|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-364 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 606.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAM 80
Cdd:COG3839 1 MASLELENVSKSYGGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSPAM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 241 NMLNATVEMDGLKVGTHHFKLHNkkfeklKAAGYLDKEIILGIRAEDIHeepifIQTSPETQFESEVVVSELLGSEIMVH 320
Cdd:COG3839 240 NLLPGTVEGGGVRLGGVRLPLPA------ALAAAAGGEVTLGIRPEHLR-----LADEGDGGLEATVEVVEPLGSETLVH 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 312828735 321 STFQGMELISKLDSRTQVMTNDKITLAFDMNKCHFFDEKTGNRI 364
Cdd:COG3839 309 VRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-364 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 522.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSPAM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 241 NMLNATVEMDGlkvGTHHFKLHNKKFEKLKAAGYLDKEIILGIRAEDIHeepifiQTSPETQFESEVVVSELLGSEIMVH 320
Cdd:PRK11650 241 NLLDGRVSADG---AAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIA------LSSAEGGVPLTVDTVELLGADNLAH 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 312828735 321 STFQGMELISKLDSRTQVMTNDKITLAFDMNKCHFFDEKTGNRI 364
Cdd:PRK11650 312 GRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-358 |
1.71e-152 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 433.37 E-value: 1.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAM 80
Cdd:COG3842 3 MPALELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSpaM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 241 NMLNATV---EMDGLKVGTHHFKLHNkkfeklKAAGYLDKEIILGIRAEDIHeepiFIQTSPETQFESEVVVSELLGSEI 317
Cdd:COG3842 240 NLLPGTVlgdEGGGVRTGGRTLEVPA------DAGLAAGGPVTVAIRPEDIR----LSPEGPENGLPGTVEDVVFLGSHV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 312828735 318 MVH-STFQGMELISKLDSRTQVM--TNDKITLAFDMNKCHFFDE 358
Cdd:COG3842 310 RYRvRLGDGQELVVRVPNRAALPlePGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-358 |
3.77e-151 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 430.61 E-value: 3.77e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAM 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSPAM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 241 NMLNATV---EMDGLKVgthhfKLHNKKFEKLKAAG---YLDKEIILGIRAEdiHEEPifiQTSPETQFESEVVVSELLG 314
Cdd:PRK11000 240 NFLPVKVtatAIEQVQV-----ELPNRQQVWLPVEGrgvQVGANMSLGIRPE--HLLP---SDIADVTLEGEVQVVEQLG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 312828735 315 SEIMVHSTFQGME--LISKLDSRTQVMTNDKITLAFDMNKCHFFDE 358
Cdd:PRK11000 310 NETQIHIQIPAIRqnLVYRQNDVVLVEEGATFAIGLPPERCHLFRE 355
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
2.46e-142 |
|
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: 402.02 E-value: 2.46e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
2.35e-113 |
|
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: 329.20 E-value: 2.35e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGF-VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
7.47e-113 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 327.17 E-value: 7.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-247 |
8.79e-111 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 328.06 E-value: 8.79e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSpaMNML 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIF 251
|
....
