|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-373 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 520.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAM 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 161 PLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFI 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLG-----TTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 241 GAPEMNIKPSTLVEKegqiGLTVGQYTLVLNERqqakVATHTGEKVFFGVRPEFIsmSLQPFVGNHSQGELVRVENMGHE 320
Cdd:COG3839 235 GSPPMNLLPGTVEGG----GVRLGGVRLPLPAA----LAAAAGGEVTLGIRPEHL--RLADEGDGGLEATVEVVEPLGSE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 321 FFMYIKVENFELTCRLPSDEArpiIENGlhRTVYFQFDMDKCHIFDAKTEKNI 373
Cdd:COG3839 305 TLVHVRLGGQELVARVPGDTR---LRPG--DTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-373 |
2.79e-152 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 433.12 E-value: 2.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 161 PLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFI 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLK-----TTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 241 GAPEMNIKPSTLVEKEGQIGLTvGQYTLVLNerqqAKVATHTGEKVFFGVRPEFISMSLQPFvGNHSQGELvrVENMGHE 320
Cdd:PRK11650 236 GSPAMNLLDGRVSADGAAFELA-GGIALPLG----GGYRQYAGRKLTLGIRPEHIALSSAEG-GVPLTVDT--VELLGAD 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 321 FFMYIKVENFELTCRLPSdEARPIIenglHRTVYFQFDMDKCHIFDAKTEKNI 373
Cdd:PRK11650 308 NLAHGRWGGQPLVVRLPH-QERPAA----GSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-367 |
2.67e-138 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 397.55 E-value: 2.67e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAM 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 161 PLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFI 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELG-----ITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 241 GapEMNIKPSTLVEKEGQiGLTVGQYTLVLNerqqAKVATHTGEKVFFGVRPEFISMSLQPfVGNHSQGELVRVENMGHE 320
Cdd:COG3842 237 G--EANLLPGTVLGDEGG-GVRTGGRTLEVP----ADAGLAAGGPVTVAIRPEDIRLSPEG-PENGLPGTVEDVVFLGSH 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1540023143 321 FFMYIKVEN-FELTCRLPSDEARPIienGLHRTVYFQFDMDKCHIFDA 367
Cdd:COG3842 309 VRYRVRLGDgQELVVRVPNRAALPL---EPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-365 |
1.37e-122 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 358.57 E-value: 1.37e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYSNgfraVH---GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG 77
Cdd:PRK11000 1 MASVTLRNVTKAYGD----VViskDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 158 FDEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVA 237
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGR-----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 238 GFIGAPEMNIKPSTL--VEKEG-QIGLTVGQYTLVLNERQQAKVathtGEKVFFGVRPEFISMSLQPFVGNHsqGELVRV 314
Cdd:PRK11000 232 GFIGSPKMNFLPVKVtaTAIEQvQVELPNRQQVWLPVEGRGVQV----GANMSLGIRPEHLLPSDIADVTLE--GEVQVV 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 315 ENMGHEFFMYIKVENFELTCRLPSDEARPIIENGlhrTVYFQFDMDKCHIF 365
Cdd:PRK11000 306 EQLGNETQIHIQIPAIRQNLVYRQNDVVLVEEGA---TFAIGLPPERCHLF 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-222 |
1.14e-113 |
|
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: 329.99 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 11 KVYSNgFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPH 90
Cdd:cd03301 8 KRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLR 170
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 171 ASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVD 222
Cdd:cd03301 167 VQMRAELKRLQQRLG-----TTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
16-358 |
3.06e-100 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 300.52 E-value: 3.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN-NLAPKSRGIAMVFQNYALYPHMTVK 94
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQHYALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR 174
Cdd:COG1118 94 ENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 175 IRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGapEMNIkpSTLVE 254
Cdd:COG1118 174 RWLRRLHDELG-----GTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNV--LRGRV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 255 KEGQigLTVGQYTLVLNERQQAKVAThtgekvfFGVRPEFISMSLQPFVGNHSQGELVRVENMGHEFFMYIKVENFE--- 331
Cdd:COG1118 245 IGGQ--LEADGLTLPVAEPLPDGPAV-------AGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLEDGEgqp 315
|
330 340
....*....|....*....|....*....
gi 1540023143 332 LTCRLPSDEARpiiENGLHR--TVYFQFD 358
Cdd:COG1118 316 LEAEVTKEAWA---ELGLAPgdPVYLRPR 341
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-241 |
5.74e-100 |
|
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: 295.69 E-value: 5.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVK 94
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR 174
Cdd:cd03300 91 ENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 175 IRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIG 241
Cdd:cd03300 171 LELKRLQKEL-----GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-222 |
9.24e-100 |
|
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: 294.43 E-value: 9.24e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 NYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 164 NLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVD 222
Cdd:cd03259 160 ALDAKLREELREELKELQRELG-----ITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-293 |
7.09e-95 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 288.00 E-value: 7.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGL 101
Cdd:PRK09452 32 NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFENVAFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 KLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLH 181
Cdd:PRK09452 112 RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 182 KQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGapEMNIKPSTLVE--KEGQI 259
Cdd:PRK09452 192 RKL-----GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFDATVIErlDEQRV 264
|
250 260 270
....*....|....*....|....*....|....
gi 1540023143 260 GLTVGQYTLVLNERQQAKVathtGEKVFFGVRPE 293
Cdd:PRK09452 265 RANVEGRECNIYVNFAVEP----GQKLHVLLRPE 294
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-315 |
1.15e-90 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 276.49 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFNKLGKVYSNGFR---AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVV-----NNLAP 73
Cdd:NF040933 1 VTVRVENVTKIFKKGKKevvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVaspgkIIVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 74 KSRGIAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKP 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 154 DVFLFDEPLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTN 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELK-----ITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPAN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 234 MFVAGFIGapEMNIKPSTLVEKEGQIGLTVgqytlvlneRQQAKVATHTGEKVFFGVRPEFISMSLQPFVGNHSQGEL-- 311
Cdd:NF040933 236 IFVARLIG--DINLLEGKVEEEGLVDGNDL---------KIPLPNPKLEAGEVIIGIRPEDIDISESDMRLPPGFVEVgk 304
|
....
gi 1540023143 312 VRVE 315
Cdd:NF040933 305 GRVK 308
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-308 |
9.81e-87 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 266.20 E-value: 9.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGLK 102
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 103 LSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHK 182
Cdd:PRK11432 105 MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 183 QLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGapEMNIKPSTLveKEGQIglT 262
Cdd:PRK11432 185 QFN-----ITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMG--DANIFPATL--SGDYV--D 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1540023143 263 VGQYTLVLNERQQAKVATHTGekvFFGVRPEFISMSLQpfvGNHSQ 308
Cdd:PRK11432 254 IYGYRLPRPAAFAFNLPDGEC---TVGVRPEAITLSEQ---GEESQ 293
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-297 |
1.22e-85 |
|
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: 262.43 E-value: 1.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 35 IVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQ 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 115 VAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLkksgkAATTV 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL-----GITFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 195 YVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGapEMNIKPSTLVEKEGQIGLTVGQYTLVLNERQ 274
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIG--EINVFEATVIERKSEQVVLAGVEGRRCDIYT 233
|
250 260
....*....|....*....|...
gi 1540023143 275 QAKVAthTGEKVFFGVRPEFISM 297
Cdd:TIGR01187 234 DVPVE--KDQPLHVVLRPEKIVI 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-242 |
7.25e-78 |
|
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: 239.55 E-value: 7.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVK 94
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKL----SKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLR 170
Cdd:cd03296 93 DNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 171 ASMRIRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGA 242
Cdd:cd03296 173 KELRRWLRRLHDEL-----HVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
5.55e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 235.37 E-value: 5.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVY---SNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKsrg 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 158 FDEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVM-----KLGHIMQVDTP 224
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGK-----TVLFVTHDVDEAVFLADRVVVLsarpgRIVEEIDVDLP 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
15-318 |
3.36e-75 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 237.43 E-value: 3.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVK 94
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR 174
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 175 IRISDLhkqLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGApeMNIKPSTLVE 254
Cdd:PRK11607 190 LEVVDI---LERVG--VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEGVLKE 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 255 KEGQiGLTVGQYTLVLNERQQAKVATHTGEKVFFGVRPEFISMSLQPFVG--NHSQGELVRVENMG 318
Cdd:PRK11607 263 RQED-GLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADgcNFAVGEVIHIAYLG 327
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-318 |
7.98e-75 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 235.74 E-value: 7.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAF 99
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISD 179
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 180 LHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGAPemNIKPSTLVEKEGQI 259
Cdd:NF040840 176 WHREF-----GFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGVAEKGGEGT 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 260 GLTVGQYTLVLNERQQAkvathtgeKVFFGVRPEFISMSLQPFVG---NHSQGELVRVENMG 318
Cdd:NF040840 249 ILDTGNIKIELPEEKKG--------KVRIGIRPEDITISTEKVKTsarNEFKGKVEEIEDLG 302
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-213 |
1.82e-73 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 227.74 E-value: 1.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNG---FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNnlaPKSRGIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 161 PLSNLDAKLRASMRiriSDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVM 213
Cdd:cd03293 158 PFSALDALTREQLQ---EELLDIWRETGK--TVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-244 |
2.05e-70 |
|
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: 220.64 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQ 83
Cdd:cd03295 3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 NYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRL--PRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:cd03295 83 QIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 162 LSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIG 241
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQELGK-----TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
...
gi 1540023143 242 APE 244
Cdd:cd03295 238 ADR 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-301 |
3.47e-66 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 213.41 E-value: 3.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYSNGfRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYA 86
Cdd:PRK10851 6 ANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPHMTVKENLAFGLKLskLPKDQ------IEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 161 PLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFI 240
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELK-----FTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 241 GapEMNikpstlvEKEGQI---GLTVGQYTLVLN--ERQQAKVathtgeKVFFgvRPEFISMSLQP 301
Cdd:PRK10851 238 G--EVN-------RLQGTIrggQFHVGAHRWPLGytPAYQGPV------DLFL--RPWEVDISRRT 286
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-242 |
9.94e-66 |
|
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: 208.34 E-value: 9.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGL 101
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 KLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLH 181
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 182 KQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGA 242
Cdd:cd03299 177 KEFG-----VTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGF 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
3.41e-64 |
|
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: 202.42 E-value: 3.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN----NLAPKSRGIA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFGlklsklpkdqieaqvaeaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 160 EPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGH 217
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGI-----TVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-240 |
5.56e-64 |
|
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: 205.18 E-value: 5.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK------SRGIAMVFQNYALYPHMT 92
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAS 172
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 173 MRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFI 240
Cdd:cd03294 199 MQDELLRLQAELQK-----TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
16-290 |
2.33e-61 |
|
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: 201.23 E-value: 2.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP------KSRGIAMVFQNYALYP 89
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL 169
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 170 RASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGAPE----- 244
Cdd:TIGR01186 165 RDSMQDELKKLQATLQK-----TIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDlsqvf 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 245 -----MNIKPSTLVEKEGQIGLTVGqYTLVLNERQQAKVATHTGeKVFFGV 290
Cdd:TIGR01186 240 daeriAQRMNTGPITKTADKGPRSA-LQLMRDERVDSLYVVDRQ-NKLVGV 288
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-218 |
6.14e-59 |
|
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: 190.39 E-value: 6.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNG---FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG----- 77
Cdd:cd03255 3 LKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 -IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:cd03255 83 hIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 157 LFDEPLSNLDAKLRAS-MRIrISDLHKQLKKsgkaaTTVYVTHDQTEAMtMGDRICVMKLGHI 218
Cdd:cd03255 163 LADEPTGNLDSETGKEvMEL-LRELNKEAGT-----TIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
4.99e-58 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 188.33 E-value: 4.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVI-FNKLGKVYSNG---FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR 76
Cdd:COG1136 1 MSPLLeLRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 77 G------IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIV 150
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 151 KKPDVFLFDEPLSNLDAKLRAS-MRIrISDLHKQLKKsgkaaTTVYVTHDQtEAMTMGDRICVMKLGHI 218
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGT-----TIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-222 |
5.11e-57 |
|
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: 185.19 E-value: 5.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKIN---DGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN------NLAPKSRGIAMVFQNYALYPHMT 92
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkkiNLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKLPKDQIeaQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAS 172
Cdd:cd03297 92 VRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540023143 173 MRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVD 222
Cdd:cd03297 170 LLPELKQIKKNLN-----IPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-227 |
8.58e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.87 E-value: 8.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIG--DRVVNNLAPKSRgIAMVFQNYA 86
Cdd:COG1131 6 LTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgeDVARDPAEVRRR-IGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:COG1131 84 LYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 167 AKLRASMRirisDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:COG1131 164 PEARRELW----ELLRELAAEGK--TVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-233 |
1.34e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.41 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN----NLAPKSRGIA 79
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFGL-KLSKLPKDQIEAQVAE-------AAKIleledllDRLPRQLSGGQAQRVAVGRAIVK 151
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMEllervglADKA-------DAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 152 KPDVFLFDEPLSNLDAKLR----ASMRirisdlhkQLKKSGKaaTTVYVTHDqteamtMG------DRICVMKLGHIMQV 221
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVgevlDVMR--------DLAKEGM--TMVVVTHE------MGfarevaDRVVFMDGGRIVEE 217
|
250
....*....|..
gi 1540023143 222 DTPDNLYHYPTN 233
Cdd:COG1126 218 GPPEEFFENPQH 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-218 |
1.97e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 173.70 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAM 80
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 161 PLSNLDAKlrasMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:COG2884 164 PTGNLDPE----TSWEIMELLEEINRRGT--TVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-229 |
3.13e-52 |
|
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: 173.29 E-value: 3.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQ 83
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 NyalyP-----HMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLF 158
Cdd:COG1122 83 N----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 159 DEPLSNLDAKlrasMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYH 229
Cdd:COG1122 159 DEPTAGLDPR----GRRELLELLKRLNKEGK--TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-229 |
4.82e-52 |
|
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: 173.24 E-value: 4.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 14 SNGF--RAVH-GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAMVFQNY 85
Cdd:COG1127 12 TKSFgdRVVLdGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGMLFQGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLAFGLK-LSKLPKDQIEAQVAE---------AAKileledlldRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:COG1127 92 ALFDSLTVFENVAFPLReHTDLSEAEIRELVLEklelvglpgAAD---------KMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 156 FLFDEPLSNLDAklRASMRIR--ISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYH 229
Cdd:COG1127 163 LLYDEPTAGLDP--ITSAVIDelIRELRDELG-----LTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-231 |
1.78e-51 |
|
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: 179.33 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVY----SNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIA 79
Cdd:COG1123 266 LSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQN--YALYPHMTVKENLAFGLKLSK-LPKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:COG1123 346 MVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELlERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 156 FLFDEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:COG1123 426 LILDEPTSALDVSVQAQILNLLRDLQRELGL-----TYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-218 |
4.52e-51 |
|
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: 169.63 E-value: 4.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNgFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS----RGIA 79
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFGL-KLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLF 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 159 DEPLSNLDAKLRASmrirISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03262 160 DEPTSALDPELVGE----VLDVMKDLAEEGM--TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
3.77e-50 |
|
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: 167.26 E-value: 3.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVF 82
Cdd:cd03225 2 LKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 83 QNyalyP-HM----TVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:cd03225 82 QN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 158 FDEPLSNLDAKLRAsmriRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGH 217
Cdd:cd03225 158 LDEPTAGLDPAGRR----ELLELLKKLKAEGK--TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-218 |
1.32e-49 |
|
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: 167.29 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSNGFR---AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQ 83
Cdd:COG1124 7 LSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 NY--ALYPHMTVKENLAFGLKLSKLPkdQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:COG1124 87 DPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELlEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 161 PLSNLDaklrASMRIRISDLHKQLKKSGKaATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:COG1124 165 PTSALD----VSVQAEILNLLKDLREERG-LTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-315 |
3.09e-49 |
|
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: 169.51 E-value: 3.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN------NLAPKSRGIAMVFQNYALYPHMTVKEN 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiFLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKLPKDQIE-AQVAEAAKILELEDLLdrlPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRI 175
Cdd:COG4148 98 LLYGRKRAPRAERRISfDEVVELLGIGHLLDRR---PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 176 RISDLHKQLKKSgkaatTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGApeMNIKPSTLVEK 255
Cdd:COG4148 175 YLERLRDELDIP-----ILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEA--GSVLEATVAAH 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 256 EGQIGLT---VGQYTLVLNERQQAkvathTGEKVFFGVRPEFISMSLQPFVG----NHSQGELVRVE 315
Cdd:COG4148 248 DPDYGLTrlaLGGGRLWVPRLDLP-----PGTRVRVRIRARDVSLALEPPEGssilNILPGRVVEIE 309
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-219 |
3.40e-49 |
|
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: 165.37 E-value: 3.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSNG---FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG-----IAM 80
Cdd:cd03257 7 LSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNY--ALYPHMTVKENLAFGLKLSKLPKDQ---IEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:cd03257 87 VFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKearKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 156 FLFDEPLSNLDAKLRAsmriRISDLHKQLKKSgKAATTVYVTHDQTEAMTMGDRICVMKLGHIM 219
Cdd:cd03257 167 LIADEPTSALDVSVQA----QILDLLKKLQEE-LGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-227 |
9.81e-48 |
|
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: 161.90 E-value: 9.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 12 VYSNGFRAVH-GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAMVFQNY 85
Cdd:cd03261 7 TKSFGGRTVLkGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLAFGLK-LSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:cd03261 87 ALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 165 LDAKlraSMRIrISDLHKQLKKSgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03261 167 LDPI---ASGV-IDDLIRSLKKE-LGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
21-233 |
3.87e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.64 E-value: 3.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGI----AMVFQNYALYPHMTVKEN 96
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFG-LKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRI 175
Cdd:PRK09493 98 VMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 176 RISDLHKQlkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTN 233
Cdd:PRK09493 178 VMQDLAEE------GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
7.19e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 160.41 E-value: 7.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYSNGFRAVH---GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNnlAPKS-R 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPalqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGAdR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 77 GIamVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:COG4525 79 GV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 157 LFDEPLSNLDAKLRASMRIRISDLhkqLKKSGKAAttVYVTHDQTEAMTMGDRICVM 213
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDV---WQRTGKGV--FLITHSVEEALFLATRLVVM 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-216 |
7.67e-47 |
|
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: 158.95 E-value: 7.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEviFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS----- 75
Cdd:TIGR02673 1 MIE--FHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 RGIAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 156 FLFDEPLSNLDAKLRAsmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:TIGR02673 159 LLADEPTGNLDPDLSE----RILDLLKRLNKRG--TTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-219 |
1.57e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 159.07 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAM 80
Cdd:COG3638 5 LRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFG-------LK--LSKLPKDQIE------AQVAEAAKILEledlldrlpR--QLSGGQAQRV 143
Cdd:COG3638 85 IFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDREralealERVGLADKAYQ---------RadQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 144 AVGRAIVKKPDVFLFDEPLSNLDAKL-RASMRIrISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIM 219
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDG-----ITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-225 |
4.08e-46 |
|
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: 157.34 E-value: 4.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 12 VYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETI-----SDGEVRIGDRVVNNLAPKS----RGIAMVF 82
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelrRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 83 QNYALYPhMTVKENLAFGLKLS-KLPKDQIEAQVAEAAKILE--LEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:cd03260 88 QKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAAlwDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 160 EPLSNLDaklRASMRiRISDLHKQLKKSgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPD 225
Cdd:cd03260 167 EPTSALD---PISTA-KIEELIAELKKE---YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
7.59e-46 |
|
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: 163.92 E-value: 7.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVI-FNKLGKVYSNG-FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL---ETISDGEVRIGDRVVNNLAPKS 75
Cdd:COG1123 1 MTPLLeVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 RG--IAMVFQN--YALYPhMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVK 151
Cdd:COG1123 81 RGrrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 152 KPDVFLFDEPLSNLDAKLRAsmriRISDLHKQLKKSgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQA----EILDLLRELQRE-RGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-242 |
7.74e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.84 E-value: 7.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGLK 102
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 103 LS-KLPKDQiEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLH 181
Cdd:COG3840 98 PGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 182 KQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGA 242
Cdd:COG3840 177 RERG-----LTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-218 |
5.46e-45 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 154.10 E-value: 5.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAM 80
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 161 PLSNLDAKLRAsmriRISDLhkqLKKSGKAATTVYV-THDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03292 163 PTGNLDPDTTW----EIMNL---LKKINKAGTTVVVaTHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-218 |
1.72e-44 |
|
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: 153.12 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNGFRAVH---GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS----- 75
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTalkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 RGIAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 156 FLFDEPLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELG-----LTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-218 |
1.54e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 154.08 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNG---FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RG 77
Cdd:COG1135 4 LENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAE-------AAKileledlLDRLPRQLSGGQAQRVAVGRAIV 150
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAEllelvglSDK-------ADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 151 KKPDVFLFDEPLSNLDAK--------LRasmririsDLHKQLKksgkaATTVYVTHDqteamtMG------DRICVMKLG 216
Cdd:COG1135 157 NNPKVLLCDEATSALDPEttrsildlLK--------DINRELG-----LTIVLITHE------MDvvrricDRVAVLENG 217
|
..
