILfgLKVRKVQKEERQKR 113
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR----------MAVFSQHHV-DGLDLSSNPL--LYMMRCFPGVPEQK 606
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446493527 114 LMEAIEMVGLKEYVKMKPG-QLSGGQRQRVALARAIVSQAPICLMDEPLSNLD 165
Cdd:PLN03073 607 LRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-213 |
6.66e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 19 VKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGL-EEISSGDLIINER---VANDLEPKDRNLSMVFQN---YALYPHLS 91
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKpvkIRNPQQAIAQGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 92 VEENILfgLKVrkVQKEERQKRLMEAIEMVGLKEYVK----------MKPGQLSGGQRQRVALARAIVSQAPICLMDEPL 161
Cdd:PRK13549 358 VGKNIT--LAA--LDRFTGGSRIDDAAELKTILESIQrlkvktaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493527 162 SNLDAKLRAQMRIEIREIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQ 213
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-193 |
2.29e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 22 VSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLII--NERVAndlepKDRNLSMVFQNYalyphlSVEENILFG 99
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpNERLG-----KLRQDQFAFEEF------TVLDTVIMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 100 -LKVRKVqKEERQK--RLMEAIEMVGLK------EYVKM-------KPGQL------------------SGGQRQRVALA 145
Cdd:PRK15064 89 hTELWEV-KQERDRiyALPEMSEEDGMKvadlevKFAEMdgytaeaRAGELllgvgipeeqhyglmsevAPGWKLRVLLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493527 146 RAIVSQAPICLMDEPLSNLDaklraqmrIE-IREIQQRL---GITMIYVTHD 193
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLD--------INtIRWLEDVLnerNSTMIIISHD 211
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
12-204 |
2.67e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.94 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 12 KNAEETAVKGVSVHIKKGEFFVLVGPSGCGKSTLlrmiagleeisSGDLIINERVANDLEpkdrNLSMVFQNY------- 84
Cdd:cd03270 4 RGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----------AFDTIYAEGQRRYVE----SLSAYARQFlgqmdkp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 85 ------ALYPHLSVEENIL-----------------FGLKVRKVQKEERQKRLMEaiemVGLkEYVKM--KPGQLSGGQR 139
Cdd:cd03270 69 dvdsieGLSPAIAIDQKTTsrnprstvgtvteiydyLRLLFARVGIRERLGFLVD----VGL-GYLTLsrSAPTLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 140 QRVALARAIVSQ--APICLMDEPLSNLDAKLRAQMRIEIREIQQrLGITMIYVTHDQiEAMTMGDRI 204
Cdd:cd03270 144 QRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDE-DTIRAADHV 208
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
35-118 |
1.93e-04 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 41.07 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 35 VGPSGCGKSTLLRMIA---GLEEISSGDLIINERVANDLEPKDRNLSmvfqnyalyphlsveenilfglKVRKVQKEERQ 111
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAeklGFPHISAGDLLREEAKERGLVEDRDEMR----------------------KLPLEPQKELQ 58
|
....*..
gi 446493527 112 KRLMEAI 118
Cdd:pfam13207 59 KLAAERI 65
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-253 |
3.17e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 18 AVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSGDLIINERVAndlepkdrnlsMVFQNYALYPHLSVEENI- 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA-----------LIAISSGLNGQLTGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 97 LFGLKVrKVQKEERQKRLMEAIEMVGLKEYVKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLDAKLRAQMRIEI 176
Cdd:PRK13545 108 LKGLMM-GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 177 REIQQRlGITMIYVTHDQIEAMTMGDRIMVLNKGSIQQVGtplDIyNEPANEFVASFIGSPSMNINDGEVDKEKGVL 253
Cdd:PRK13545 187 NEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG---DI-KEVVDHYDEFLKKYNQMSVEERKDFREEQIS 258
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-119 |
7.07e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.93 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 26 IKKGE-FFVLVGPSGCGKSTLLRMIagLEEIssgdliinervandlePKDRNLSMVFqnyalYPHLSVEEnIL------F 98
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRL--LERL----------------PDDVKVAYIP-----NPQLSPAE-LLraiadeL 94
|
90 100
....*....|....*....|.