gi 312828735 244 NATV 247
Cdd:PRK09452 252 DATV 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-319 |
8.96e-111 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 327.10 E-value: 8.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN-DVEPKNRDIAMV 81
Cdd:COG1118 2 SIEVRNISKRFGSF-TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 162 LSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGspAMN 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 242 MLNATVEMDGLKVGTHHFKLHnkkfeklkaAGYLDKEIILGIRAEDIHeepIFIQTSPETQFESEVVVSELLGSEIMV 319
Cdd:COG1118 239 VLRGRVIGGQLEADGLTLPVA---------EPLPDGPAVAGVRPHDIE---VSREPEGENTFPATVARVSELGPEVRV 304
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-356 |
1.11e-107 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 319.64 E-value: 1.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNTVV---KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND-----VEP 73
Cdd:NF040933 1 VTVRVENVTKIFKKGKKEVvalDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 KNRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 154 KVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQ 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 234 FIGSpaMNMLNATVEMDGLKV-GTHHFKLHNKKFEKLKAagyldkeiILGIRAEDIHEEPIFIQTSPETQF--ESEVVVS 310
Cdd:NF040933 241 LIGD--INLLEGKVEEEGLVDgNDLKIPLPNPKLEAGEV--------IIGIRPEDIDISESDMRLPPGFVEvgKGRVKVS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 312828735 311 ELLGSEIMVHSTFQGMELIS-KLDSRTQVMTNDKITLAFDMNKCHFF 356
Cdd:NF040933 311 SYAGGVFRVVVSPIDDDSIEiIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-289 |
3.18e-102 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 305.42 E-value: 3.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSpaM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--V 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 312828735 241 NMLNATVEMDG-LKVGTHHFKLhNKKFEKLKAAGyldkeiILGIRAEDIH 289
Cdd:TIGR03265 239 NWLPGTRGGGSrARVGGLTLAC-APGLAQPGASV------RLAVRPEDIR 281
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-288 |
1.32e-99 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 298.94 E-value: 1.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSPamNML 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIF 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 312828735 244 NATVEMDGLKVGTHHFKLHNKkfeklKAAGYLDKEIILGIRAEDI 288
Cdd:PRK11432 244 PATLSGDYVDIYGYRLPRPAA-----FAFNLPDGECTVGVRPEAI 283
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-247 |
1.98e-95 |
|
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: 287.08 E-value: 1.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKV 115
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 116 NEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQ 195
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312828735 196 TEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSpaMNMLNATV 247
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATV 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-220 |
1.87e-94 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 282.36 E-value: 1.87e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTY---DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKNRD 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP---VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 158 MDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDG-----DIMQVGTPR 220
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPR 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-237 |
1.45e-91 |
|
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: 274.22 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVF 82
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMAFGLKLRKV----NKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 159 DEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGS 237
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-208 |
2.01e-89 |
|
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: 267.80 E-value: 2.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN---TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVepkNRDIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP---GPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVL 208
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-320 |
2.84e-88 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 269.64 E-value: 2.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtvVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:NF040840 2 IRIENLSKDWKEFK--LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGspAMNML 243
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 244 NATVEMDG----LKVGTHHFKLHNKKFEKLKaagyldkeiiLGIRAEDIHEEPIFIQTSPETQFESEVVVSELLGSEIMV 319
Cdd:NF040840 238 EGVAEKGGegtiLDTGNIKIELPEEKKGKVR----------IGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKL 307
|
.
gi 312828735 320 H 320
Cdd:NF040840 308 T 308
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-237 |
5.89e-87 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 264.65 E-value: 5.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVF 82
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGL--TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGS 237
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-236 |
7.24e-86 |
|
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: 259.58 E-value: 7.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdnNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:cd03299 1 LKVENLSKDW--KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIG 236
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-236 |
3.62e-84 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 255.49 E-value: 3.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQNY 85
Cdd:TIGR00968 3 IANISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 86 ALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR00968 82 ALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 166 DAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIG 236
Cdd:TIGR00968 162 DAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-237 |
1.82e-83 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 258.61 E-value: 1.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGS 237
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
2.70e-80 |
|
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: 245.67 E-value: 2.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGL--TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-262 |
5.25e-78 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 243.45 E-value: 5.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:PRK10851 3 IEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKL----RKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIGSpa 239
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE-- 239
|
250 260
....*....|....*....|...