gi 1540023143 217 HI 218
Cdd:COG1135 218 RI 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-227 |
3.18e-43 |
|
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: 150.41 E-value: 3.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAM 80
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGlKLSKLPK--------DQIEAQVA-EAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVK 151
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSG-RLGRRSTwrslfglfPKEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 152 KPDVFLFDEPLSNLDAKL-RASMRIrISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03256 162 QPKLILADEPVASLDPASsRQVMDL-LKRINRE-----EGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-218 |
1.65e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.27 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPhMTVKENLA 98
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQEPALWG-GTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 99 FGLKLSKLPKDQiEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAsmriRIS 178
Cdd:COG4619 96 FPFQLRERKFDR-ERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR----RVE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540023143 179 DL-HKQLKKSGKAAttVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:COG4619 171 ELlREYLAEEGRAV--LWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-221 |
2.40e-41 |
|
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: 144.62 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 24 DLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFG--- 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 101 -LKLSKLPKDQIEAqvaeAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISD 179
Cdd:TIGR01277 98 gLKLNAEQQEKVVD----AAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1540023143 180 LHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQV 221
Cdd:TIGR01277 174 LCSE-----RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-224 |
3.94e-41 |
|
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: 144.53 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSrgiAMVFQNYALYPHMTVKENLAFGL 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR---MVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 K--LSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRasmririSD 179
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR-------GN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 180 LHKQLKKSGKAA--TTVYVTHDQTEAMTMGDRICVM------KLGHIMQVDTP 224
Cdd:TIGR01184 153 LQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILEVPFP 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-218 |
4.02e-41 |
|
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: 142.54 E-value: 4.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNNLAPKSRGIAMVFQNY 85
Cdd:cd03230 4 RNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRIGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLafglklsklpkdqieaqvaeaakileledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03230 83 SLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 166 DAKLRASMRirisDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03230 127 DPESRREFW----ELLRELKKEGK--TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-235 |
2.34e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 142.84 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNgFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN---NLAPKS-----RG 77
Cdd:COG4161 5 LKNINCFYGS-HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirllrQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENL-AFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 157 LFDEPLSNLDAKLRAsmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMF 235
Cdd:COG4161 164 LFDEPTAALDPEITA----QVVEIIRELSQTG--ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQTEAF 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-235 |
5.43e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 141.69 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN---NLAPKS-----RGIAMVFQNYALYPH 90
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirelrRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFG-LKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL 169
Cdd:PRK11124 97 LTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 170 RAsmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMF 235
Cdd:PRK11124 177 TA----QIVSIIRELAETG--ITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEAF 236
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-210 |
5.53e-40 |
|
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: 140.83 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDrvVNNLAPKSR--------GIAMVFQNYALYPHMT 92
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNG--QETPPLNSKkaskfrreKLGYLFQNFALIENET 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAs 172
Cdd:TIGR03608 93 VEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD- 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1540023143 173 mriRISDLHKQLKKSGKaaTTVYVTHDqTEAMTMGDRI 210
Cdd:TIGR03608 172 ---EVLDLLLELNDEGK--TIIIVTHD-PEVAKQADRV 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
1.31e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.04 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS----- 75
Cdd:PRK11264 1 MSAIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 -----RGIAMVFQNYALYPHMTVKENLAFG-LKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAI 149
Cdd:PRK11264 80 irqlrQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 150 VKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKksgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYH 229
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR------TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
250
....*....|....*..
gi 1540023143 230 YP----TNMFVAGFIGA 242
Cdd:PRK11264 234 DPqqprTRQFLEKFLLQ 250
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
1.32e-39 |
|
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: 138.28 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYpHMTVKENLafglklsklpkdqieaqvaeaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 161 PLSNLDAKLRASmririsdLHKQLKKSGKAATTVYVTHDqTEAMTMGDRICVMKLGH 217
Cdd:cd03228 123 ATSALDPETEAL-------ILEALRALAKGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.59e-39 |
|
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: 137.78 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPHMTVKENL 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 AFGLKLSKLPKDQIEAQVAEAAK----ILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEklglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-228 |
4.19e-39 |
|
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: 139.36 E-value: 4.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAM 80
Cdd:TIGR02315 4 VENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENL---AFGLK------LSKLPKDQIEAQVAEAAKILELEDLLDRLpRQLSGGQAQRVAVGRAIVK 151
Cdd:TIGR02315 84 IFQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDKERALSALERVGLADKAYQRA-DQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 152 KPDVFLFDEPLSNLDAKlraSMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:TIGR02315 163 QPDLILADEPIASLDPK---TSKQVMDYLKRINKEDGI--TVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-229 |
5.25e-39 |
|
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: 146.06 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIA 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALyPHMTVKENLAFG------------LK-------LSKLPkDQIEAQVAEAAkileledlldrlpRQLSGGQA 140
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLGrpdasdeeleaaLEaagldefVAALP-DGLDTPLGEGG-------------RGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 141 QRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAsmriRISDLHKQLKKSgkaATTVYVTHDqTEAMTMGDRICVMKLGHIMQ 220
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEA----EILQALRRLAKG---RTVILITHR-LALLAQADRILVLDDGRIVE 551
|
....*....
gi 1540023143 221 VDTPDNLYH 229
Cdd:COG4988 552 QGTHEELLA 560
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-239 |
6.96e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 143.25 E-value: 6.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP------KSRGIAMVFQNYALYPHMT 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAS 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 173 MRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGF 239
Cdd:PRK10070 203 MQDELVKLQAKHQR-----TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-224 |
1.06e-38 |
|
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: 139.10 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFR-AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVN--NLAPKSRGIAMV 81
Cdd:TIGR04520 3 VENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDeeNLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNyalyPH-----MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:TIGR04520 83 FQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 157 LFDEPLSNLDAKLRAS-MRIrISDLHKQLKKsgkaaTTVYVTHDQTEAmTMGDRICVMKLGHIMQVDTP 224
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEvLET-IRKLNKEEGI-----TVISITHDMEEA-VLADRVIVMNKGKIVAEGTP 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-231 |
1.13e-38 |
|
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: 140.57 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE---TISDGEVRIGDRVVNNLAPK------SRGIAMVFQN-Y- 85
Cdd:COG0444 18 VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKelrkirGREIQMIFQDpMt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLAFGLKL-SKLPKDQIEAQVAEAAK---ILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:COG0444 98 SLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLErvgLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 162 LSNLDaklrASMRIRISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:COG0444 178 TTALD----VTIQAQILNLLKDLQRELGLA-ILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-224 |
1.74e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 138.27 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYsnGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRgiaMVFQNY 85
Cdd:PRK11247 16 NAVSKRY--GERTVlNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLAFGLKLSKLPK--DQIEA-QVAEAAKileledlldRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:PRK11247 91 RLLPWKKVIDNVGLGLKGQWRDAalQALAAvGLADRAN---------EWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 163 SNLDAKLRASMRIRISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHI---MQVDTP 224
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQ-----HGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLP 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-227 |
2.99e-38 |
|
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: 137.30 E-value: 2.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG-IAMVFQNY 85
Cdd:COG4555 5 ENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRqIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 166 DAklRASMRIRisDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:COG4555 164 DV--MARRLLR--EILRALKKEGK--TVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-227 |
4.07e-38 |
|
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: 136.10 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNGFR-AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDR-VVNNLAPKSRGIAMV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 162 LSNLDAKLRasmririSDLHKQLKKSGKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03263 161 TSGLDPASR-------RAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-217 |
5.76e-38 |
|
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: 133.91 E-value: 5.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQ 83
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 nyalyphmtvkenlafglklsklpkdqieaqvaeaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 164 NLDAKLRASMRIRISDLHKQlkksgkAATTVYVTHDQTEAMTMGDRICVMKLGH 217
Cdd:cd00267 110 GLDPASRERLLELLRELAEE------GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-227 |
9.64e-38 |
|
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: 136.33 E-value: 9.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYPHMT 92
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelARRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFG----LKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:COG1120 92 VRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 169 lrasMRIRISDLHKQL-KKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIM------QVDTPDNL 227
Cdd:COG1120 172 ----HQLEVLELLRRLaRERGR--TVVMVLHDLNLAARYADRLVLLKDGRIVaqgppeEVLTPELL 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-218 |
1.78e-37 |
|
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: 134.16 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 24 DLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGLKL 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 104 S-KLPKDQIEAqVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHK 182
Cdd:cd03298 98 GlKLTAEDRQA-IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1540023143 183 QLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03298 177 ETK-----MTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-199 |
2.24e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.76 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAG-LE---TISdGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKE 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSpafSAS-GEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLKlSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRi 175
Cdd:COG4136 96 NLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFR- 173
|
170 180
....*....|....*....|....
gi 1540023143 176 riSDLHKQLKKSGKAAttVYVTHD 199
Cdd:COG4136 174 --EFVFEQIRQRGIPA--LLVTHD 193
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-301 |
3.89e-37 |
|
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: 137.17 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNN------LAPKSRGIAMVFQNYALYPHMTVKEN 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKLPKDQI-EAQVAEAAKILELEDLLdrlPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRI 175
Cdd:TIGR02142 96 LRYGMKRARPSERRIsFERVIELLGIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 176 RISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPtNMFVAGFigAPEMNIKPSTLVEK 255
Cdd:TIGR02142 173 YLERLHAEFG-----IPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP-DLPWLAR--EDQGSLIEGVVAEH 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1540023143 256 EGQIGLT---VGQYTLVLNERQQAkvathTGEKVFFGVRPEFISMSLQP 301
Cdd:TIGR02142 245 DQHYGLTalrLGGGHLWVPENLGP-----TGARLRLRVPARDVSLALQK 288
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-228 |
6.63e-37 |
|
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: 134.50 E-value: 6.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNG----FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS---- 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 -RGIAMVFQnyalYPHM-----TVKENLAFGLKLSKLPKDQIEAQVAEAAKIL-ELEDLLDRLPRQLSGGQAQRVAVGRA 148
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVgLDEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 149 IVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGL-----TVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-231 |
1.10e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 135.63 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAMVFQN-YA-LYPH 90
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLKLSKL-PKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:COG4608 112 MTVGDIIAEPLRIHGLaSKAERRERVAELlELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 169 LRAS----MRirisDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:COG4608 192 IQAQvlnlLE----DLQDELG-----LTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-227 |
1.86e-36 |
|
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: 140.35 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYpHMTVKEN 96
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGlkLSKLPKDQIEaqvaEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:COG2274 569 ITLG--DPDATDEEII----EAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 166 DAKLRAsmriRISDlhkQLKKSGKAATTVYVTHDqTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:COG2274 643 DAETEA----IILE---NLRRLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-225 |
1.70e-35 |
|
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: 129.48 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNL------APKSRGIAMVFQNYALYPHMTVK 94
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedaraRLRARHVGFVFQSFQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEA-----QVAEAAKIleledllDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL 169
Cdd:COG4181 109 ENVMLPLELAGRRDARARAralleRVGLGHRL-------DHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 170 RAsmriRISDLHKQLKK-SGkaATTVYVTHDQTEAmTMGDRICVMKLGHIMQVDTPD 225
Cdd:COG4181 182 GE----QIIDLLFELNReRG--TTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-227 |
5.02e-35 |
|
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: 127.94 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMVFQNYALYPHMT 92
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGlkLSKLPKDQIEAQVAEAAKIleledlldrLPR----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:cd03224 92 VEENLLLG--AYARRRAKRKARLERVYEL---------FPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 163 SNLDAKLRAsmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03224 161 EGLAPKIVE----EIFEAIRELRDEG--VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-227 |
2.03e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 126.33 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNNLAPKSRGIAMVFQNYAL 87
Cdd:cd03265 6 LVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 168 KLRASMRIRISDLHKqlkksgKAATTVYV-THDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03265 165 QTRAHVWEYIEKLKE------EFGMTILLtTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-227 |
2.31e-34 |
|
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: 133.35 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYpHMTVKEN 96
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFG------------LK-------LSKLPkDQIEAQVAEAAkileledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:COG4987 429 LRLArpdatdeelwaaLErvglgdwLAALP-DGLDTWLGEGG-------------RRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 158 FDEPLSNLDAKLRASMrirISDLHKQLKksGKaaTTVYVTHDQTeAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:COG4987 495 LDEPTEGLDAATEQAL---LADLLEALA--GR--TVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-227 |
4.19e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 132.60 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYpH 90
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLKlsklpkDQIEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:COG1132 428 GTIRENIRYGRP------DATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 160 EPLSNLD----AKLRASMRirisdlhkQLKKsGKaaTTVYVTHDQTEAMTMgDRICVMKLGHIMQVDTPDNL 227
Cdd:COG1132 502 EATSALDteteALIQEALE--------RLMK-GR--TTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEEL 561
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-242 |
1.93e-33 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 124.94 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNgFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVN------NLAPKS- 75
Cdd:TIGR03005 1 VRFSDVTKRFGI-LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHmpgrngPLVPADe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 ------RG-IAMVFQNYALYPHMTVKENLAFGLKLSK-LPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGR 147
Cdd:TIGR03005 80 khlrqmRNkIGMVFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 148 AIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHD-----LTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEI 234
|
250
....*....|....*
gi 1540023143 228 YHYPTNMFVAGFIGA 242
Cdd:TIGR03005 235 FRQPKEERTREFLSK 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-227 |
2.49e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRvvnNLAPKSRGIAMVFQNYALYPH--MT 92
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYVPQRAEVDWDfpIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGL----KLSKLPKDQIEAQVAEA-----------AKIleledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:COG1121 94 VRDVVLMGRygrrGLFRRPSRADREAVDEAlervgledladRPI-----------GELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 158 FDEPLSNLDAKlrasMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIM-----QVDTPDNL 227
Cdd:COG1121 163 LDEPFAGVDAA----TEEALYELLRELRREGK--TILVVTHDLGAVREYFDRVLLLNRGLVAhgppeEVLTPENL 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
16-225 |
3.03e-33 |
|
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: 123.70 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP---KSRGIAMVFQNYALYPHMT 92
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQIPRLFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENL----------AFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:cd03219 92 VLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 163 SNLDAKLRAsmriRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPD 225
Cdd:cd03219 172 AGLNPEETE----ELAELIRELRERGI--TVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-206 |
3.20e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 124.43 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNnlAPKS-RGIamVFQNYALYPHMTVK 94
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAeRGV--VFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR 174
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|..