gi 446493527 99 GLKVRKVQKEERQKRLMEAIE 119
Cdd:COG3267 95 GLEPKGASKADLLRQLQEFLL 115
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
36-64 |
8.16e-04 |
|
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: 39.39 E-value: 8.16e-04
10 20 30
....*....|....*....|....*....|..
gi 446493527 36 GPSGCGKSTLLRMIA---GLEEISSGDLIINE 64
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTEE 37
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
127-212 |
1.07e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 127 VKMKPGQLSGGQRQRVALARAIVSQAPICLMDEPLSNLD--AKLraqmriEIREIQQRL-----GITMIyvTHDQIEAMT 199
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKY------EIYTIINELaaegkGVIVI--SSELPELLG 469
|
90
....*....|...
gi 446493527 200 MGDRIMVLNKGSI 212
Cdd:NF040905 470 MCDRIYVMNEGRI 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-165 |
2.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 23 SVHIKKGEFFVLVGPSGCGKSTLLRMIA-----GL----------EEISSGDLIINERVAN-DLEpkdRNLSMVFQNYAL 86
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqilhveQEVVGDDTTALQCVLNtDIE---RTQLLEEEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 87 YPHLSVEENILFGLKVRK----VQKEERQKRL------MEAIE-----------MVGLK---EYVKMKPGQLSGGQRQRV 142
Cdd:PLN03073 274 AQQRELEFETETGKGKGAnkdgVDKDAVSQRLeeiykrLELIDaytaearaasiLAGLSftpEMQVKATKTFSGGWRMRI 353
|
170 180
....*....|....*....|...
gi 446493527 143 ALARAIVSQAPICLMDEPLSNLD 165
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-58 |
2.47e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 2.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 2 IELKNVSKVYKNaeETAVKGVSVHIKKGEFFVLVGPSGCGKSTLLRMIAGLEEISSG 58
Cdd:PRK15064 320 LEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-194 |
2.54e-03 |
|
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: 38.11 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 23 SVHIKKGEFFVLVGPSGCGKSTLLRMIAgleeissgdliinervandlepkdrnLSMVFQNYALYPHLSVEENIlfglkv 102
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------LALGGAQSATRRRSGVKAGC------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 103 rkvqkeerQKRLMEAIEMVGLKeyvkmkpgQLSGGQRQRVALARAI----VSQAPICLMDEPLSNLDakLRAQMRIE--I 176
Cdd:cd03227 63 --------IVAAVSAELIFTRL--------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLD--PRDGQALAeaI 124
|
170
....*....|....*...
gi 446493527 177 REIQQRlGITMIYVTHDQ 194
Cdd:cd03227 125 LEHLVK-GAQVIVITHLP 141
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
36-113 |
3.68e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 37.86 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 36 GPSGCGKSTLLRMIA---GLEEISSGDliINERVAndlepKDRNLSMV-FQNYAlyphlsvEENILFGLKVRKVQKEERQ 111
Cdd:PRK04182 7 GPPGSGKTTVARLLAeklGLKHVSAGE--IFRELA-----KERGMSLEeFNKYA-------EEDPEIDKEIDRRQLEIAE 72
|
..
gi 446493527 112 KR 113
Cdd:PRK04182 73 KE 74
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
117-179 |
3.88e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 3.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493527 117 AIEMVGLKEYVKMKpgQLSGGQRQRVALAR--AI--VSQAPICLMDEPLSNLDAKLRAQMRIEIREI 179
Cdd:cd03272 144 SLTNMKQDEQQEMQ--QLSGGQKSLVALALifAIqkCDPAPFYLFDEIDAALDAQYRTAVANMIKEL 208
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-49 |
5.90e-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: 5.90e-03
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
27-49 |
6.70e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.38 E-value: 6.70e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-225 |
7.73e-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: 38.46 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493527 90 LSVEENILF--GLKVRKVQKEERQKRLMEAIEM------VGLkEYVKMK--PGQLSGGQRQRVALARAIVSQ--APICLM 157
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERlgflidVGL-DYLSLSraAGTLSGGEAQRIRLATQIGSGltGVLYVL 514
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493527 158 DEPLSNLDAklRAQMR-IEIREIQQRLGITMIYVTHDQiEAMTMGDRIMVLNKGS------IQQVGTPLDIYNEP 225
Cdd:TIGR00630 515 DEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDIGPGAgehggeVVASGTPEEILANP 586
|
|
| |