gi 312828735 240 MNMLNATVEMDGLKVGTHHFKLH 262
Cdd:PRK10851 240 VNRLQGTIRGGQFHVGAHRWPLG 262
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-235 |
1.88e-74 |
|
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: 231.38 E-value: 1.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE---RMNDVEPKN---RDIAMVFQNYALYPHMTV 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaAMSRKELRElrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQM 173
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 174 RTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFI 235
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
1.35e-73 |
|
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: 225.91 E-value: 1.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND----VEPKNRDIA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHMTVFENMAFGlklrkvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-236 |
1.79e-72 |
|
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: 229.74 E-value: 1.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEP------KNRDIAMVFQNYALYPHMTV 93
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQM 173
Cdd:TIGR01186 89 LQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 174 RTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIG 236
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-235 |
5.17e-72 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 229.22 E-value: 5.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTydnNNTV-VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK------NRDIAMV 81
Cdd:COG4175 34 LEKT---GQTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKelrelrRKKMSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG4175 111 FQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 162 LSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFI 235
Cdd:COG4175 191 FSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
3.50e-68 |
|
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: 213.51 E-value: 3.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY---DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRD--- 77
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 ---IAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALtMASRIVVLKDGDI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
4.47e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 213.75 E-value: 4.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY---DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK------ 74
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 NRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQtEALTMASRIVVLKDGDI 213
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-217 |
7.54e-68 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 212.54 E-value: 7.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 21 KDFNLHI---TDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVE------PKNRDIAMVFQNYALYPHM 91
Cdd:cd03297 11 PDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 92 TVFENMAFGLKlrKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:cd03297 91 NVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312828735 172 QMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-223 |
1.00e-66 |
|
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: 210.27 E-value: 1.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNyalyP-----HMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 157 LMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-236 |
1.32e-66 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 210.00 E-value: 1.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdnnNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:COG3840 2 LRLDDLTYRY---GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFG----LKLRKVNKkeieQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlrpgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIG 236
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
5.28e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.07 E-value: 5.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERM--NDVEPKNRdIAMV 81
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVarDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 162 LSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
2.16e-64 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 212.84 E-value: 2.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN----TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN---- 75
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 -RDIAMVFQN--YALYPHMTVFENMAFGLKLRKV-NKKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-235 |
1.34e-63 |
|
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: 202.52 E-value: 1.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRD-----I 78
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLK-LRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 158 MDEPLSNLD---AKLRVQMrteILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNcIFVAQF 234
Cdd:COG1127 165 YDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD-PWVRQF 240
|
.
gi 312828735 235 I 235
Cdd:COG1127 241 L 241
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
1.40e-61 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 198.16 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNNT---VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKNRD 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP---VTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 158 MDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVL 208
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-226 |
1.43e-61 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 197.52 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDvEPKN-----RDI 78
Cdd:COG1126 2 IEIENLHKSFGDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGL-KLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 158 MDEPLSNLDAklrvQMRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG1126 160 FDEPTSALDP----ELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-213 |
1.96e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 196.43 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-----RDI 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 159 DEPLSNLDAklrvQMRTEILKLHKRLN---TTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:COG2884 162 DEPTGNLDP----ETSWEIMELLEEINrrgTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-248 |
1.75e-60 |
|
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: 198.40 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 22 DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND------VEPKNRDIAMVFQNYALYPHMTVFE 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGLKLRKVNKKEIEqkVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLrvqmRT 175
Cdd:COG4148 97 NLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR----KA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 176 EIL----KLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPncIFVAQFIGSPAMNMLNATVE 248
Cdd:COG4148 171 EILpyleRLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP--DLLPLAGGEEAGSVLEATVA 245
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
5.61e-60 |
|
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: 192.30 E-value: 5.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYDNNNTVV-KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMV 81
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNyalyP-HM----TVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 157 LMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
1.51e-57 |
|
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: 187.32 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDN---NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDI 78
Cdd:COG1124 2 LEVRNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKafRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNY--ALYPHMTVFENMAFGLKLRKVnkKEIEQKVNEAAEILGLT-EYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-225 |
6.58e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 185.65 E-value: 6.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-----RDI 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFG-------LK--LRKVNKKEIeQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAI 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 150 VRDAKVFLMDEPLSNLDAKL-RVQMRTeILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTP--------R 220