gi 1540023143 175 iriSDLHKQLKKSGKaaTTVYVTHDQTEAMTM 206
Cdd:PRK11248 169 ---TLLLKLWQETGK--QVLLITHDIEEAVFM 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-203 |
5.29e-33 |
|
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: 122.20 E-value: 5.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG-IAMVFQN 84
Cdd:COG4133 5 AENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFGLKLSKLPKDqiEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:COG4133 84 DGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540023143 165 LDAKLRAsmriRISDLHKQLKKSGKAAttVYVTHDQTEA 203
Cdd:COG4133 162 LDAAGVA----LLAELIAAHLARGGAV--LLTTHQPLEL 194
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-218 |
6.07e-33 |
|
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: 122.48 E-value: 6.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNNLAPKSRGIAMVFQNYALYPHMTVKE 95
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRRLGFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRi 175
Cdd:cd03266 98 NLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540023143 176 risDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03266 177 ---EFIRQLRALGK--CILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-218 |
7.36e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.98 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNlAPKSRGIAMVFQN--YALYPH 90
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQDvdYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 mTVKENLAFGLKLSKLPKDQIEAQVaeaaKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklR 170
Cdd:cd03226 88 -SVREELLLGLKELDAGNEQAETVL----KDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---Y 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540023143 171 ASMRiRISDLHKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03226 160 KNME-RVGELIRELAAQGKA--VIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-218 |
8.32e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.30 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFR---AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RG 77
Cdd:PRK11153 4 LKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 158 FDEPLSNLDAKLRASmrirISDLHKQL-KKSGkaATTVYVTHDqteamtMG------DRICVMKLGHI 218
Cdd:PRK11153 164 CDEATSALDPATTRS----ILELLKDInRELG--LTIVLITHE------MDvvkricDRVAVIDAGRL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-218 |
1.66e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 121.61 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 24 DLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGLKL 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 104 S-KLPKDQiEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDL-- 180
Cdd:PRK10771 99 GlKLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcq 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1540023143 181 HKQLkksgkaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:PRK10771 178 ERQL-------TLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-232 |
6.98e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.51 E-value: 6.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR-----GIAMVFQN--YALYPH 90
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLKL--SKLPKDQIEAQV-AEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 168 KLRAsmriRISDLHKQLKKSgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPT 232
Cdd:PRK15079 195 SIQA----QVVNLLQQLQRE-MGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-241 |
9.79e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 120.33 E-value: 9.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 11 KVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL-----ETISDGEVRIGDRvvNNLAPK------SRGIA 79
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGR--NIYSPDvdpievRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFGLKLSKL--PKDQIEAQV----AEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKP 153
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 154 DVFLFDEPLSNLDAKLRAsmriRISDLHKQLKKSgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP-- 231
Cdd:PRK14267 169 KILLMDEPTANIDPVGTA----KIEELLFELKKE---YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPeh 241
|
250
....*....|..
gi 1540023143 232 --TNMFVAGFIG 241
Cdd:PRK14267 242 elTEKYVTGALG 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-234 |
3.52e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVvnnLAPKS-----RGIAMVFQNyalyPH--- 90
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETvwdvrRQVGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 --MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:PRK13635 95 vgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 169 LRASMRIRISDLHKQlkksgKAATTVYVTHDQTEAMTmGDRICVMKLGHIMQVDTPDNLYHYPTNM 234
Cdd:PRK13635 175 GRREVLETVRQLKEQ-----KGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-220 |
6.12e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 118.37 E-value: 6.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSNG--FRA------VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS----- 75
Cdd:TIGR02769 8 VTHTYRTGglFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 RGIAMVFQNY--ALYPHMTVKENLAFGLK-LSKLPKDQIEAQVAEAAK-ILELEDLLDRLPRQLSGGQAQRVAVGRAIVK 151
Cdd:TIGR02769 88 RDVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDmVGLRSEDADKLPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 152 KPDVFLFDEPLSNLDAKLRASmrirISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKLGHIMQ 220
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAV----ILELLRKLQQAFGTA-YLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-218 |
2.01e-30 |
|
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: 114.45 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALyphmt 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKelARKIAYVPQALEL----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 vkenlafgLKLSKLpkdqieaqvaeAAKILeledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlras 172
Cdd:cd03214 85 --------LGLAHL-----------ADRPF----------NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA---- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1540023143 173 MRIRISDLHKQLKKS-GKaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03214 132 HQIELLELLRRLARErGK--TVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
4.22e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFR-AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN--NLAPKSRGIAMVF 82
Cdd:PRK13632 10 VENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 83 QNyalyPH-----MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:PRK13632 90 QN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 158 FDEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAmTMGDRICVMKLGHIMQVDTPD 225
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKK-----TLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-227 |
1.41e-29 |
|
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: 113.92 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMVFQNYALYPHMT 92
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKlPKDQIEAQVAEAAKILeledlldrlPR----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:COG0410 95 VEENLLLGAYARR-DRAEVRADLERVYELF---------PRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 163 SNLDAKLRAsmriRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:COG0410 165 LGLAPLIVE----EIFEIIRRLNREGV--TILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-218 |
1.57e-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: 119.02 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETiSDGEVRIGDRVVNNLAPKS-----RGIAMVFQN-YA-LYP 89
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HMTVKENLAFGLKL--SKLPKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:COG4172 378 RMTVGQIIAEGLRVhgPGLSAAERRARVAEAlEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 167 aklrASMRIRISDLHKQL-KKSGKAattvYV--THDQT--EAMTmgDRICVMKLGHI 218
Cdd:COG4172 458 ----VSVQAQILDLLRDLqREHGLA----YLfiSHDLAvvRALA--HRVMVMKDGKV 504
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-213 |
3.10e-29 |
|
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: 118.16 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAM 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHmTVKENLAFGLKlsklpkDQIEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAI 149
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP------DASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAF 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 150 VKKPDVFLFDEPLSNLDAKLRASMRIRISDLhkqlkksGKAATTVYVTHDqTEAMTMGDRICVM 213
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRAL-------AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-225 |
4.11e-29 |
|
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: 113.21 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQNYALYPHMT 92
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriaRLGIARTFQNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLA---------------FGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:COG0411 96 VLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 158 FDEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPD 225
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGI-----TILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-227 |
4.68e-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: 112.71 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNYALYpHMTVKENLAFGlKLSKLPKDQIEAqvAEAAKILELEDLLdrlPRQ-----------LSGGQAQRVAVGRAIV 150
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG-RPDATDEEVIEA--AKAAQIHDKIMRF---PDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 151 KKPDVFLFDEPLSNLDA-KLRASMRirisdlhkQLKKSGKAATTVYVTHDQTEAMTmGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03253 154 KNPPILLLDEATSALDThTEREIQA--------ALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-216 |
4.73e-29 |
|
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: 111.49 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL---ETISdGEVRIGDRVVNNLAPKSRgIA 79
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtgLGVS-GEVLINGRPLDKRSFRKI-IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFglklsklpkdqieaqvaeAAKIleledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMF------------------AAKL-----------RGLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 160 EPLSNLDaklrASMRIRISDLHKQLKKSGKaaTTVYVTHD-QTEAMTMGDRICVMKLG 216
Cdd:cd03213 137 EPTSGLD----SSSALQVMSLLRRLADTGR--TIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-231 |
9.57e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 112.20 E-value: 9.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNnLAPKSRG----------------IAMVFQN 84
Cdd:COG4598 25 KGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIR-LKPDRDGelvpadrrqlqrirtrLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFG-LKLSKLPKDQIEAQvAEA--AKILELEDLLDRlPRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:COG4598 104 FNLWSHMTVLENVIEApVHVLGRPKAEAIER-AEAllAKVGLADKRDAY-PAHLSGGQQQRAAIARALAMEPEVMLFDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 162 LSNLDAKLRAS----MRirisdlhkQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:COG4598 182 TSALDPELVGEvlkvMR--------DLAEEGR--TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-228 |
1.48e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.52 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVV-NNLAPKSRGIAMVFQNyalyPH-----MT 92
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTeENVWDIRHKIGMVFQN----PDnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAS 172
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 173 MRIRISDLHKQLKksgkaATTVYVTHDQTEaMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13650 179 LIKTIKGIRDDYQ-----MTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-227 |
2.58e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 12 VYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL-ETIS----DGEVRIGDRvvNNLAPKS------RGIAM 80
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGE--DIYDPDVdvvelrRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPhMTVKENLAFGLKLS-KLPKDQIEAQVAEAAkileledlldrlpRQ-----------------LSGGQAQR 142
Cdd:COG1117 97 VFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESL-------------RKaalwdevkdrlkksalgLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 143 VAVGRAIVKKPDVFLFDEPLSNLDAKlrASMriRISDLHKQLKKSgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVD 222
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPI--STA--KIEELILELKKD---YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
....*
gi 1540023143 223 TPDNL 227
Cdd:COG1117 236 PTEQI 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-218 |
5.81e-28 |
|
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: 107.51 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSnGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQny 85
Cdd:cd03216 6 ITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMVYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 alyphmtvkenlafglklsklpkdqieaqvaeaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 166 DAKLRASMRIRIsdlhKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03216 114 TPAEVERLFKVI----RRLRAQGVA--VIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-272 |
6.87e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.88 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNG--F--RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN------NLA 72
Cdd:PRK13634 2 DITFQKVEHRYQYKtpFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 73 PKSRGIAMVFQnyalYP-HM----TVKENLAFGLKLSKLPKDQIEAQVAEAAK-ILELEDLLDRLPRQLSGGQAQRVAVG 146
Cdd:PRK13634 82 PLRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIElVGLPEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 147 RAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDN 226
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKE-----KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1540023143 227 LYHYPTNMFVAGfIGAPEmNIKPSTLVEKegQIGLTVGQYTLVLNE 272
Cdd:PRK13634 233 IFADPDELEAIG-LDLPE-TVKFKRALEE--KFGISFPKPCLTLEE 274
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-220 |
8.97e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.16 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAMVFQNY--ALYPHMT 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLK-LSKLPKDQIEAQVAEAAK-ILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLR 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRaVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540023143 171 ASMrirISDLHKQLKKSGKAAttVYVTHDQTEAMTMGDRICVMKLGHIMQ 220
Cdd:PRK10419 188 AGV---IRLLKKLQQQFGTAC--LFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-210 |
9.72e-28 |
|
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: 108.39 E-value: 9.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRvvnNLAPKSRGIAMVFQNYAL---YPhM 91
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 TVKENLAFGL-----KLSKLPKDQIEAqVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:cd03235 86 SVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540023143 167 AKlrasMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRI 210
Cdd:cd03235 165 PK----TQEDIYELLRELRREGM--TILVVTHDLGLVLEYFDRV 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-218 |
1.42e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-----RGIAM 80
Cdd:PRK10908 4 FEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 161 PLSNLDAKLRASmrirISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:PRK10908 164 PTGNLDDALSEG----ILRLFEEFNRVG--VTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-214 |
1.86e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQNYALYPHMT 92
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqAAGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSKLP---KDQIEAQVAEA-----------AKIleledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLF 158
Cdd:COG1129 96 VAENIFLGREPRRGGlidWRAMRRRARELlarlgldidpdTPV-----------GDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 159 DEPLSNLDAK----LRASMRirisdlhkQLKKSGKAatTVYVTHDQTEAMTMGDRICVMK 214
Cdd:COG1129 165 DEPTASLTEReverLFRIIR--------RLKAQGVA--IIYISHRLDEVFEIADRVTVLR 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-239 |
2.69e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.03 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVV-NNLAPKSRGIAMVFQNY-ALYPHMTVKEN 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTaENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIR 176
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 177 ISDLhkqlkKSGKAATTVYVTHDQTEAMTmGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGF 239
Cdd:PRK13642 183 IHEI-----KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-231 |
2.89e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.52 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVV---------------NNLAPKSRGIAMVFQNYA 86
Cdd:PRK10619 23 GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadkNQLRLLRTRLTMVFQHFN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPHMTVKENLAFG----LKLSKlpKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:PRK10619 103 LWSHMTVLENVMEApiqvLGLSK--QEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 163 SNLDAKLRASMrIRISdlhKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:PRK10619 181 SALDPELVGEV-LRIM---QQLAEEGK--TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-218 |
3.85e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.25 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKlGKVysNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP--KSRGIAMV 81
Cdd:COG1101 9 KTFNP-GTV--NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykRAKYIGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNYAL--YPHMTVKENLA--------FGLKLSKLPK--DQIEAQVAE---------AAKILeledlldrlprQLSGGQA 140
Cdd:COG1101 86 FQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKrrELFRELLATlglglenrlDTKVG-----------LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 141 QRVAVGRAIVKKPDVFLFDEPLSNLDAKlRASmriRISDLHKQLKKSGKaATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPK-TAA---LVLELTEKIVEENN-LTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-228 |
4.06e-27 |
|
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: 107.24 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPhMTVKENLAF 99
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLKlsklpkDQIEAQVAEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:cd03249 100 GKP------DATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 169 lraSMRIrisdLHKQLKKSGKAATTVYVTHDQTEAMTMgDRICVMKLGHIMQVDTPDNLY 228
Cdd:cd03249 174 ---SEKL----VQEALDRAMKGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-238 |
6.95e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL-----ETISDGEVRIGDRVV--NNLAPKSRGIAMVFQNYALYPHMTVK 94
Cdd:PRK14247 21 GVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRRVQMVFQIPNPIPNLSIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEAQ-----VAEAAKILELEDLLDRLPR-QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:PRK14247 101 ENVALGLKLNRLVKSKKELQervrwALEKAQLWDEVKDRLDAPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 169 LRAsmriRISDLHKQLKKSgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP----TNMFVAG 238
Cdd:PRK14247 181 NTA----KIESLFLELKKD---MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhelTEKYVTG 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-220 |
1.26e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.05 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYSNG---FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP------KSRG 77
Cdd:PRK11629 9 DNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 158 FDEPLSNLDAKLRASmrirISDLHKQLKKSGKAATTVyVTHDQTEAMTMgDRICVMKLGHIMQ 220
Cdd:PRK11629 169 ADEPTGNLDARNADS----IFQLLGELNRLQGTAFLV-VTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-218 |
1.75e-26 |
|
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: 105.36 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYpHMTVKEN 96
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKlpkdqiEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03245 98 ITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 166 DakLRASMRIRisdlhKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHI 218
Cdd:cd03245 172 D--MNSEERLK-----ERLRQLLGDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-218 |
2.22e-26 |
|
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: 104.61 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYSNGfRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGIAMVFQNYA 86
Cdd:cd03268 4 NDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPHMTVKENLAFGLKLSKLPKDQIEaqvaEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 167 AKLRASMRIRISDlhkqLKKSGKaatTVYV-THDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03268 159 PDGIKELRELILS----LRDQGI---TVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-228 |
3.45e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN--NLAPKSRGIAMVFQNyalyPH-----MTVKE 95
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRKHIGIVFQN----PDnqfvgSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMri 175
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL-- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 176 riSDLHKQLkKSGKAATTVYVTHDQTEAMTmGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13648 182 --LDLVRKV-KSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-228 |
4.62e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.54 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN----NLAPKSRGIAMVFQN---- 84
Cdd:PRK13639 11 YPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 -YAlyPhmTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:PRK13639 91 lFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 164 NLDAkLRASmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13639 167 GLDP-MGAS---QIMKLLYDLNKEG--ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-218 |
4.92e-26 |
|
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: 103.81 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSNGfRAVHGIDLKINDGEFmVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG-IAMVFQNYAL 87
Cdd:cd03264 6 LTKRYGKK-RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:cd03264 84 YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 168 KLRASMRIRISDLhkqlkksGKAATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03264 164 EERIRFRNLLSEL-------GEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-251 |
5.87e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNN------LAPKSRGIAMVFQnyalYPHM 91
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVRKKVGVVFQ----FPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 -----TVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLL-DRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:PRK13643 96 qlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 166 DAKlrasMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYptnmfvAGFIGAPEM 245
Cdd:PRK13643 176 DPK----ARIEMMQLFESIHQSGQ--TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE------VDFLKAHEL 243
|
....*.