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPaeltdavlR 240
|
....*
gi 312828735 221 EIYDA 225
Cdd:COG3638 241 EIYGG 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-234 |
1.84e-56 |
|
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: 184.24 E-value: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-----RDIAM 80
Cdd:cd03261 3 LRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLK-LRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 160 EPLSNLD---AKLRVQMrteILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNcIFVAQF 234
Cdd:cd03261 162 EPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD-PLVRQF 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-225 |
2.33e-55 |
|
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: 181.61 E-value: 2.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-----RDI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFEN--------MAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQ-MRTeILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-217 |
3.53e-55 |
|
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: 180.39 E-value: 3.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN---TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE---RMNDVEPKNR- 76
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 77 -DIAMVFQNY--ALYPHMTVFENMAFGLKLRKVNKKE--IEQKVNEAAEILGLTE-YLGRKPKALSGGQRQRVALGRAIV 150
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
5.06e-55 |
|
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: 181.47 E-value: 5.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGerMNDVEPKN-----RD 77
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlweirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNyalyPH-----MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRD 152
Cdd:TIGR04520 79 VGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 153 AKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALtMASRIVVLKDGDIMQVGTPREIY 223
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-217 |
1.10e-54 |
|
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: 178.84 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 22 DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQNYALYPHMTVFENMAFG- 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 101 ---LKLRKVNKkeieQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEI 177
Cdd:cd03298 96 spgLKLTAEDR----QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312828735 178 LKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-227 |
1.27e-54 |
|
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: 179.85 E-value: 1.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMV 81
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFG----LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 158 MDEPLSNLDakLRVQMRT-EILK-LHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPN 227
Cdd:COG1120 161 LDEPTSHLD--LAHQLEVlELLRrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPEL 230
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-215 |
2.04e-54 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 179.17 E-value: 2.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNN---NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPknrDIAM 80
Cdd:NF040729 2 LKIQNISKTFINNkkeNEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP---DRGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVL--KDGDIMQ 215
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKILE 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
8.94e-54 |
|
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: 176.57 E-value: 8.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK----NRDIA 79
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHMTVFENMAFGL-KLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 159 DEPLSNLDAklrvQMRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03262 160 DEPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
1.11e-53 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 177.00 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN---TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN----- 75
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHdQTEAL-TMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
2.41e-53 |
|
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: 176.20 E-value: 2.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE--RMNDVEPKnRDIAMV 81
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvRKEPREAR-RQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 162 LSNLDAKLRVQMRtEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYD 224
Cdd:COG4555 160 TNGLDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-226 |
3.31e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 176.05 E-value: 3.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 17 NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDI----AMVFQNYALYPHMT 92
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 93 VFENMAFG-LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLrv 171
Cdd:PRK09493 94 ALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 172 qmRTEILKLHKRLNT---TTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK09493 172 --RHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
1.46e-52 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 173.51 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 23 FNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQNYALYPHMTVFENMAFGLK 102
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 103 LR-KVNKKEiEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLH 181
Cdd:TIGR01277 97 PGlKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 312828735 182 KRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
2.41e-52 |
|
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: 181.25 E-value: 2.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY-DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL---ESITSGDFYIDGERMNDVEPKNR--D 77
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQN--YALYPhMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-226 |
3.06e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.73 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN---TVVKDFNLHITDKEfiVF--VGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--- 75
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 --RDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG1135 80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 154 KVFLMDEPLSNLDAKlrvqmrT--EILKL----HKRLNTTTIYVTHDqtealtM------ASRIVVLKDGDIMQVGTPRE 221
Cdd:COG1135 160 KVLLCDEATSALDPE------TtrSILDLlkdiNRELGLTIVLITHE------MdvvrriCDRVAVLENGRIVEQGPVLD 227
|
....*
gi 312828735 222 IYDAP 226
Cdd:COG1135 228 VFANP 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-211 |
8.45e-51 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 168.97 E-value: 8.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELklEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN----- 75
Cdd:TIGR02673 1 MIEF--HNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 156 FLMDEPLSNLDAklrvQMRTEILKLHKRLN---TTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:TIGR02673 159 LLADEPTGNLDP----DLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
8.63e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.46 E-value: 8.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMV 81
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPhMTVFENMAFGLKLRkvNKKEIEQKVNEAAEILGLTE-YLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
7.90e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 168.40 E-value: 7.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYD----NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN---- 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 -RDIAMVFQnyalYPHM-----TVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTE-YLGRKPKALSGGQRQRVALGRA 148
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 149 IVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-220 |
1.81e-49 |
|
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: 166.10 E-value: 1.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPknrDIAMVFQNYALYPHMTVFENMAF 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 100 GLK--LRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEI 177