gi 1540023143 246 NIKPST 251
Cdd:PRK13643 244 GVPKAT 249
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-219 |
6.06e-26 |
|
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: 109.57 E-value: 6.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYpHMTVKEN 96
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGlklSKLPKDQieaQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:TIGR03375 559 IALG---APYADDE---EILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 166 DAklRASMRIRisdlhKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIM 219
Cdd:TIGR03375 633 DN--RSEERFK-----DRLKRWLAGKTLVLVTH-RTSLLDLVDRIIVMDNGRIV 678
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-232 |
8.39e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-----GDrvVNNLAPKSRGIAMVFQN-YA 86
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGD--FSKLQGIRKLVGIVFQNpET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK13644 89 QFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 167 AKLRASMRIRISDLHKqlkksgKAATTVYVTHDqTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPT 232
Cdd:PRK13644 169 PDSGIAVLERIKKLHE------KGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-228 |
1.14e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDrvVN------NLAPKSRGIAMVFQ--NYALYP 89
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDitdkkvKLSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HmTVKENLAFGLKLSKLPKDQIEAQVAEAAKIL--ELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 168 KLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13637 178 KGRDEILNKIKELHKEYN-----MTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-222 |
2.00e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 105.34 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 35 IVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN------NLAPKSRGIAMVFQNYALYPHMTVKENLAFGLKlsklPK 108
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----KS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 109 DQieAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA-----------KLRASMRIRI 177
Cdd:PRK11144 105 MV--AQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrellpyleRLAREINIPI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540023143 178 sdlhkqlkksgkaattVYVTHDQTEAMTMGDRICVMKLGHIMQVD 222
Cdd:PRK11144 183 ----------------LYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-227 |
4.26e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.43 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGE--VRIGDRVVN--NLAPKSRG-----IAMVFQNYALY 88
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmtKPGPDGRGrakryIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 89 PHMTVKENL--AFGLKLSK---LPKDQIEAQVA-----EAAKILELEdlldrlPRQLSGGQAQRVAVGRAIVKKPDVFLF 158
Cdd:TIGR03269 378 PHRTVLDNLteAIGLELPDelaRMKAVITLKMVgfdeeKAEEILDKY------PDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 159 DEPLSNLDAKLRASMRIRISDLHKQLKKsgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEMEQ-----TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-231 |
4.41e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNnlAPKS------RGIAMVFQN-YA-LY 88
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLK--ADPEaqkllrQKIQIVFQNpYGsLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 89 PHMTVKENLAFGLKL-SKLPKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK11308 107 PRKKVGQILEEPLLInTSLSAAERREKALAMmAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 167 AKLRASMRIRISDLHKQLKKSgkaatTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLS-----YVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
5.21e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFNKLGKVYSNGFrAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GI 78
Cdd:PRK13537 6 APIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 79 AMVFQNyaLYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLF 158
Cdd:PRK13537 85 VPQFDN--LDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 159 DEPLSNLDAKLRASMRIRIsdlhKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERL----RSLLARGK--TILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-219 |
6.53e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.51 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS-RG-IAMVFQNyalyPH 90
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQD----PD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 -----MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:PRK13647 90 dqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 166 DAKLRASMRIRISDLHKQlkksGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIM 219
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQ----GK--TVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-216 |
7.18e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 11 KVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQNYAL 87
Cdd:COG3845 13 KRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaiALGIGMVHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGL---KLSKLPKDQIEAQVAE-----------AAKIleledlldrlpRQLSGGQAQRVAVGRAIVKKP 153
Cdd:COG3845 92 VPNLTVAENIVLGLeptKGGRLDRKAARARIRElserygldvdpDAKV-----------EDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 154 DVFLFDEPLSNLD----AKLRASMRirisdlhkQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:COG3845 161 RILILDEPTAVLTpqeaDELFEILR--------RLAAEGK--SIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-218 |
1.57e-24 |
|
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: 98.44 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG--IAMVFQNYALYPHmTVKENLaf 99
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDELFSG-SIAENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 glklsklpkdqieaqvaeaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAsmriRISD 179
Cdd:cd03246 97 -----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER----ALNQ 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540023143 180 LHKQLKKSGkaATTVYVTHdQTEAMTMGDRICVMKLGHI 218
Cdd:cd03246 138 AIAALKAAG--ATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-219 |
2.71e-24 |
|
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: 104.00 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTT----LRMLAGLETISDGEVRIGDRVVNNLAPKS----RG--IAMVFQN-- 84
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFGLKLSK-LPKDQIEAQVAEA---AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:COG4172 103 TSLNPLHTIGKQIAEVLRLHRgLSGAAARARALELlerVGIPDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 161 PLSNLDAKLRAsmriRISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKLGHIM 219
Cdd:COG4172 183 PTTALDVTVQA----QILDLLKDLQRELGMA-LLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-278 |
4.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGD---RVVNNLAPKSRGIAMVFQNyalyPH----- 90
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLR 170
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 171 ASMRIRISDLHkqlKKSGkaATTVYVTHDQTEAMTmGDRICVMKLGHIMQVDTPDNLYhyptnmfvagfigapemnikps 250
Cdd:PRK13633 181 REVVNTIKELN---KKYG--ITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF---------------------- 232
|
250 260
....*....|....*....|....*...
gi 1540023143 251 TLVEKEGQIGLTVGQYTLVLNERQQAKV 278
Cdd:PRK13633 233 KEVEMMKKIGLDVPQVTELAYELKKEGV 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-203 |
4.16e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNL------APKSRGIAMVFQNYALYPHMTVKE 95
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeearaKLRAKHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAsmri 175
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD---- 183
|
170 180
....*....|....*....|....*...
gi 1540023143 176 RISDLHKQLKKSgKAATTVYVTHDQTEA 203
Cdd:PRK10584 184 KIADLLFSLNRE-HGTTLILVTHDLQLA 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-218 |
6.46e-23 |
|
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: 94.42 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMV---FQNYALYPHM 91
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 TVKENLAFglklsklpkdqieaqvaeaakileledlldrlPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRA 171
Cdd:cd03215 94 SVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1540023143 172 SMRIRISDlhkqLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03215 142 EIYRLIRE----LADAGKA--VLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-233 |
7.15e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 7.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETIsDGEVRIGDRVV----------NNLAPKSRGIAMVFQNYAL 87
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVEffnqniyerrVNLNRLRRQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPhMTVKENLAFGLKL----SKLPKDQI-EAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:PRK14258 100 FP-MSVYDNVAYGVKIvgwrPKLEIDDIvESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 163 SNLDAKlrASMRIRiSDLHKQLKKSgkAATTVYVTHDQTEAMTMGDRICVMK-----LGHIMQVDTPDNLYHYPTN 233
Cdd:PRK14258 179 FGLDPI--ASMKVE-SLIQSLRLRS--ELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHD 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-216 |
7.24e-23 |
|
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: 95.04 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLA-------PKSRGiamvfqnyaLYPH 90
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG---------LYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAklr 170
Cdd:cd03269 85 MKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP--- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540023143 171 ASMRIrISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:cd03269 162 VNVEL-LKDVIRELARAGK--TVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
1.04e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.85 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVI-FNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLET---ISDGEVRIGDRVVNNLAPKSR 76
Cdd:PRK09984 1 MQTIIrVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 77 GI-------AMVFQNYALYPHMTVKENLAFGlKLSKLPK--------DQIEAQVA-EAAKILELEDLLDRLPRQLSGGQA 140
Cdd:PRK09984 80 DIrksrantGYIFQQFNLVNRLSVLENVLIG-ALGSTPFwrtcfswfTREQKQRAlQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 141 QRVAVGRAIVKKPDVFLFDEPLSNLDAKlraSMRIRISDLHKQLKKSGkaaTTVYVTHDQTE-AMTMGDRICVMKLGHI 218
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPE---SARIVMDTLRDINQNDG---ITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-228 |
1.38e-22 |
|
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: 94.99 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYpHMTVKEN 96
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKlsklpkDQIEAQVAEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03251 96 IAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 166 DakLRASMRIRisdlhKQLKKSGKAATTVYVTHDQTeAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:cd03251 170 D--TESERLVQ-----AALERLMKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-220 |
1.96e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLetIS-DGEVRIGDRVVNNLAPKS--RGIAMVFQNYALyPHMTVKENLAF 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLklSKLPKDQIEaQVAEAAKILELEdlldrlPRQ--------------LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:PRK11174 446 GN--PDASDEQLQ-QALENAWVSEFL------PLLpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 166 DAKL-RASMRirisdlhkQLKKSGKAATTVYVTH--DQTEAMtmgDRICVMKLGHIMQ 220
Cdd:PRK11174 517 DAHSeQLVMQ--------ALNAASRRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQ 563
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-204 |
2.80e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDrvvnnlapkSRGIAMVFQNYAL---YPhM 91
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 TVKENLAFGL----KLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:NF040873 73 TVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1540023143 168 KLRAsmriRISDLHKQLKKSGkaATTVYVTHDQTEAM 204
Cdd:NF040873 153 ESRE----RIIALLAEEHARG--ATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-228 |
3.74e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNG----FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNN------LAP 73
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 74 KSRGIAMVFQnyalYPHM-----TVKENLAFGLKLSKLPKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGR 147
Cdd:PRK13646 83 VRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLlMDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 148 AIVKKPDVFLFDEPLSNLDAKlrasMRIRISDLHKQLK-KSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDN 226
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQ----SKRQVMRLLKSLQtDENK--TIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
..
gi 1540023143 227 LY 228
Cdd:PRK13646 233 LF 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-228 |
8.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNN------LAPKSRGIAMVFQnyalYPHM 91
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 -----TVKENLAFGLKLSKLPKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:PRK13649 97 qlfeeTVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 166 DAKLRASMRirisDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13649 177 DPKGRKELM----TLFKKLHQSG--MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-225 |
1.91e-21 |
|
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: 95.59 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG--IAMVFQNYALYPHmTVKENL 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 A-FGlklsklpkDQIEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:COG4618 427 ArFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 166 D----AKLRASMRirisdlhkQLKKSGkaATTVYVTHDQTeAMTMGDRICVMKLGHIMQVDTPD 225
Cdd:COG4618 499 DdegeAALAAAIR--------ALKARG--ATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-241 |
2.07e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.54 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 12 VYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETI-----SDGEVRIGDRvvNNLAPK------SRGIAM 80
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGK--NLYAPDvdpvevRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYPHmTVKENLAFGLKLSKLPKDQ---IEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:PRK14243 96 VFQKPNPFPK-SIYDNIAYGARINGYKGDMdelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 158 FDEPLSNLDaklrASMRIRISDLHKQLKKSgkaATTVYVTHDQTEAMTMGDRICVM---------KLGHIMQVDTPDNLY 228
Cdd:PRK14243 175 MDEPCSALD----PISTLRIEELMHELKEQ---YTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIF 247
|
250
....*....|....*..
gi 1540023143 229 HYP----TNMFVAGFIG 241
Cdd:PRK14243 248 NSPqqqaTRDYVSGRFG 264
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-225 |
2.13e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYPHMTVKE 95
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlARRLALLPQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGL--------KLSklPKDQieAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDa 167
Cdd:PRK11231 96 LVAYGRspwlslwgRLS--AEDN--ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 168 klrASMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPD 225
Cdd:PRK11231 171 ---INHQVELMRLMRELNTQGK--TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-218 |
2.83e-21 |
|
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: 95.11 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRG--IAMVFQNYALYPHmTVKENL 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 A-FGlklsklpkDQIEAQ-VAEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:TIGR01842 413 ArFG--------ENADPEkIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 165 LDAKLRASMRIRIsdlhKQLKKSGkaATTVYVTHdQTEAMTMGDRICVMKLGHI 218
Cdd:TIGR01842 485 LDEEGEQALANAI----KALKARG--ITVVVITH-RPSLLGCVDKILVLQDGRI 531
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-227 |
4.59e-21 |
|
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: 90.75 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIA 79
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHmTVKENLAFGLKLSKlpkdqiEAQVAEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRA 148
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 149 IVKKPDVFLFDEPLSNLDAKLRAsmririsDLHKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEK-------LIQEALEKLMKGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-241 |
4.98e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.99 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 12 VYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDgEVRIGDRVVNN----LAPKS------RGIAMV 81
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYNghniYSPRTdtvdlrKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNYALYPhMTVKENLAFGLKLSKLpKDQ------IEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGI-KDKqvldeaVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 156 FLFDEPLSNLDAkLRASmriRISDLHKQLKKSgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP---- 231
Cdd:PRK14239 170 ILLDEPTSALDP-ISAG---KIEETLLGLKDD---YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPkhke 242
|
250
....*....|
gi 1540023143 232 TNMFVAGFIG 241
Cdd:PRK14239 243 TEDYISGKFG 252
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-240 |
8.97e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFN-KLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN--------NLA 72
Cdd:PRK14246 7 AEDVFNiSRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 73 PKSRGIAMVFQNYALYPHMTVKENLAF-----GLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGR 147
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFPHLSIYDNIAYplkshGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 148 AIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLkksgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI-------AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|...
gi 1540023143 228 YHYPTNMFVAGFI 240
Cdd:PRK14246 240 FTSPKNELTEKYV 252
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-218 |
9.04e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYSNgFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVR-----IGDRVVNNLA--PKSRGia 79
Cdd:COG4152 5 KGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepLDPEDRRRIGylPEERG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 mvfqnyaLYPHMTVKENLAFGLKLSKLPKDQIEAQVAE-----------AAKIleledlldrlpRQLSGGQAQRVAVGRA 148
Cdd:COG4152 82 -------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEwlerlglgdraNKKV-----------EELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 149 IVKKPDVFLFDEPLSNLD---AKLrasmrirISDLHKQLKKSGKaaTTVYVTH--DQTEAMTmgDRICVMKLGHI 218
Cdd:COG4152 144 LLHDPELLILDEPFSGLDpvnVEL-------LKDVIRELAAKGT--TVIFSSHqmELVEELC--DRIVIINKGRK 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
10-231 |
1.01e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 10 GKVYSNGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDrvvnNLAPKSRG--------IA 79
Cdd:PRK11831 12 GVSFTRGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGE----NIPAMSRSrlytvrkrMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFGLKL-SKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLF 158
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 159 DEPLSNLDAKLRASMRIRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAL-----GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-219 |
1.22e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.64 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGI------AMVFQNYALYPHMTVKE 95
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL-RASMR 174
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgEEVMA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540023143 175 IRisdlhKQLKKSGKaaTTVYVTHDQTEAmTMGDRICVMKLGHIM 219
Cdd:PRK10535 186 IL-----HQLRDRGH--TVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-199 |
1.73e-20 |
|
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: 92.81 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNyalyPH 90
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQD----AH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 M---TVKENLAFGlklsklPKDQIEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:TIGR02868 420 LfdtTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPIL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540023143 157 LFDEPLSNLDAKLRASMrirISDLHKQLkkSGKaaTTVYVTHD 199
Cdd:TIGR02868 494 LLDEPTEHLDAETADEL---LEDLLAAL--SGR--TVVLITHH 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-161 |
3.05e-20 |
|
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: 88.35 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMVFQNYALYPHMTVKE 95
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 96 NLAFGLKLSKLPKDQIEAQVAEAAKILELEDLldrlpRQ---LSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:TIGR03410 95 NLLTGLAALPRRSRKIPDEIYELFPVLKEMLG-----RRggdLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-251 |
3.19e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.06 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYPHMTVKE 95
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaaSRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLK--LSKL-PKDQIEAQVAEAAKILELEDLLDRLP-RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklrA 171
Cdd:PRK09536 97 VVEMGRTphRSRFdTWTETDRAAVERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLD----I 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 172 SMRIRISDLHKQLKKSGKAAttVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTnmFVAGFIGAPEMNIKPST 251
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTA--VAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT--LRAAFDARTAVGTDPAT 248
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-242 |
4.56e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.78 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL---ETISDGEVRIGDRVVNNLAPK------SRGIAMVFQN--YAL 87
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKelnklrAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGLKLSK-LPKDQ-IEAQVA--EAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKgMSKAEaFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 164 NLDAKLRAsmriRISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGFIGA 242
Cdd:PRK09473 191 ALDVTVQA----QIMTLLNELKREFNTA-IIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-168 |
4.67e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.03 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK-SRGIAMVFQNYALYPHMTV 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 94 KENLAFGLKLSKLPKDQIEAQVAEAAkileLEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-225 |
6.22e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 5 IFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLapksrGIAMVFQn 84
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 yalyPHMTVKENLAFGLKLSKLPKDQIEAQVAEAA-------KIleledlldRLP-RQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:COG1134 101 ----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVefaelgdFI--------DQPvKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 157 LFDEPLSNLDA--KLRASMRIRisdlhkQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPD 225
Cdd:COG1134 169 LVDEVLAVGDAafQKKCLARIR------ELRESGR--TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-239 |
9.31e-20 |
|
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: 90.79 E-value: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN--NLAPKSRGIAMVFQNYALYPHmT 92
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-S 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKLSklpkdQIEAQvaEAAKILELEDLLDRLPRQ-----------LSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:TIGR03797 543 IFENIAGGAPLT-----LDEAW--EAARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 162 LSNLDAKLRASmrirISDLHKQLKksgkaATTVYVTHDQTEAMTmGDRICVMKLGHIMQVDTPDNLyhyptnMFVAGF 239
Cdd:TIGR03797 616 TSALDNRTQAI----VSESLERLK-----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL------MAREGL 677
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-219 |
1.09e-19 |
|
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: 87.00 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK-SRGIAMVF-QNYALYPHMTVKE 95
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRI 175
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540023143 176 RISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIM 219
Cdd:cd03267 195 FLKEYNRE-----RGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-228 |
1.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.58 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSNGF----RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN------NLAPKS 75
Cdd:PRK13641 5 FENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 RGIAMVFQnyalYPHM-----TVKENLAFGLKLSKLPKDQIEAQVAE-AAKILELEDLLDRLPRQLSGGQAQRVAVGRAI 149
Cdd:PRK13641 85 KKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 150 VKKPDVFLFDEPLSNLDAKLRASMririSDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM----MQLFKDYQKAGH--TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-231 |
1.55e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP----KSRgiAMVFQNYAL 87
Cdd:PRK13548 10 VRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaelaRRR--AVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 -YPhMTVKENLAFGL---KLSKLPKDQIEAQVAEAAKILELEDLLDrlpRQLSGGQAQRVAVGRAIV------KKPDVFL 157
Cdd:PRK13548 88 sFP-FTVEEVVAMGRaphGLSRAEDDALVAAALAQVDLAHLAGRDY---PQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 158 FDEPLSNLDakLRasMRIRISDLHKQLKKSGKAATTVyVTHDQTEAMTMGDRICVMKLGHIM------QVDTPDNL---Y 228
Cdd:PRK13548 164 LDEPTSALD--LA--HQHHVLRLARQLAHERGLAVIV-VLHDLNLAARYADRIVLLHQGRLVadgtpaEVLTPETLrrvY 238
|
...
gi 1540023143 229 HYP 231
Cdd:PRK13548 239 GAD 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-228 |
1.68e-19 |
|
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: 86.44 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 8 KLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMVFQN 84
Cdd:cd03218 5 NLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 165 LDAklrasmrIRISDLH---KQLKKSGkaaTTVYVT-HDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:cd03218 164 VDP-------IAVQDIQkiiKILKDRG---IGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-227 |
2.48e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYsNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNL---APKSRG 77
Cdd:PRK10895 1 MATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 IAMVFQNYALYPHMTVKENLAFGLKLSK-LPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 157 LFDEPLSNLDAklrasmrIRISDLHKQLKKSGKAATTVYVT-HDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:PRK10895 160 LLDEPFAGVDP-------ISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-227 |
2.50e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVifNKLGKVYSNGfRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGI 78
Cdd:COG4604 1 MIEI--KNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 79 AMVFQNYALYPHMTVKENLAFGL------KLSKlpKDqiEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKK 152
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFGRfpyskgRLTA--ED--REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 153 PDVFLFDEPLSNLDAKL-RASMRIrisdLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHsVQMMKL----LRRLADELGK--TVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-216 |
2.50e-19 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 85.21 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRvvnnlapksrgIAMVFQNyALYPHMTVKE 95
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGLK------------------LSKLPK-DQIEaqVAEaakileledlldrlpR--QLSGGQAQRVAVGRAIVKKPD 154
Cdd:cd03250 85 NILFGKPfdeeryekvikacalepdLEILPDgDLTE--IGE---------------KgiNLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 155 VFLFDEPLSNLDAKLRAsmRIrISDLHKQLKKSGKaaTTVYVTHdQTEAMTMGDRICVMKLG 216
Cdd:cd03250 148 IYLLDDPLSAVDAHVGR--HI-FENCILGLLLNNK--TRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-218 |
2.87e-19 |
|
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: 85.28 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVnnlapksrgiAMVFQNYALYPHMTVKEN 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIR 176
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1540023143 177 ISDLHKQlkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03220 185 LRELLKQ------GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-232 |
5.67e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 5.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL---------ETISDGeVRIGDRVVNNLAPKsrgIAMVFQNyalyP 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnsKITVDG-ITLTAKTVWDIREK---VGIVFQN----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 H-----MTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:PRK13640 94 DnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 165 LDaklrASMRIRISDLHKQLKKSgKAATTVYVTHDQTEAmTMGDRICVMKLGHIMQVDTPDNLYHYPT 232
Cdd:PRK13640 174 LD----PAGKEQILKLIRKLKKK-NNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-277 |
6.64e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN----NLAPKSRGIAMVFQ--NYA 86
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLRESVGMVFQdpDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPhMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK13636 95 LFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 167 AKlrasmriRISDLHKQLKKSGK--AATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHyPTNMFVAGFIGAPE 244
Cdd:PRK13636 174 PM-------GVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA-EKEMLRKVNLRLPR 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 1540023143 245 MNIKPSTLVEKEG----QIGLTVGQYTLVLNERQQAK 277
Cdd:PRK13636 246 IGHLMEILKEKDGfvfdELDLTISQARKTLNSWKNKI 282
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-227 |
8.62e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.26 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVV--NNLAPKSRGIAMVfQNYALYPHMTVK 94
Cdd:NF033858 279 FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRVGYMS-QAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQR--VAVgrAIVKKPDVFLFDEPLSNLDAKLRAS 172
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlsLAV--AVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 173 M-RIRIsDLhkqlkkSGKAATTVYV-THDQTEAMTMgDRICVMKLGHIMQVDTPDNL 227
Cdd:NF033858 436 FwRLLI-EL------SREDGVTIFIsTHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-228 |
9.86e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 9.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNG----FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGD-------RVVNNL 71
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 72 APKSRGIAMVFQ--NYALYPHmTVKENLAFGLKLSKLPKDQIEAQVAEAAK-ILELEDLLDRLPRQLSGGQAQRVAVGRA 148
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 149 IVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKKSgkaatTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLY 228
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKR-----IIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-228 |
1.58e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYsNGFRAVHGIDLKINDGEfmvIV---GPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GI---- 78
Cdd:COG1137 9 LVKSY-GKRTVVKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIgylp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 79 --AMVFQNyalyphMTVKENLAFGLKLSKLPKDQIEAQVAEA------AKILELEDLldrlprQLSGGQAQRVAVGRAIV 150
Cdd:COG1137 85 qeASIFRK------LTVEDNILAVLELRKLSKKEREERLEELleefgiTHLRKSKAY------SLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 151 KKPDVFLFDEPLSNLDAklrasmrIRISDLHK---QLKKSGKAattVYVT-HDQTEAMTMGDRICVMKLGHIMQVDTPDN 226
Cdd:COG1137 153 TNPKFILLDEPFAGVDP-------IAVADIQKiirHLKERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
..
gi 1540023143 227 LY 228
Cdd:COG1137 223 IL 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-227 |
1.72e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR-GIAMVFQNYALYPHMTVKENLA 98
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQFDNLDLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 99 FGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRIs 178
Cdd:PRK13536 137 VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL- 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540023143 179 dlhKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:PRK13536 216 ---RSLLARGK--TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
2.01e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIFNKLGKVYSNgFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLaPKSR---- 76
Cdd:PRK11614 3 KVMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAKimre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 77 GIAMVFQNYALYPHMTVKENLAFGLKLSKlpKDQIEAQVAEAAKIL-ELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 156 FLFDEPlsnlDAKLRASMRIRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:PRK11614 159 LLLDEP----SLGLAPIIIQQIFDTIEQLREQG--MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-224 |
2.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 14 SNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGD----------RVVNNLAPKS-------- 75
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSKKiknfkelr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 RGIAMVFQ--NYALYPHmTVKENLAFG---LKLSKLPKDQIEAQVAEaaKILELEDLLDRLPRQLSGGQAQRVAVGRAIV 150
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLN--KMGLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 151 KKPDVFLFDEPLSNLDAKLRASMririSDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTP 224
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEM----MQLILDAKANNK--TVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-227 |
3.46e-18 |
|
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: 82.83 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDG-EVRIGDRV-----VNNLAPKsrgIAMV---FQNYaLYPH 90
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedVWELRKR---IGLVspaLQLR-FPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 MTVKENLAFGLK----LSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:COG1119 95 ETVLDVVLSGFFdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 167 AKLRASMRIRISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIM------QVDTPDNL 227
Cdd:COG1119 175 LGARELLLALLDKLAAE-----GAPTLVLVTHHVEEIPPGITHVLLLKDGRVVaagpkeEVLTSENL 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-242 |
4.57e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIG-------DRVVNNLAPKS-------RG--IAM 80
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIELSEQSaaqmrhvRGadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQN--YALYPHMTVKENLAFGLKLSK-LPKDQIEAQ---VAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPD 154
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEakrMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 155 VFLFDEPLSNLDAKLRASMRIRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNM 234
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEM-----SMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....*...
gi 1540023143 235 FVAGFIGA 242
Cdd:PRK10261 264 YTRALLAA 271
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-202 |
5.56e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRA-----VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALY 88
Cdd:PRK10247 14 GYLAgdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 89 PHmTVKENLAFGLKLSKLPKDQiEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDak 168
Cdd:PRK10247 94 GD-TVYDNLIFPWQIRNQQPDP-AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD-- 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1540023143 169 lrASMRIRISDL-HKQLKKSGKAAttVYVTHDQTE 202
Cdd:PRK10247 170 --ESNKHNVNEIiHRYVREQNIAV--LWVTHDKDE 200
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-231 |
6.79e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.93 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVN-NLAPKSRGIAMVFQN-- 84
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKeNIREVRKFVGLVFQNpd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 -YALYPhmTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:PRK13652 89 dQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 164 NLDAKLRASMRIRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETY-----GMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-199 |
7.17e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 7.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTT----LRMLAgletiSDGEVRIGDRVVNNLAPKS-----RGIAMVFQ--NYAL 87
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGLKL--SKLPKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVmEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190
....*....|....*....|....*....|....*
gi 1540023143 165 LDAKLRAsmriRISDLHKQLKKSGKAAtTVYVTHD 199
Cdd:PRK15134 456 LDKTVQA----QILALLKSLQQKHQLA-YLFISHD 485
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-224 |
7.89e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYPHMTVKENLA 98
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 99 FGlKLSKLP-----KDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASM 173
Cdd:PRK10253 104 RG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 174 RIRISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTP 224
Cdd:PRK10253 183 LELLSELNRE-----KGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
23-227 |
8.45e-18 |
|
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: 85.18 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPHmTVKENLAfg 100
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWlrRQMGVVLQENVLFSR-SIRDNIA-- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 101 lklskLPKDQI-EAQVAEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:TIGR01846 553 -----LCNPGApFEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 169 LRASMRirisdlhKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:TIGR01846 628 SEALIM-------RNMREICRGRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-232 |
8.46e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.09 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYPHMTVKENL 97
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelARRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 AFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAI------VKKPDVFLF-DEPLSNLDakLR 170
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPTSALD--LA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 171 ---ASMRirisdLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIM------QVDTPDNL---YHYPT 232
Cdd:COG4559 175 hqhAVLR-----LARQLARRG--GGVVAVLHDLNLAAQYADRILLLHQGRLVaqgtpeEVLTDELLervYGADL 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-218 |
9.45e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 9.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS---RGIAMVFQN---YALYPHM 91
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 TVKENLAFGL--KLSKLP--KDQIEAQVAEA-------------AKIleledlldrlpRQLSGGQAQRVAVGRAIVKKPD 154
Cdd:COG1129 346 SIRENITLASldRLSRGGllDRRRERALAEEyikrlriktpspeQPV-----------GNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 155 VFLFDEPLSNLD--AKlrasmririSDLHK---QLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:COG1129 415 VLILDEPTRGIDvgAK---------AEIYRlirELAAEGKA--VIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-227 |
1.60e-17 |
|
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: 80.99 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIG--DRVVNNLAPKSRGIAMVFQNYALYpHMTVKEN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghDLALADPAWLRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAfgLKLSKLPKDQIEaqvaEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03252 96 IA--LADPGMSMERVI----EAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 166 DAKlraSMRIRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:cd03252 170 DYE---SEHAIMRNMHDIC-----AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-198 |
1.74e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIgdrvvnnlaPKSRGIAMVFQNyalyPHM---TVKEN 96
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQR----PYLplgTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKLPKDQIeAQVAEAA---KILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASM 173
Cdd:COG4178 446 LLYPATAEAFSDAEL-REALEAVglgHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
170 180
....*....|....*....|....*
gi 1540023143 174 ririsdlHKQLKKSGKAATTVYVTH 198
Cdd:COG4178 525 -------YQLLREELPGTTVISVGH 542
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-218 |
2.19e-17 |
|
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: 80.39 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLetISDGEVRIGDRVVNNLAPK----SRGIAMVFQNYALYPHMTV 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFNGQPRKpdqfQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 94 KENLAFG--LKLSKLPKDQIEAQVAEAAKILELEDLLDRLP--RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL 169
Cdd:cd03234 99 RETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 170 RASMrirISDLhKQLKKSGKaatTVYVTHDQ--TEAMTMGDRICVMKLGHI 218
Cdd:cd03234 179 ALNL---VSTL-SQLARRNR---IVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-221 |
2.22e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLA-----PKSRGIAMVFQN-YA-LYPHM 91
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 TVKENLAFGLKLSKL-PKDQIEAQVAEA-AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL 169
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLlERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 170 RASMRIRISDLHKQLkksgkAATTVYVTHDQTEAMTMGDRICVMKLGHIMQV 221
Cdd:PRK10261 499 RGQIINLLLDLQRDF-----GIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-216 |
2.31e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYSnGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVV---NNLAPKSRGIAMVF 82
Cdd:PRK11288 7 FDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 83 QNYALYPHMTVKENLAFGlklsKLP-------KDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:PRK11288 86 QELHLVPEMTVAENLYLG----QLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 156 FLFDEPLSNLDAklRASMRI-RISDlhkQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:PRK11288 162 IAFDEPTSSLSA--REIEQLfRVIR---ELRAEGRV--ILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-267 |
2.50e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEV--------------RIGDRVVNNLAPKSRG----- 77
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLVIQKTRFkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 78 -------IAMVFQ--NYALYpHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKIL-ELEDLLDRLPRQLSGGQAQRVAVGR 147
Cdd:PRK13651 100 ikeirrrVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVgLDESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 148 AIVKKPDVFLFDEPLSNLDAKlrasMRIRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQ-VDTPDN 226
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQ----GVKEILEIFDNLNKQGK--TIILVTHDLDNVLEWTKRTIFFKDGKIIKdGDTYDI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1540023143 227 LyhyPTNMFVAgfigapEMNIKPSTL---VEKEGQIGLTVGQYT 267
Cdd:PRK13651 253 L---SDNKFLI------ENNMEPPKLlnfVNKLEKKGIDVPKVT 287
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-227 |
5.19e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAM 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 81 VFQNYALYpHMTVKENLAFGlklsklPKDQIEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAI 149
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 150 VKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKqlkksGKaaTTVYVTHDQT---EAmtmgDRICVMKLGHIMQVDTPDN 226
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK-----GR--TTFIIAHRLStvrNA----DRILVFDNGRVVESGSFDE 555
|
.
gi 1540023143 227 L 227
Cdd:PRK13657 556 L 556
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-220 |
6.94e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.83 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN--NLAPKSRGIAMVFQN--YALYPHMTVK 94
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFGLKL-SKLPKDQIEAQVAEAAK-ILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklrAS 172
Cdd:PRK15112 108 QILDFPLRLnTDLEPEQREKQIIETLRqVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD----MS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540023143 173 MRIRISDLHKQLK-KSGKAatTVYVTHDQTEAMTMGDRICVMKLGHIMQ 220
Cdd:PRK15112 184 MRSQLINLMLELQeKQGIS--YIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-331 |
7.99e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYS-NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDR-VVNNLAPKSRGIAMV 81
Cdd:TIGR01257 929 VCVKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 162 LSNLDAKLRASmrirISDLhkqLKKSGKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLyhypTNMFVAGF-- 239
Cdd:TIGR01257 1089 TSGVDPYSRRS----IWDL---LLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGFyl 1157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 240 IGAPEMNIKPSTLVEKEGQIGLTVGQYTLvlneRQQAKVATHTGEKVFFGVRPEFISMSLqpfvgnHSQGELVRVENMGH 319
Cdd:TIGR01257 1158 TLVRKMKNIQSQRGGCEGTCSCTSKGFST----RCPARVDEITPEQVLDGDVNELMDLVY------HHVPEAKLVECIGQ 1227
|
330
....*....|..