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312828735 178 LKLHKRLNTTTIYVTHDQTEALTMASRIVVLKD------GDIMQVGTPR 220
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPR 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-222 |
1.89e-49 |
|
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: 165.82 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 13 YDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESI-----TSGDFYIDGE--RMNDVEPKN--RDIAMVFQ 83
Cdd:cd03260 9 YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKdiYDLDVDVLElrRRVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPhMTVFENMAFGLKLRKV-NKKEIEQKVNEAAEILGLTEYLGRKPKA--LSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03260 89 KPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 161 PLSNLD--AKLRVQMRteILKLHKRlnTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:cd03260 168 PTSALDpiSTAKIEEL--IAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-220 |
2.22e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 166.39 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEpknRDIAMVFQ 83
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKlrkvnkKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDI---MQVGTPR 220
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLPR 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-208 |
1.83e-48 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 162.65 E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAG-LESI--TSGDFYIDGERMNDVEPKNRDIAM 80
Cdd:COG4136 2 LSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKlRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTmASRIVVL 208
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDL 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-208 |
3.20e-48 |
|
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: 162.01 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE---RMNDVEPKN--RD-IA 79
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKfrREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312828735 160 EPLSNLDAKLRvQMRTEILKLHKRLNTTTIYVTHDqTEALTMASRIVVL 208
Cdd:TIGR03608 160 EPTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
7.51e-48 |
|
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: 161.52 E-value: 7.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY-DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN-DVEPKNRDIAMV 81
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 162 LSNLDAKLRVQMRTEILKLhkRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-213 |
7.82e-48 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 161.67 E-value: 7.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNnntVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:PRK10771 2 LKLTDITWLYHH---LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFG----LKLRKVNKkeieQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlnpgLKLNAAQR----EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-225 |
1.80e-47 |
|
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: 161.31 E-value: 1.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-----RDI 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVN--------KKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-227 |
2.92e-47 |
|
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: 163.74 E-value: 2.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 22 DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVE------PKNRDIAMVFQNYALYPHMTVFE 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGLKlrKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRT 175
Cdd:TIGR02142 95 NLRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312828735 176 EILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPN 227
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
4.92e-47 |
|
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: 157.56 E-value: 4.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNR-DIAMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMafglklrkvnkkeieqkvneaaeilglteylgrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 163 SNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-234 |
5.97e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 164.44 E-value: 5.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDG---ERMNDVE---PKNRDIAMVFQNYALYPHMTV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAElreVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQM 173
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 174 RTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQF 234
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-222 |
2.17e-46 |
|
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: 168.09 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:COG2274 473 DIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYpHMTVFENMAFGlklrkvnKKEI-EQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGR 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG-------DPDAtDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 148 AIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDqTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
5.26e-46 |
|
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: 159.45 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVK---DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLES---ITSGDFYIDGERMNDVEPKN-- 75
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 ----RDIAMVFQN-Y-ALYPHMTVFENMAFGLKL-RKVNKKEIEQKVNEAAEILGLT---EYLGRKPKALSGGQRQRVAL 145
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 146 GRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
.
gi 312828735 226 P 226
Cdd:COG0444 242 P 242
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
6.52e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 157.55 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKNRDIAMVFQ 83
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
2.35e-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: 154.87 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK-----NRDI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 159 DEPLSNLDAklrvQMRTEILKLHKRLN---TTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03292 161 DEPTGNLDP----DTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
4.99e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.64 E-value: 4.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAM 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYpHMTVFENMAFGlklrkvnKKEI-EQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRA 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 149 IVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-210 |
2.66e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 151.48 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDV-EPKNRDIAMVF 82
Cdd:COG4133 3 LEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDArEDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMAFGLKLRKVNKKEIEqkVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 163 SNLDAKlRVQMRTEILKLHKRLNTTTIYVTHDQTEALtmASRIVVLKD 210
Cdd:COG4133 160 TALDAA-GVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
3.58e-44 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 159.92 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALyPHMTVFENMAFGlklrkvNKKEIEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRA 148
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 149 IVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDqTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
1.12e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVEPKNRDIAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPH--MTVFENMAFGLK-----LRKVNKKEiEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 154 KVFLMDEPLSNLDAKlrvqMRTEILKLHKRLN---TTTIYVTHDQTEALTMASRIVVLKDGdIMQVGTPREIYDAPN 227
Cdd:COG1121 159 DLLLLDEPFAGVDAA----TEEALYELLRELRregKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
6.69e-43 |
|
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: 148.74 E-value: 6.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN---TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEP----K 74
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDArarlR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 NRDIAMVFQNYALYPHMTVFENMAFGLKLRkvNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALtMASRIVVLKDGDIMQ 215
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-218 |
9.98e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 148.62 E-value: 9.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN------- 75
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 -RDIAMVFQNYALYPHMTVFENM-AFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 154 KVFLMDEPLSNLDAKLRVQMrTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
1.96e-42 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 145.60 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNN-NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYpHMTVFENMafglklrkvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDqTEALTMASRIVVLKDG 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-223 |
1.22e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 147.19 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT--VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERM--NDVEPKNRDIA 79
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNyalyPH-----MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK13650 85 MVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEaLTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
1.85e-41 |
|
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: 142.77 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVF 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QnyalyphmtvfenmafglklrkvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312828735 163 SNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
3.00e-41 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 142.96 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVF 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QnyalyphmtvfenmafglklrkvnkkeieqkvneAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 163 SNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
3.82e-41 |
|
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: 141.63 E-value: 3.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMVFQNYALYPHMTVFENM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 98 AFGLKLRKVNKKEIEQKVNEAAEILGLTEY----LGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-223 |
1.83e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 144.03 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDI----AMVFQ--NYALYPHmTV 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRKVNKKEIEQKVNEAAEILGLT--EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312828735 172 QMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
36-226 |
5.16e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.10 E-value: 5.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN-----DVEPKNRDIAMVFQN-YA-LYPHMTVFENMAFGLKL-RKVN 107
Cdd:COG4608 50 VGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglsgrELRPLRRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIhGLAS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 108 KKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVQMRTEIL----KLHK 182
Cdd:COG4608 130 KAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD----VSIQAQVLnlleDLQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 183 RLNTTTIYVTHDqteaLTM----ASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG4608 206 ELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
6.99e-40 |
|
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: 141.04 E-value: 6.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEP---KNRDIAM 80
Cdd:cd03219 1 LEVRGLTKRFGGL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVN----------KKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-252 |
9.78e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.67 E-value: 9.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYDNN-NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND--VEPKNRDIAMV 81
Cdd:PRK13632 9 KVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNyalyPH-----MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK13632 89 FQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 157 LMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALtMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQ--- 233
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKAKids 243
|
250 260
....*....|....*....|..
gi 312828735 234 -FIG--SPAMNMLNATVEMDGL 252
Cdd:PRK13632 244 pFIYklSKKLKGIDPTYNEEEL 265
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
1.12e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 141.69 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAE--LKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND--VEPKN 75
Cdd:PRK13635 1 MKEeiIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNyalyPH-----MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:PRK13635 81 RQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTmASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
1.48e-39 |
|
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: 139.27 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEqkvnEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRtEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03268 156 GLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-213 |
1.80e-39 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 139.41 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY---DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDV------EPK 74
Cdd:TIGR02211 2 LKCENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLssneraKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 NRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMaSRIVVLKDGDI 213
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-218 |
3.01e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN---DVEPKN----- 75
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNYALYPHMTVFENMAFG-LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 155 VFLMDEPLSNLDAKLRVQmrteILKLHKRLNTTTI---YVTHDQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQ----IVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-217 |
7.99e-39 |
|
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: 137.88 E-value: 7.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT---VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDvEPKN--RDI 78
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 159 DEPLSNLDAKLRVQMRtEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03266 161 DEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-209 |
1.21e-38 |
|
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: 137.28 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVEPKNRDIAMVFQNYAL---YPhM 91
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 92 TVFENMAFGL-----KLRKVNKKEiEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:cd03235 86 SVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 312828735 167 AKLRVQMrTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLK 209
Cdd:cd03235 165 PKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-237 |
1.35e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.71 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYDNNN---TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-----R 76
Cdd:PRK11153 3 ELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 77 DIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 157 LMDEPLSNLDAklrvQMRTEILKLHK----RLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVA 232
Cdd:PRK11153 163 LCDEATSALDP----ATTRSILELLKdinrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
....*
gi 312828735 233 QFIGS 237
Cdd:PRK11153 239 EFIQS 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
3.16e-38 |
|
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: 137.48 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPknRDIA- 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGL-VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP--HRIAr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 --MV--FQNYALYPHMTVFENMA---------------FGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQR 140
Cdd:COG0411 79 lgIArtFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 141 QRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPR 220
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
..