gi 1540023143 320 EFFMYIKVENFE 331
Cdd:TIGR01257 1228 ELIFLLPNKNFK 1239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-219 |
9.78e-17 |
|
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: 77.35 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNL-APKSRGIAMVFQNYALYpHMTVKENL 97
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLeKALSSLISVLNQRPYLF-DTTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 AfglklsklpkdqieaqvaeaakileledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMrirI 177
Cdd:cd03247 96 G----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL---L 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1540023143 178 SDLHKQLKksGKaaTTVYVTHDQTeAMTMGDRICVMKLGHIM 219
Cdd:cd03247 139 SLIFEVLK--DK--TLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-218 |
1.17e-16 |
|
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: 81.40 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYpHMTVKENLA 98
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 99 FGLklsklPkDQIEAQVAEAAKILELEDLLDRLPRQ-----------LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:COG5265 454 YGR-----P-DASEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 168 KLRAsmririsDLHKQLKKSGKAATTVYVTH------DqteamtmGDRICVMKLGHI 218
Cdd:COG5265 528 RTER-------AIQAALREVARGRTTLVIAHrlstivD-------ADEILVLEAGRI 570
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-218 |
1.44e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 9 LGKVYSnGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAP---KSRGIAMVFQNY 85
Cdd:PRK15439 17 ISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAA---KILELEDLLDRLPRQLsggqaqrVAVGRAIVKKPDVFLFDEPL 162
Cdd:PRK15439 96 LLFPNLSVKENILFGLPKRQASMQKMKQLLAALGcqlDLDSSAGSLEVADRQI-------VEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 163 SNLDAklrasmrIRISDLHKQLKK-SGKAATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:PRK15439 169 ASLTP-------AETERLFSRIRElLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-216 |
1.77e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 8 KLGKVYSnGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQN 84
Cdd:PRK09700 10 GIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFGLKLSK-------LPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:PRK09700 89 LSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 158 FDEPLSNLDAK----LRASMRirisdlhkQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:PRK09700 169 MDEPTSSLTNKevdyLFLIMN--------QLRKEGTA--IVYISHKLAEIRRICDRYTVMKDG 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-231 |
3.83e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS---RGIAMVFQNYALYPHMT 92
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFG----LK------LSKLP---KDQIEAqVAEAAKILELEDLLDRLPRQ---LSGGQAQRVAVGRAIVKKPDVF 156
Cdd:PRK11300 97 VIENLLVAqhqqLKtglfsgLLKTPafrRAESEA-LDRAATWLERVGLLEHANRQagnLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 157 LFDEPLSNLDAKLRASMRIRISDLHKQLKksgkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHN-----VTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-232 |
4.00e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.77 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPHmTVKENLAF 99
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlhRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLKlsKLPKDQIEAqvaeAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAk 168
Cdd:TIGR00958 578 GLT--DTPDEEIMA----AAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDA- 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 169 lrasmriRISDLHKQLKKSgKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPT 232
Cdd:TIGR00958 651 -------ECEQLLQESRSR-ASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-167 |
8.46e-16 |
|
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: 75.22 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 14 SNGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK-SRGIAMVFQNYALYPHM 91
Cdd:cd03231 9 ERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 92 TVKENLAFglklskLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:cd03231 89 SVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-167 |
9.01e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIgdrvvnnlaPKSRGIAMVFQNYALYPHMTVKENLAFGL 101
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPPLDDDLTVLDTVLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 K-LSKLPK--DQIEAQVAE--------------------------AAKILE----LEDLLDRLPRQLSGGQAQRVAVGRA 148
Cdd:COG0488 87 AeLRALEAelEELEAKLAEpdedlerlaelqeefealggweaearAEEILSglgfPEEDLDRPVSELSGGWRRRVALARA 166
|
170
....*....|....*....
gi 1540023143 149 IVKKPDVFLFDEPLSNLDA 167
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLDL 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-219 |
1.16e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETIS--DGEVRIGDRVV--NNLAPKSR-GIAMVFQNYALYP 89
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELqaSNIRDTERaGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLL---DRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK13549 96 ELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDinpATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 167 AKlrasmRIRI-SDLHKQLKKSGKAAttVYVTHDQTEAMTMGDRICVMKLG-HIM 219
Cdd:PRK13549 176 ES-----ETAVlLDIIRDLKAHGIAC--IYISHKLNEVKAISDTICVIRDGrHIG 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-241 |
1.36e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 35 IVGPSGCAKSTTLRMLAGL-ETIS----DGEVRIGDRVVNN---LAPKSRGIAMVFQNYALYPhMTVKENLAFGLKLSKL 106
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFNyrdVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 107 -PKDQI----EAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLH 181
Cdd:PRK14271 131 vPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 182 KQLkksgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP----TNMFVAGFIG 241
Cdd:PRK14271 211 DRL-------TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYVAGLSG 267
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-167 |
1.67e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRgIAMVFQNYALYPHMTVKENLAFGL 101
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 102 KLsklpKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:PRK13539 99 AF----LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-232 |
2.35e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTT----LRMLAGLETI-SDGEVRI-GDRVVNNLAPKSRG-----IAMVFQN-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFhGESLLHASEQTLRGvrgnkIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFGLKLSK-LPKDQIEAQVA---EAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRgMRREAARGEILnclDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 161 PLSNLDAKLRAsmriRISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPT 232
Cdd:PRK15134 183 PTTALDVSVQA----QILQLLRELQQELNMG-LLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-225 |
2.43e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVV----------------------NNLAP 73
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVAlcekcgyverpskvgepcpvcgGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 74 K---------------SRGIAMVFQ-NYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSG 137
Cdd:TIGR03269 92 EevdfwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 138 GQAQRVAVGRAIVKKPDVFLFDEPLSNLD---AKLrasmririsdLHKQLKKSGKAA-TTVYVTHDQTEAMT-MGDRICV 212
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKL----------VHNALEEAVKASgISMVLTSHWPEVIEdLSDKAIW 241
|
250
....*....|...
gi 1540023143 213 MKLGHIMQVDTPD 225
Cdd:TIGR03269 242 LENGEIKEEGTPD 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-212 |
2.61e-15 |
|
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: 74.75 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 27 INDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIgdrVVNNLAPKSRGIAMVFQnyalyphMTVKENLAFGLKlSKL 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYE-------GTVRDLLSSITK-DFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 107 PKDQIEAQVAEAAKILELEDLLDrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA--KLRASMRIRISDLHKQl 184
Cdd:cd03237 91 THPYFKTEIAKPLQIEQILDREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqRLMASKVIRRFAENNE- 166
|
170 180
....*....|....*....|....*...
gi 1540023143 185 kksgkaATTVYVTHDQTEAMTMGDRICV 212
Cdd:cd03237 167 ------KTAFVVEHDIIMIDYLADRLIV 188
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-227 |
4.70e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLetISDGEVRIGDRVVNNL---APKSRGI-AMVFQNYALYPHMTVKEN 96
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR--SPKGVKGSGSVLLNGMpidAKEMRAIsAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAF------GLKLSKLPKDQIEAQVAEAAKILELEDLLDRLP---RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:TIGR00955 120 LMFqahlrmPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 168 kLRASMRIRISdlhKQLKKSGKaatTVYVTHDQ--TEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:TIGR00955 200 -FMAYSVVQVL---KGLAQKGK---TIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-237 |
4.76e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTT----LRML-AGLETISdGEVRIGDRVVNNLAPKSRGIAMVFQN--YALYPHMT 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILpAGVRQTA-GRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 ----VKENLafgLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:PRK10418 98 mhthARETC---LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 169 LRAsmriRISDLHKQLKKSgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP----TNMFVA 237
Cdd:PRK10418 175 AQA----RILDLLESIVQK-RALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPkhavTRSLVS 242
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-227 |
7.53e-15 |
|
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: 75.93 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLapkSRGIAMVF 82
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 83 QNY-ALYPHM---TVKENLAFGLKlSKLPKDQIEaQVAEAAKILE--------LEDLLDRLPRQLSGGQAQRVAVGRAIV 150
Cdd:TIGR01193 550 INYlPQEPYIfsgSILENLLLGAK-ENVSQDEIW-AACEIAEIKDdienmplgYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 151 KKPDVFLFDEPLSNLDAKLRASMrirISDLHKQLKKsgkaaTTVYVTHDQTEAmTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKI---VNNLLNLQDK-----TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-218 |
9.24e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL--------ETISDGEVRIGDRVVNNlapKSRGIAMVFQNYAL 87
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKASNIRDT---ERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGLKLSkLPKDQIE--AQVAEA----AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:TIGR02633 90 VPELSVAENIFLGNEIT-LPGGRMAynAMYLRAknllRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 162 LSNLDaklRASMRIRIsDLHKQLKKSGKAAttVYVTHDQTEAMTMGDRICVMKLG-HI 218
Cdd:TIGR02633 169 SSSLT---EKETEILL-DIIRDLKAHGVAC--VYISHKLNEVKAVCDTICVIRDGqHV 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-219 |
1.27e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 14 SNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMV---FQNYAL 87
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 YPHMTVKENLAFGL----KLSKLP---KDQIEAQVAEAAKILELEDLLDRLP-RQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:COG3845 348 VPDMSVAENLILGRyrrpPFSRGGfldRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 160 EPLSNLDAklRASMRIrisdlHKQL---KKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHIM 219
Cdd:COG3845 428 QPTRGLDV--GAIEFI-----HQRLlelRDAGAA--VLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-166 |
1.30e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 10 GKVYSNGFRAVHG-IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNlAPKSRGIAMVFQNYALY 88
Cdd:PRK13543 16 ALAFSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 89 PHMTVKENLAFglkLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK13543 95 ADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-219 |
1.77e-14 |
|
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: 71.40 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 11 KVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE--TISDGEVRIGDRVVNNLAPKSR---GIAMVFQNY 85
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPhmtvkenlafGLKLSKLPKDqieaqVAEAakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03217 87 PEIP----------GVKNADFLRY-----VNEG----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 166 DAKlraSMRIrISDLHKQLKKSGKAAttVYVTH-----DQTEAmtmgDRICVMKLGHIM 219
Cdd:cd03217 136 DID---ALRL-VAEVINKLREEGKSV--LIITHyqrllDYIKP----DRVHVLYDGRIV 184
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-218 |
1.99e-14 |
|
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: 71.73 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK--SRGIAMVFQNYALYPHmTVKENLAF 99
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLKLSKLPKDQIEAQVAEAAKILELEDLLDRLP-----RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR 174
Cdd:cd03248 111 GLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQ 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540023143 175 IRISDLHKQlkksgkaaTTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03248 191 QALYDWPER--------RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-231 |
2.11e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.24 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL----ETISDGEVRIGDRVVNNLAPKSR------GIAMVFQN-- 84
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENLAFGLKL----SKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 161 PLSNLDAKLRAsmriRISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:PRK11022 180 PTTALDVTIQA----QIIELLLELQQKENMA-LVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-219 |
2.75e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPHmTVKEN 96
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRVHLFSA-TLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLK---------------LSKLPKDQ--IEAQVAEAAkileledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:PRK11160 434 LLLAAPnasdealievlqqvgLEKLLEDDkgLNAWLGEGG-------------RQLSGGEQRRLGIARALLHDAPLLLLD 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 160 EPLSNLDAKLRAsmriRISDLhkqLKKSGKAATTVYVTHDQTeAMTMGDRICVMKLGHIM 219
Cdd:PRK11160 501 EPTEGLDAETER----QILEL---LAEHAQNKTVLMITHRLT-GLEQFDRICVMDNGQII 552
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-168 |
2.98e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGiAMVF---QNyALYPHMTVKENL 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ-DLLYlghQP-GIKTELTALENL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 98 AFGLKLSKLPKDQIEAQVAEAAKIleleDLLDRLP-RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQVGL----AGFEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
3.20e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFnKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRvvnNLAPKS------R 76
Cdd:PRK09700 263 ETVF-EVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSpldavkK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 77 GIAMVFQNY---ALYPHMTVKENLAFG--LKLSK------LPKDQIEAQVAEAAK--ILELEDLLDRLPRQLSGGQAQRV 143
Cdd:PRK09700 339 GMAYITESRrdnGFFPNFSIAQNMAISrsLKDGGykgamgLFHEVDEQRTAENQRelLALKCHSVNQNITELSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 144 AVGRAIVKKPDVFLFDEPLSNLDAKLRAsmriRISDLHKQLKKSGKaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQV 221
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKA----EIYKVMRQLADDGK--VILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-167 |
3.65e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISD--GEVRIGDRVVNNlaPKSRGIAMVFQNYALYPHMTVKENL 97
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 AFgLKLSKLPKD---QIEAQVAEA-------AKILELEDLLDRLpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:PLN03211 162 VF-CSLLRLPKSltkQEKILVAESviselglTKCENTIIGNSFI-RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-230 |
7.93e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.82 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNL---APKSRgIAMVFQNYALYPHmTVKE 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSWRSR-LAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAFGlklsklPKDQIEAQVAEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:PRK10789 408 NIALG------RPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 165 LDAklRASMRIrisdLHkQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTPDNL----------YHY 230
Cdd:PRK10789 482 VDG--RTEHQI----LH-NLRQWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLaqqsgwyrdmYRY 549
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-199 |
1.35e-13 |
|
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: 71.89 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIF--NKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRigdrvvnnLAPkSRGIA 79
Cdd:TIGR03719 1 AQYIYtmNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQP-GIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 80 MVFQNYALYPHMTVKENLAFGL-----KLSKL---------PKDQIEAQVAEAAKILELEDLLDR--LPRQ--------- 134
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVaeikdALDRFneisakyaePDADFDKLAAEQAELQEIIDAADAwdLDSQleiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 135 ----------LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlrasmriRISDLHKQLKKSgkAATTVYVTHD 199
Cdd:TIGR03719 152 cppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLQEY--PGTVVAVTHD 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-201 |
1.85e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.56 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIgdrvvnnlaPKSRGIAMVFQ 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 NyalyPHM---TVKENLAFglklsklPKDQIeaqvaeaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDE 160
Cdd:cd03223 72 R----PYLplgTLREQLIY-------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540023143 161 PLSNLDAKLRASMririsdlHKQLKKSGkaATTVYVTHDQT 201
Cdd:cd03223 118 ATSALDEESEDRL-------YQLLKELG--ITVISVGHRPS 149
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-218 |
2.33e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.06 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGletISDGEVRI-GDRVVNNLAPKsrGIAMVFQNYALY----- 88
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVeGDIHYNGIPYK--EFAEKYPGEIIYvseed 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 89 ---PHMTVKENLAFGLKLsklpkdQIEAQVaeaakileledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:cd03233 93 vhfPTLTVRETLDFALRC------KGNEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540023143 166 DaklrASMRIRISDLHKQLKKSGKAATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:cd03233 150 D----SSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-221 |
3.03e-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: 71.52 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVvnnlapksrgiAMVFQNyALYPHMTVKENLAF 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLKLsklpKDQIEAQVAEAAKILELEDLLDRLPR--------QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRA 171
Cdd:TIGR00957 722 GKAL----NEKYYQQVLEACALLPDLEILPSGDRteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540023143 172 SMRIRISDLHKQLKksGKaaTTVYVTHDQTeAMTMGDRICVMKLGHIMQV 221
Cdd:TIGR00957 798 HIFEHVIGPEGVLK--NK--TRILVTHGIS-YLPQVDVIIVMSGGKISEM 842
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-211 |
4.69e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.35 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRV-----VNNLapksRGIAMVF-QNYALYPHM 91
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrKEFA----RRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 TVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlrA 171
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV--S 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540023143 172 SMRIRisDLHKQLKKSGKaaTTVYVT-HDqteamtMGD--RIC 211
Cdd:COG4586 190 KEAIR--EFLKEYNRERG--TTILLTsHD------MDDieALC 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-214 |
5.75e-13 |
|
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: 67.46 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI--GDRVVNNLAPKSRGIAMVFQNYALY-------- 88
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 89 PHMT----VKENL-AFGLklsklpkDQIEAQvAEAAKILELEDLldrlPRQL--------SGGQAQRVAVGRAIVKKPDV 155
Cdd:COG4778 106 PRVSaldvVAEPLlERGV-------DREEAR-ARARELLARLNL----PERLwdlppatfSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 156 FLFDEPLSNLDAKLRASMRirisDLHKQLKKSGkaATTVYVTHDqTEAM-TMGDRICVMK 214
Cdd:COG4778 174 LLLDEPTASLDAANRAVVV----ELIEEAKARG--TAIIGIFHD-EEVReAVADRVVDVT 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-224 |
1.23e-12 |
|
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: 66.36 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 3 EVIFNKLGKVYSNGFRAV-HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRgI 78
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlrSR-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 79 AMVFQNYALYPHmTVKENLA-FG----------LKLSKL------PKDQIEAQVAEaakileledlldrLPRQLSGGQAQ 141
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDpFGeysdeelwqaLERVGLkefvesLPGGLDTVVEE-------------GGENLSVGQRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 142 RVAVGRAIVKKPDVFLFDEPLSNLDaklRASMRIrisdLHKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQV 221
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVD---PETDAL----IQKTIREAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEF 218
|
...