gi 312828735 221 EI 222
Cdd:COG0411 239 EV 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
5.76e-38 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 135.40 E-value: 5.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtVVKDFNLHITDKeFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVePKNRD-----I 78
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DV-LKQPQklrrrI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 159 DEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-222 |
7.10e-38 |
|
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: 135.19 E-value: 7.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 7 EHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGermNDV--EPKN--RDIAMVF 82
Cdd:cd03265 4 ENLVKKYGDF-EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVvrEPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 163 SNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
1.44e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.43 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL-----ESITSGDFYIDGE---RMNDVE 72
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQdifKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 73 PKNRdIAMVFQNYALYPHMTVFENMAFGLKLRKV--NKKEIEQKVNEAAEILGLTE----YLGRKPKALSGGQRQRVALG 146
Cdd:PRK14247 80 LRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 147 RAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLntTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
2.92e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 134.83 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYD----NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDV----EPK- 74
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVtklpEYKr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 NRDIAMVFQNYAL--YPHMTVFENMA--------FGLKLRkVNKKEIEQKVNEAAEI-LGLTEYLGRKPKALSGGQRQRV 143
Cdd:COG1101 79 AKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRG-LTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDAKlrvqMRTEILKLHKRL----NTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPK----TAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
6.41e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 137.20 E-value: 6.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDI 78
Cdd:COG4987 332 PSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYpHMTVFENmafglkLRKVNKKEIEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN------LRLARPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 148 AIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-226 |
8.86e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 130.73 E-value: 8.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL-----ESITSGDFYIDGERM--NDVEP--KNRDIAMV 81
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPieVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHMTVFENMAFGLKLRKV--NKKEIEQKVNEAAEILGLTE----YLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK14267 91 FQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRLntTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-221 |
1.29e-35 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 129.65 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHmTVFENMAFGlklRKVNKKEieqKVNEAAEILGLTEYLGRKPKA-----------LSGGQRQRVALGRA 148
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 149 IVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
1.58e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 130.31 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE-------RMNDVEPKNR 76
Cdd:COG4598 9 LEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 77 D--------IAMVFQNYALYPHMTVFENMAFG-LKLRKVNKKEieqkVNEAAEIL----GLTEYLGRKPKALSGGQRQRV 143
Cdd:COG4598 88 RqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAE----AIERAEALlakvGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDAKLrVQmrtEILKLHKRLNT---TTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPR 220
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*..
gi 312828735 221 EIYDAPNCIFVAQFIGS 237
Cdd:COG4598 240 EVFGNPKSERLRQFLSS 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-211 |
4.03e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 4.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKN-RD----- 77
Cdd:COG1129 5 LEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP---VRFRSpRDaqaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMTVFENMAFGLKLRK---VNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 155 VFLMDEPLSNLDAKlrvqmrtEILKLHKRLN------TTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:COG1129 161 VLILDEPTASLTER-------EVERLFRIIRrlkaqgVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-222 |
7.39e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 128.28 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVepKNRDIAMVF-- 82
Cdd:COG4604 3 EIKNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT--PSRELAKRLai 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 --QNYALYPHMTVFENMAFG--------LKlrkvnkKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRD 152
Cdd:COG4604 80 lrQENHINSRLTVRELVAFGrfpyskgrLT------AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 153 AKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
36-226 |
9.30e-35 |
|
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: 133.66 E-value: 9.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESiTSGDFYIDGERMNDVEPKN-----RDIAMVFQN-YA-LYPHMTVFENMAFGLKL--RKV 106
Cdd:COG4172 318 VGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVhgPGL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 107 NKKEIEQKVNEAAEILGLT-EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMrTEILK-LHKRL 184
Cdd:COG4172 397 SAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQI-LDLLRdLQREH 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312828735 185 NTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG4172 476 GLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-226 |
1.07e-34 |
|
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: 128.02 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-------- 75
Cdd:TIGR03005 1 VRFSDVTKRFGIL-TVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpade 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 -------RDIAMVFQNYALYPHMTVFENMAFGLKLRK-VNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGR 147
Cdd:TIGR03005 80 khlrqmrNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 148 AIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQP 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
2.98e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 125.47 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMnDVEPKNRdIAMVFQ 83
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312828735 164 NLDAKLRVQMRTEILKLhKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
6.12e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.06 E-value: 6.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYdNNNT-----VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdGERMNDVEPKNRD 77
Cdd:PRK13634 2 DITFQKVEHRY-QYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 -------IAMVFQnyalYPHMTVFE-----NMAFGLKLRKVNKKEIEQKVNEAAEILGLTE-YLGRKPKALSGGQRQRVA 144
Cdd:PRK13634 80 lkplrkkVGIVFQ----FPEHQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 145 LGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYD 224
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
...