gi 1540023143 222 DTP 224
Cdd:cd03244 219 DSP 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-218 |
1.27e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 7 NKLGKVYSNGfRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEV--RIGDRVVNNLAPKSRGI------ 78
Cdd:PRK11701 10 RGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDLYALSEAErrrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 79 ---AMVFQNYALYPHMTVK------ENL-AFGLK------------LSK--LPKDQIEAQvaeaakileledlldrlPRQ 134
Cdd:PRK11701 89 tewGFVHQHPRDGLRMQVSaggnigERLmAVGARhygdiratagdwLERveIDAARIDDL-----------------PTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 135 LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAsmriRISDLHKQLKKS-GKAAttVYVTHDQTEAMTMGDRICVM 213
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA----RLLDLLRGLVRElGLAV--VIVTHDLAVARLLAHRLLVM 225
|
....*
gi 1540023143 214 KLGHI 218
Cdd:PRK11701 226 KQGRV 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-199 |
2.57e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFNKLGKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNlAPKSRGIAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 82 FQNYAL---YPhMTVKENLAFG----LKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPD 154
Cdd:PRK15056 84 PQSEEVdwsFP-VLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540023143 155 VFLFDEPLSNLDAKLRAsmriRISDLHKQLKKSGKaaTTVYVTHD 199
Cdd:PRK15056 163 VILLDEPFTGVDVKTEA----RIISLLRELRDEGK--TMLVSTHN 201
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-261 |
3.42e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN----NLAPKSRGIAMVFQNYALYPHMT-VKEN 96
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQDPEQQIFYTdIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIR 176
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 177 ISDLhkqlkkSGKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMFVAGfigapemnIKPSTLVEKE 256
Cdd:PRK13638 179 IRRI------VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAG--------LTQPWLVKLH 244
|
....*
gi 1540023143 257 GQIGL 261
Cdd:PRK13638 245 TQLGL 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-166 |
6.72e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVnnlapksrgIAMVFQNYA-LYPHMTVKENL- 97
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK---------IGYFDQHQEeLDPDKTVLDELr 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 ----------------AFGlklskLPKDQIEAQVaeaakileledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:COG0488 402 dgapggteqevrgylgRFL-----FSGDDAFKPV-----------------GVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
....*
gi 1540023143 162 LSNLD 166
Cdd:COG0488 460 TNHLD 464
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-216 |
1.03e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 63.89 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTL-RMLAGLETISdGEVRIGDRVVNNLA-----PKSRG-IAMVFQNY 85
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSNKNESEPSfeatrSRNRYsVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYpHMTVKENLAFGLKLSKlpkdQIEAQVAEAAKILELEDLLDRLPR--------QLSGGQAQRVAVGRAIVKKPDVFL 157
Cdd:cd03290 89 WLL-NATVEENITFGSPFNK----QRYKAVTDACSLQPDIDLLPFGDQteigergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 158 FDEPLSNLDAKLRAS-MRIRISDLHKQLKKsgkaaTTVYVTHdQTEAMTMGDRICVMKLG 216
Cdd:cd03290 164 LDDPFSALDIHLSDHlMQEGILKFLQDDKR-----TLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-218 |
1.76e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQNY---ALYPHMTV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglANGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 94 KENLAFgLKLSKLPKD--QIEAQVAEAAKILELEDLLDRLPRQ------LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:PRK10762 348 KENMSL-TALRYFSRAggSLKHADEQQAVSDFIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 166 D--AKLrasmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:PRK10762 427 DvgAKK------EIYQLINQFKAEG--LSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-253 |
3.37e-11 |
|
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: 62.77 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFrAVHGIDLkINDGEFMVIVGPSGCAKSTTLRMLAGletisdgevrigdRVVNNLA-----PKSRGIAMVFQNYALYP 89
Cdd:cd03236 13 NSF-KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAG-------------KLKPNLGkfddpPDWDEILDEFRGSELQN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HMT-VKENlafGLKLSKLPK--DQIEAQVA-----------EAAKILELEDLLDRLP------RQLSGGQAQRVAVGRAI 149
Cdd:cd03236 78 YFTkLLEG---DVKVIVKPQyvDLIPKAVKgkvgellkkkdERGKLDELVDQLELRHvldrniDQLSGGELQRVAIAAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 150 VKKPDVFLFDEPLSNLDAKLRASMRIRIsdlhKQLKKSGKAatTVYVTHDQTEAMTMGDRICVM--KLGhIMQVDTPDNL 227
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLI----RELAEDDNY--VLVVEHDLAVLDYLSDYIHCLygEPG-AYGVVTLPKS 227
|
250 260
....*....|....*....|....*.
gi 1540023143 228 YHYPTNMFVAGFIGAPEMNIKPSTLV 253
Cdd:cd03236 228 VREGINEFLDGYLPTENMRFREESIE 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-199 |
6.36e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 1 MAEVIF--NKLGKVYSNGFRAVHGIDL------KINdgefmvIVGPSGCAKSTTLRMLAGLETISDGEVRigdrvvnnLA 72
Cdd:PRK11819 2 MAQYIYtmNRVSKVVPPKKQILKDISLsffpgaKIG------VLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 73 PKSRgIAMVFQNYALYPHMTVKENL--AFGLKLSKLPK--------------------------DQIEA----------- 113
Cdd:PRK11819 68 PGIK-VGYLPQEPQLDPEKTVRENVeeGVAEVKAALDRfneiyaayaepdadfdalaaeqgelqEIIDAadawdldsqle 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 114 QVAEA-------AKILeledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlrasmriRISDLHKQLKK 186
Cdd:PRK11819 147 IAMDAlrcppwdAKVT-----------KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLEQFLHD 208
|
250
....*....|....
gi 1540023143 187 -SGkaaTTVYVTHD 199
Cdd:PRK11819 209 yPG---TVVAVTHD 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
23-166 |
6.41e-11 |
|
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: 59.77 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVvnnlapksrgiamvfqnyalyphmtvkenlafglK 102
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------------------------K 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 103 LSKLPkdqieaqvaeaakileledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:cd03221 65 IGYFE--------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-227 |
7.59e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLR-MLAGLETISDGEVRIgdrvvnnlapksRG-IAMVFQNYALYpHMTVKENLAFG 100
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI------------RGtVAYVPQVSWIF-NATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 101 LK------------------LSKLP-KDQIEaqVAEAAKileledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEP 161
Cdd:PLN03130 703 SPfdperyeraidvtalqhdLDLLPgGDLTE--IGERGV-------------NISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 162 LSNLDAKLRASMririsdLHKQLKKSGKAATTVYVThDQTEAMTMGDRICVMKLGHIMQVDTPDNL 227
Cdd:PLN03130 768 LSALDAHVGRQV------FDKCIKDELRGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-249 |
7.61e-11 |
|
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: 63.88 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 6 FNKLGKVYS-NGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNNLAPKSRGIAMVFQ 83
Cdd:TIGR01257 1940 LNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 84 NYALYPHMTVKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:TIGR01257 2020 FDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 164 NLDAKLRASMRIRISDLHKQlkksGKAatTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNL-YHYPTNMFVAGFIGA 242
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIRE----GRA--VVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkSKFGDGYIVTMKIKS 2173
|
....*..
gi 1540023143 243 PEMNIKP 249
Cdd:TIGR01257 2174 PKDDLLP 2180
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-227 |
2.30e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.24 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETiSDGEVRIGDRVVN--NLAPKSRGIAMVFQNYALYPHMTVKENLAF 99
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSdwSAAELARHRAYLSQQQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 100 GLKlSKLPKDQIE---AQVAEAAKILELEdlldrlPR---QLSGGQAQRVAVGRAIVK-KPDV------FLFDEPLSNLD 166
Cdd:COG4138 93 HQP-AGASSEAVEqllAQLAEALGLEDKL------SRpltQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 167 AKLRASMririSDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIM------QVDTPDNL 227
Cdd:COG4138 166 VAQQAAL----DRLLRELCQQG--ITVVMSSHDLNHTLRHADRVWLLKQGKLVasgetaEVMTPENL 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-189 |
2.76e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.64 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRvvnnlapksrgIAMVFQNYALYPHmTVKENLAFGLK 102
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 103 ------LSKLPKDQIEAQVAEAAKILELEDLLDRLprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD---------- 166
Cdd:cd03291 124 ydeyryKSVVKACQLEEDITKFPEKDNTVLGEGGI--TLSGGQRARISLARAVYKDADLYLLDSPFGYLDvftekeifes 201
|
170 180
....*....|....*....|....*.
gi 1540023143 167 --AKLRAS-MRIRISDLHKQLKKSGK 189
Cdd:cd03291 202 cvCKLMANkTRILVTSKMEHLKKADK 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-189 |
2.88e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRvvnnlapksrgIAMVFQNYALYPHmTVKENLAFGLK 102
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 103 L------SKLPKDQIE---AQVAEAAKILELEDLLDrlprqLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD------- 166
Cdd:TIGR01271 513 YdeyrytSVIKACQLEediALFPEKDKTVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDSPFTHLDvvtekei 587
|
170 180
....*....|....*....|....*....
gi 1540023143 167 -----AKLRAS-MRIRISDLHKQLKKSGK 189
Cdd:TIGR01271 588 fesclCKLMSNkTRILVTSKLEHLKKADK 616
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-224 |
3.69e-10 |
|
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: 58.96 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNN--LAPKSRGIAMVFQNYALYPHmTVKE 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipLEDLRSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 NLAfglklsklPKD-QIEAQVAEAAKILELEDlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASmr 174
Cdd:cd03369 101 NLD--------PFDeYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540023143 175 irisdLHKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTP 224
Cdd:cd03369 164 -----IQKTIREEFTNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-199 |
4.33e-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: 60.95 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 26 KINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVvnnlAPKSRGIAmvfQNYalypHMTVKENLAFGLKlSK 105
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI----SYKPQYIS---PDY----DGTVEEFLRSANT-DD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 106 LPKDQIEAQVAEAAKILELEDLLDrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklrASMRIRISDLHKQLK 185
Cdd:COG1245 430 FGSSYYKTEIIKPLGLEKLLDKNV---KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAIRRFA 502
|
170
....*....|....
gi 1540023143 186 KSGKAATTVyVTHD 199
Cdd:COG1245 503 ENRGKTAMV-VDHD 515
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-218 |
5.18e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 15 NGFrAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVV--NNLAPKSRGIAMVFQNYALYPHM- 91
Cdd:PRK10522 335 NGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaEQPEDYRKLFSAVFTDFHLFDQLl 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 ----TVKENLAFGLKLSKLP-KDQIEAQVAEAAKIleledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK10522 414 gpegKPANPALVEKWLERLKmAHKLELEDGRISNL------------KLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 167 AKLRasmRIRISDLHKQLKKSGKaaTTVYVTHDQtEAMTMGDRICVMKLGHI 218
Cdd:PRK10522 482 PHFR---REFYQVLLPLLQEMGK--TIFAISHDD-HYFIHADRLLEMRNGQL 527
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-167 |
7.94e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 13 YSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPH 90
Cdd:PRK10790 350 YRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlrQGVAMVQQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 mTVKENLAFGLKLSklpkdqiEAQVAEAAKILELEDLLDRLP-----------RQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:PRK10790 430 -TFLANVTLGRDIS-------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILD 501
|
....*...
gi 1540023143 160 EPLSNLDA 167
Cdd:PRK10790 502 EATANIDS 509
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-225 |
8.35e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE--TISDGEVRIGDRVVNNLAPKSR---GIAMVFQNYALYPHMTVKE 95
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 nlaFgLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQ---------LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:COG0396 97 ---F-LRTALNARRGEELSAREFLKLLKEKMKELGLDEDfldryvnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 167 AklrASMRIrISDLHKQLKKSGKAatTVYVTH-----DQTEAmtmgDRICVMKLGHIMQVDTPD 225
Cdd:COG0396 173 I---DALRI-VAEGVNKLRSPDRG--ILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGKE 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-171 |
1.15e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 4 VI-FNKLGKVYsngfravhGIDLKINDGEFMV-------IVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVnnlapks 75
Cdd:TIGR03719 322 VIeAENLTKAF--------GDKLLIDDLSFKLppggivgVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 76 rgIAMVFQNY-ALYPHMTVKENLAFGLKLSKLPKDQIEAQvAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPD 154
Cdd:TIGR03719 387 --LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSR-AYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|....*...
gi 1540023143 155 VFLFDEPLSNLDAK-LRA 171
Cdd:TIGR03719 464 VLLLDEPTNDLDVEtLRA 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-216 |
1.31e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 30 GEFMVIVGPSGCAKSTTLRMLAGLETISD--GEVRI-GDRVVNNLApksRGIAMVFQNYALYPHMTVKENLAFGLKLskl 106
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGVitGEILInGRPLDKNFQ---RSTGYVEQQDVHSPNLTVREALRFSALL--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 107 pkdqieaqvaeaakileledlldrlpRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlRASMRIRIsdlhkqLKK 186
Cdd:cd03232 107 --------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ-AAYNIVRF------LKK 153
|
170 180 190
....*....|....*....|....*....|..
gi 1540023143 187 SGKAATTVYVTHDQTEAMTMG--DRICVMKLG 216
Cdd:cd03232 154 LADSGQAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-167 |
1.34e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVrigdrvvnnLAPKSrgIAMVFQNyALYPHMTVKENLAF 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS--IAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 100 -----GLKLSKLPK-DQIEAQVAEAA-----KILELEDlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:PTZ00243 744 fdeedAARLADAVRvSQLEADLAQLGggletEIGEKGV-------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-210 |
2.34e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 24 DLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNNLA---PK----------SRGIAMVFQNYALYP 89
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQqdpPRnvegtvydfvAEGIEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HMTVK-------ENLAfglKLSKLPKD-------QIEAQVAEAAKILELEDLLDRLprQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:PRK11147 103 DISHLvetdpseKNLN---ELAKLQEQldhhnlwQLENRINEVLAQLGLDPDAALS--SLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 156 FLFDEPLSNLDaklrasmrIRISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRI 210
Cdd:PRK11147 178 LLLDEPTNHLD--------IETIEWLEGFLKTFQGS-IIFISHDRSFIRNMATRI 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-243 |
2.70e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKS--RGIAMVFQNYALYPHMTVKENL 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 AFGL-----KLSKLPKDQIEaQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRAS 172
Cdd:PRK10575 107 AIGRypwhgALGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 173 MRIRISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLG---------HIMQVDTPDNLYHYPTNMFVAGFIGAP 243
Cdd:PRK10575 186 VLALVHRLSQE-----RGLTVIAVLHDINMAARYCDYLVALRGGemiaqgtpaELMRGETLEQIYGIPMGILPHPAGAAP 260
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-199 |
7.15e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 27 INDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEV-----------RIGD----RVVNNLapksRGIAMVF-QNYalyph 90
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPdydgTVEDLL----RSITDDLgSSY----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 91 mtVKENLAFGLKLSKLpkdqIEAQVAEaakileledlldrlprqLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklr 170
Cdd:PRK13409 433 --YKSEIIKPLQLERL----LDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLD---- 485
|
170 180
....*....|....*....|....*....
gi 1540023143 171 ASMRIRISDLHKQLKKSGKAATTVyVTHD 199
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEREATALV-VDHD 513
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-212 |
9.88e-09 |
|
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: 54.50 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 27 INDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIgDRVVNNLAPKsrgiamvfqnyalyphmtvkenlafglklskl 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQ-------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 107 pkdqieaqvaeaaKIleledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKK 186
Cdd:cd03222 69 -------------YI------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|....*.
gi 1540023143 187 sgkaaTTVYVTHDQTEAMTMGDRICV 212
Cdd:cd03222 124 -----TALVVEHDLAVLDYLSDRIHV 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
133-199 |
1.17e-08 |
|
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: 56.72 E-value: 1.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 133 RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlrasMRIRISDLHKQLKKSGKAatTVYVTHD 199
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY----QRLNVARLIRELAEEGKY--VLVVEHD 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-220 |
1.21e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 19 AVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGE-----VRIGDRVVNNLapkSRGIAMVFQNYALYpHMTV 93
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEilldgHDLRDYTLASL---RNQVALVSQNVHLF-NDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 94 KENLAFGLKlSKLPKDQIEaqvaEAAKILELEDLLDRLPR-----------QLSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:PRK11176 434 ANNIAYART-EQYSREQIE----EAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 163 SNLDAKlraSMRIRISDLhKQLKKSgkaaTTVYVTHDQTEAMTMGDRICVMKLGHIMQ 220
Cdd:PRK11176 509 SALDTE---SERAIQAAL-DELQKN----RTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-195 |
1.49e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE--TISDGEVRIGDrvvNNLAPKSRGIAmvfqnyALYPHMTVK 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD---NQFGREASLID------AIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENLAFgLKLSKLpkdqieaqvAEAAkileledLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR 174
Cdd:COG2401 114 DAVEL-LNAVGL---------SDAV-------LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|.
gi 1540023143 175 IRISDLHKQLKKSGKAATTVY 195
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHY 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-166 |
2.26e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 27 INDGEFMVIVGPSGCAKSTTLRMLAGLeTISDGEVRIGDRVV-----NNLApKSRG---------IAM-VFQNYALYPHm 91
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsaAELA-RHRAylsqqqtppFAMpVFQYLTLHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 92 tvkenlafglklSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRV-------AVGRAIVKKPDVFLFDEPLSN 164
Cdd:PRK03695 96 ------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNS 163
|
..
gi 1540023143 165 LD 166
Cdd:PRK03695 164 LD 165
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-193 |
2.84e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRI-GDRVVNNLAPKSRGIAMVFQNYALYPHMTVKENLAFGL 101
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 KLSklpkdQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlraSMRIRISDLH 181
Cdd:PRK13540 100 HFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL---SLLTIITKIQ 171
|
170
....*....|..
gi 1540023143 182 KQLKKSGKAATT 193
Cdd:PRK13540 172 EHRAKGGAVLLT 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-218 |
3.23e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQNY---ALYPHMTVKEN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaiRAGIMLCPEDRkaeGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LA-----FGLKLSKLPKDQIEAQVAEA--AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKL 169
Cdd:PRK11288 352 INisarrHHLRAGCLINNRWEAENADRfiRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540023143 170 RAsmriRISDLHKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:PRK11288 432 KH----EIYNVIYELAAQGVA--VLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-231 |
3.52e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.53 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 17 FRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE----TISDGEVRIGDRVVNNLAPKSR------GIAMVFQN-- 84
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 85 YALYPHMTVKENL-------AFGLKLSKLPKDQIEAQVAEAAK--ILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDV 155
Cdd:COG4170 100 SCLDPSAKIGDQLieaipswTFKGKWWQRFKWRKKRAIELLHRvgIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 156 FLFDEPLSNLDAKLRAsmriRISDLHKQLKKSGKaaTTV-YVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYP 231
Cdd:COG4170 180 LIADEPTNAMESTTQA----QIFRLLARLNQLQG--TSIlLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
3.67e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKSTTLR-MLAGLETISDGEVRIGDRVVnnLAPKsrgIAMVFqnyalypHMTVKENLAFGL 101
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVA--YVPQ---VSWIF-------NATVRENILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 KLSklPKDQIEAQVAEAAK----ILELEDLLDRLPR--QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMri 175
Cdd:PLN03232 704 DFE--SERYWRAIDVTALQhdldLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV-- 779
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540023143 176 risdLHKQLKKSGKAATTVYVThDQTEAMTMGDRICVMKLGHIMQ 220
Cdd:PLN03232 780 ----FDSCMKDELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKE 819
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-171 |
4.17e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 35 IVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSRGiaMVFQNYALYPHMTVKENLAFGLKLSklpkDQIEAQ 114
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT--YIGHNLGLKLEMTVFENLKFWSEIY----NSAETL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 115 VAeAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRA 171
Cdd:PRK13541 105 YA-AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-216 |
6.15e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 30 GEFMVIVGPSGCAKSTTLRMLAGLETIsdGEVRIGDRVVNNLAPKS---RGIAMVFQNYALYPHMTVKENLAFGLKL--- 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTT--GVITGGDRLVNGRPLDSsfqRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 104 ---SKLPKDQIEAQVAEAAKILELEDLLDRLPRQ-LSGGQAQRVAVGRAIVKKPDVFLF-DEPLSNLDAKLRASmrirIS 178
Cdd:TIGR00956 867 ksvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWS----IC 942
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1540023143 179 DLHKQLKKSGKAattVYVTHDQTEAMTMG--DRICVMKLG 216
Cdd:TIGR00956 943 KLMRKLADHGQA---ILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-216 |
6.85e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR---GIAMVFQNYALYPHMT 92
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaGIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGLKL-SKLPKDQIEAQVAEAAKILELEDLLDRLPR---QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK 168
Cdd:PRK10762 96 IAENIFLGREFvNRFGRIDWKKMYAEADKLLARLNLRFSSDKlvgELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540023143 169 LRASMRIRIsdlhKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:PRK10762 176 ETESLFRVI----RELKSQGRG--IVYISHRLKEIFEICDDVTVFRDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-247 |
1.72e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRigdrvvnnLAPKSRgIAMVFQNYALYPHM--TVKe 95
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQKLYLDTTLplTVN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 96 nlafglKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklrASMRI 175
Cdd:PRK09544 88 ------RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD----VNGQV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 176 RISDLHKQLKKSGKAAtTVYVTHDQTEAMTMGDRICVMKlGHIMQVDTPDNLYHYPTNMFVAGFIGAPEMNI 247
Cdd:PRK09544 158 ALYDLIDQLRRELDCA-VLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHPEFISMFGPRGAEQLGI 227
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-212 |
1.97e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 30 GEFMVIVGPSGCAKSTTLRMLAgletisdgevrigdrvvNNLAPKSRGIAMVfqnyalyphmtvkenlafglKLSKLPKD 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-----------------RELGPPGGGVIYI--------------------DGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 110 QIEaqvaeaakiLELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQLKKSGK 189
Cdd:smart00382 45 VLD---------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK 115
|
170 180
....*....|....*....|...
gi 1540023143 190 AATTVYVTHDQTEAMTMGDRICV 212
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
133-199 |
2.47e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 2.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 133 RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKlrasMRIRISDLHKQLKKsGKAatTVYVTHD 199
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR----QRLNVARLIRELAE-GKY--VLVVEHD 270
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-200 |
2.48e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 11 KVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE--TISDGEVRIGDRVVNNLAPKSR---GIAMVFQNY 85
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKE--NLAFG--LKLSKLPK-DQIEAQVAEAAKILELEDLLDRLPRQL----SGGQAQRVAVGRAIVKKPDVF 156
Cdd:CHL00131 94 IEIPGVSNADflRLAYNskRKFQGLPElDPLEFLEIINEKLKLVGMDPSFLSRNVnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540023143 157 LFDEPLSNLDAKlraSMRIrISDLHKQLKKSGKAAttVYVTHDQ 200
Cdd:CHL00131 174 ILDETDSGLDID---ALKI-IAEGINKLMTSENSI--ILITHYQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-212 |
3.04e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 79 AMVFQNYALYpHMTVKENLAFGlklsklPKDQIEAQVAEAAKILELEDLLDRLPRQ-----------LSGGQAQRVAVGR 147
Cdd:PTZ00265 1299 SIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIAR 1371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 148 AIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKqlkksgKAATTVYVTHDQTEAMTMGDRICV 212
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD------KADKTIITIAHRIASIKRSDKIVV 1430
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-235 |
4.56e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNN--LAPKSRGIAMVFQNYALYPHmTVKENL 97
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 98 -AF----------GLKLSKLpKDQI-------EAQVAEAAKileledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:PLN03232 1331 dPFsehndadlweALERAHI-KDVIdrnpfglDAEVSEGGE-------------NFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540023143 160 EPLSNLDaklrasmrIRISDL-HKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMF 235
Cdd:PLN03232 1397 EATASVD--------VRTDSLiQRTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-171 |
9.07e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 35 IVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVnnlapksrgIAMVFQNY-ALYPHMTVKENLAFGLKLSKLPKDQI-- 111
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK---------LAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIps 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 112 EAQVA-------EAAKILEledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAK-LRA 171
Cdd:PRK11819 426 RAYVGrfnfkggDQQKKVG----------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVEtLRA 483
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-166 |
1.15e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLE--TISDGEVRIGDRVVNNLAPKSR---GIAMVFQnyalYPHMTVKEN 96
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YPVEIPGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 LAFGLKLS---------KLPKDQIEAQVAEAAKILELEDLLDRLPRQL----SGGQAQRVAVGRAIVKKPDVFLFDEPLS 163
Cdd:PRK09580 95 NQFFLQTAlnavrsyrgQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILDESDS 174
|
...
gi 1540023143 164 NLD 166
Cdd:PRK09580 175 GLD 177
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
241-295 |
1.35e-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: 44.88 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 241 GAPEMNIKPSTLVEKEGQIglTVGQYTLVLNERQQAKVATHTGEKVFFGVRPEFI 295
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLV--LGGGVTLPLPEGQVLALKLYVGKEVILGIRPEHI 53
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-218 |
2.61e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 2 AEVIFNKLGK----VYSNGFRAVHGIdlkINDGEFMVIVGPSGCAKSTTLRMLA----GLETISDGEVRIGDRVVNNLAP 73
Cdd:TIGR00956 58 LTRGFRKLKKfrdtKTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 74 KSRG-IAMVFQNYALYPHMTVKENLAFGLKLsKLPKDQIE-----------AQVAEAA---KILELEDLLDRLPRQLSGG 138
Cdd:TIGR00956 135 HYRGdVVYNAETDVHFPHLTVGETLDFAARC-KTPQNRPDgvsreeyakhiADVYMATyglSHTRNTKVGNDFVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 139 QAQRVAVGRAIVKKPDVFLFDEPLSNLDAK--------LRASMRIrisdlhkqlkksgkAATTVYVTHDQT--EAMTMGD 208
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSAtalefiraLKTSANI--------------LDTTPLVAIYQCsqDAYELFD 279
|
250
....*....|
gi 1540023143 209 RICVMKLGHI 218
Cdd:TIGR00956 280 KVIVLYEGYQ 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-161 |
3.14e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEfMV-IVGPSGCAKSTTLRMLAGLETISDGEVRI--GD----RVVNNLAPKsrgIAMVFQ----Nya 86
Cdd:NF033858 15 VALDDVSLDIPAGC-MVgLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGDmadaRHRRAVCPR---IAYMPQglgkN-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 87 LYPHMTVKENLAFGLKLSKLPKDQIEAQVAE--------------AAKileledlldrlprqLSGGQAQRVAVGRAIVKK 152
Cdd:NF033858 89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDEllratglapfadrpAGK--------------LSGGMKQKLGLCCALIHD 154
|
....*....
gi 1540023143 153 PDVFLFDEP 161
Cdd:NF033858 155 PDLLILDEP 163
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-218 |
4.13e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRavhGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPKSR-GIAMVF-----QNYALYP 89
Cdd:PRK15439 278 GFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 90 HMTVKENLAfGLKLSKLP---KDQIEAQVAEA--AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSN 164
Cdd:PRK15439 355 DAPLAWNVC-ALTHNRRGfwiKPARENAVLERyrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 165 LDAKLRASmrirISDLHKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:PRK15439 434 VDVSARND----IYQLIRSIAAQNVA--VLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-198 |
1.05e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540023143 134 QLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLhkqlkKSGKAATTVYVTH 198
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL-----KGNENRITIIIAH 638
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-174 |
1.95e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 30 GEFMVIVGPSGCAKSTTLRMLAGLET--ISDGEVRIgdrvvNNLAPKSRGIAMVF----QNYALYPHMTVKENLAFG--L 101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRI-----SGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSafL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 102 KL----SKLPKDQIEAQVAEAAKILELEDLLDRLP--RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRA-SMR 174
Cdd:PLN03140 981 RLpkevSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAiVMR 1060
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-216 |
3.06e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLAPK---SRGIAMVFQNYALYPHMT 92
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAFGlklsKLPKDQI---EAQVAEAAKILELEDLLDRLPRQ----LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNL 165
Cdd:PRK10982 90 VMDNMWLG----RYPTKGMfvdQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 166 DAKlrasmriRISDLHKQLKK-SGKAATTVYVTHDQTEAMTMGDRICVMKLG 216
Cdd:PRK10982 166 TEK-------EVNHLFTIIRKlKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-166 |
8.29e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 22 GIDLKINdgefMVIVGPSGCAKSTTLRMLAG-LETISDGEVRigdrvvnnlAPKSRgIAMVFQNYALYPHMTVKENLAFG 100
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGeLQPSSGTVFR---------SAKVR-MAVFSQHHVDGLDLSSNPLLYMM 596
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 101 LKLSKLPKDQIEAQVAEaakILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PLN03073 597 RCFPGVPEQKLRAHLGS---FGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
14-69 |
1.06e-04 |
|
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: 44.02 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 14 SNGFrAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVN 69
Cdd:COG4615 343 DEGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-227 |
1.39e-04 |
|
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: 44.17 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 23 IDLKINDGEFMVIVGPSGCAKST-TLRMLAGLETiSDGEVRI-----GDRVVNNLAPKsrgIAMVFQNYALYPHmTVKEN 96
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSlTLGLFRINES-AEGEIIIdglniAKIGLHDLRFK---ITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 97 L-AFG----------LKLSKLPK------DQIEAQVAEAAKileledlldrlprQLSGGQAQRVAVGRAIVKKPDVFLFD 159
Cdd:TIGR00957 1380 LdPFSqysdeevwwaLELAHLKTfvsalpDKLDHECAEGGE-------------NLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540023143 160 EPLSNLDAK----LRASMRIRISDlhkqlkksgkaATTVYVTHDQTEAMTMgDRICVMKLGHIMQVDTPDNL 227
Cdd:TIGR00957 1447 EATAAVDLEtdnlIQSTIRTQFED-----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-218 |
2.04e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 135 LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDaklrASMRIRISDLHKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMK 214
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID----VGAKFEIYQLIAELAKKDKG--IIIISSEMPELLGITDRILVMS 465
|
....
gi 1540023143 215 LGHI 218
Cdd:PRK10982 466 NGLV 469
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-218 |
2.86e-04 |
|
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: 42.89 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 20 VHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL-ETISDGEVRIGDRVVNNLAPK---SRGIAMVFQN---YALYPHMT 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 93 VKENLAfglkLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQ----------LSGGQAQRVAVGRAIVKKPDVFLFDEPL 162
Cdd:TIGR02633 356 VGKNIT----LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 163 SNLDAKLRAsmriRISDLHKQLKKSGKAatTVYVTHDQTEAMTMGDRICVMKLGHI 218
Cdd:TIGR02633 432 RGVDVGAKY----EIYKLINQLAQEGVA--IIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-242 |
2.99e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLET----ISDGEVRIGDRVVNNLAPKSR------GIAMVFQ--NY 85
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQepQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 86 ALYPHMTVKENLA---------------FGLKLSKlpkdQIEaqVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIV 150
Cdd:PRK15093 101 CLDPSERVGRQLMqnipgwtykgrwwqrFGWRKRR----AIE--LLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 151 KKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQlkksgKAATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHY 230
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQN-----NNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTT 249
|
250
....*....|..
gi 1540023143 231 PTNMFVAGFIGA 242
Cdd:PRK15093 250 PHHPYTQALIRA 261
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-203 |
3.24e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 10 GKVYSNGFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAG-----------L--------ETISDGEVRIGdRVVNN 70
Cdd:PRK10938 266 GVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLfgrrrgsgETIWDIKKHIG-YVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 71 LAPKSRGIAMV--------FQNYALYPHMTVKENLAFGLKLSKLpkdQIEAQVAEAakileledlldrlP-RQLSGGQAQ 141
Cdd:PRK10938 345 LHLDYRVSTSVrnvilsgfFDSIGIYQAVSDRQQKLAQQWLDIL---GIDKRTADA-------------PfHSLSWGQQR 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540023143 142 RVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMR----IRISDLHKQLkksgkaattVYVTHDQTEA 203
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRrfvdVLISEGETQL---------LFVSHHAEDA 465
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-100 |
3.76e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 16 GFRAVHGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGL--------ETISDGEVR----IGDRvvnnlapKSRGIAMVFQ 83
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCrfkdIRDS-------EALGIVIIHQ 85
|
90
....*....|....*..
gi 1540023143 84 NYALYPHMTVKENLAFG 100
Cdd:NF040905 86 ELALIPYLSIAENIFLG 102
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-235 |
5.54e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 21 HGIDLKINDGEFMVIVGPSGCAKSTTLRMLAGLETISDGEVRIGDRVVNNLapksrGIAMVFQNYALYPHM------TVK 94
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-----GLMDLRKVLGIIPQApvlfsgTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 95 ENL-AFG----------LKLSKLpKDQI-------EAQVAEAAKileledlldrlprQLSGGQAQRVAVGRAIVKKPDVF 156
Cdd:PLN03130 1331 FNLdPFNehndadlwesLERAHL-KDVIrrnslglDAEVSEAGE-------------NFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540023143 157 LFDEPLSNLDAKLRASMRirisdlhKQLKKSGKAATTVYVTHdQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYPTNMF 235
Cdd:PLN03130 1397 VLDEATAAVDVRTDALIQ-------KTIREEFKSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-166 |
7.71e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 7.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540023143 109 DQIEAQVAEA------AKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PLN03073 313 ELIDAYTAEAraasilAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-260 |
7.75e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 18 RAVHGIDLKINDGEFMVIVGPSGCA--KSTTLRMLAGLETISD--------GEVRIGDRVVNNLAPKSRGIAMVFQNyal 87
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRpwrf*twcANRRALRRTIG*HRPVR*GRRESFSG--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 88 yphmtvKENLAFGLKLSKLPKDQIEAQVAEAAKILELEDLLDRLPRQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDA 167
Cdd:NF000106 104 ------RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 168 KLRAsmriRISDLHKQLKKSGkaATTVYVTHDQTEAMTMGDRICVMKLGHIMQVDTPDNLYHYptnmfvagfIGAPEMNI 247
Cdd:NF000106 178 RTRN----EVWDEVRSMVRDG--ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK---------VGGRTLQI 242
|
250
....*....|...
gi 1540023143 248 KPSTLVEKEGQIG 260
Cdd:NF000106 243 RPAHAAELDRMVG 255
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-166 |
9.31e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 30 GEFMVIVGPSGCAKSTTLR-MLAGLETISdGEVRIGDRVvnnlapksrGIAMvFQNY--ALYPHMTVKENLAFGLK---- 102
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTKL---------EVAY-FDQHraELDPEKTVMDNLAEGKQevmv 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540023143 103 -------LSKL------PKdqieaqvaeaakileledlLDRLP-RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD 166
Cdd:PRK11147 414 ngrprhvLGYLqdflfhPK-------------------RAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
57-218 |
1.20e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 57 SDGEVRIGDRVVNNLAPK---SRGIAMVFQN---YALYPHMTVKENLAfglkLSKLPKDQIEAQVAEAAKILELEDLLD- 129
Cdd:PRK13549 316 WEGEIFIDGKPVKIRNPQqaiAQGIAMVPEDrkrDGIVPVMGVGKNIT----LAALDRFTGGSRIDDAAELKTILESIQr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 130 -----RLPRQ----LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD--AKLrasmriRISDLHKQLKKSGKAatTVYVTH 198
Cdd:PRK13549 392 lkvktASPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKY------EIYKLINQLVQQGVA--IIVISS 463
|
170 180
....*....|....*....|
gi 1540023143 199 DQTEAMTMGDRICVMKLGHI 218
Cdd:PRK13549 464 ELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
133-183 |
1.54e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 1.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1540023143 133 RQLSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAKLRASMRIRISDLHKQ 183
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
135-235 |
1.63e-03 |
|
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: 39.89 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 135 LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLDAklrASMRIrisdLHKQLKKSGKAATTVYVTHDQTEAMTmGDRICVMK 214
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDM---ATENI----LQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLS 228
|
90 100
....*....|....*....|.
gi 1540023143 215 LGHIMQVDTPDNLYHYPTNMF 235
Cdd:cd03288 229 RGILVECDTPENLLAQEDGVF 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-218 |
2.97e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540023143 135 LSGGQAQRVAVGRAIVKKPDVFLFDEPLSNLD--AKLrasmriRISDLHKQLKKSGKAatTVYVTHDQTEAMTMGDRICV 212
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKY------EIYTIINELAAEGKG--VIVISSELPELLGMCDRIYV 476
|
....*.
gi 1540023143 213 MKLGHI 218
Cdd:NF040905 477 MNEGRI 482
|
|
| |