gi 312828735 225 APN 227
Cdd:PRK13634 236 DPD 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-221 |
9.51e-34 |
|
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: 124.96 E-value: 9.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDN--NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMV 81
Cdd:cd03249 3 FKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPhMTVFENMAFGLKLRKVnkKEIEQ---KVNEAAEILGLTE-Y---LGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:cd03249 83 SQEPVLFD-GTIAENIRYGKPDATD--EEVEEaakKANIHDFIMSLPDgYdtlVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 155 VFLMDEPLSNLDAK--LRVQMrteilKLHK-RLNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:cd03249 160 ILLLDEATSALDAEseKLVQE-----ALDRaMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-215 |
2.80e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.77 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT---VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDV------EPK 74
Cdd:PRK11629 6 LQCDNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 NRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMaSRIVVLKDGDIMQ 215
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
3.01e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.09 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLE-----SITSGDFYIDGER-----MND 70
Cdd:PRK11264 1 MSAIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqpeagTIRVGDITIDTARslsqqKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 71 VEPKNRDIAMVFQNYALYPHMTVFENMAFG-LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAI 149
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 150 VRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIyVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
5.80e-33 |
|
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: 122.72 E-value: 5.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYpHMTVFENMAFGLklRKVNKKEIEqkvnEAAEILGLTEYLGRKPKA-----------LSGGQRQRVALGRAI 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGR--PGATREEVE----EAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 150 VRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-215 |
1.01e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 123.26 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNN--------TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE---RMN 69
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 70 DVEPK--NRDIAMVFQNY--ALYPHMTVFENMAFGLK-LRKVNKKEIEQKVNEAAEILGLT-EYLGRKPKALSGGQRQRV 143
Cdd:PRK10419 81 RAQRKafRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQ 215
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-223 |
1.32e-32 |
|
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: 121.88 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNR---DIAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 161 PLSNLDAKlRVQmrtEILKLHKRLNTTTIYV---THDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:cd03218 160 PFAGVDPI-AVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-213 |
1.34e-32 |
|
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: 121.54 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNN-NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYpHMTVFENMAFGLKLRKvnkkeiEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRA 148
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 149 IVRDAKVFLMDEPLSNLDaklrvqMRTEiLKLHKRLNT-----TTIYVTHdQTEALTMASRIVVLKDGDI 213
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD------MNSE-ERLKERLRQllgdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-229 |
1.41e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.99 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY-DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL--------ESITSGDFYIDGERMNDVEPK 74
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 nrdIAMVFQNY-ALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK13640 86 ---VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 154 KVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEAlTMASRIVVLKDGDIMQVGTPREIYDAPNCI 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-225 |
1.70e-32 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 122.40 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:PRK10253 6 ARLRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHMTVFENMAFG----LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 156 FLMDEPLSNLDaklrVQMRTEILKLHKRLNTTTIY----VTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:PRK10253 165 MLLDEPTTWLD----ISHQIDLLELLSELNREKGYtlaaVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
3.79e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.14 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDvEPKNRdIAmvfq 83
Cdd:COG4152 2 LELKGLTKRFGDK-TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRR-IG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 nY-----ALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG4152 75 -YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 159 DEPLSNLD---AKLrvqMRTEILKLHKRlNTTTIYVTH--DQTEALtmASRIVVLKDGDIMQVGTPREI 222
Cdd:COG4152 154 DEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEEL--CDRIVIINKGRKVLSGSVDEI 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-215 |
4.11e-32 |
|
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: 121.45 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN--------TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN 75
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 -----RDIAMVFQNY--ALYPHMTVFENMAFGLK-LRKVNKKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALG 146
Cdd:TIGR02769 83 rrafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 147 RAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQ 215
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-226 |
6.71e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.53 E-value: 6.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLR-------MVAGLEsiTSGDFYIDGERMN----DVEPKNRDIAMVFQ 83
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYdpdvDVVELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPhMTVFENMAFGLKLRKV-NKKEIEQKVNEAAEILGLTE----YLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 159 DEPLSNLD--AKLRVqmrtE--ILKLHKRLntTTIYVTHdqtealTM--ASRI----VVLKDGDIMQVGTPREIYDAP 226
Cdd:COG1117 179 DEPTSALDpiSTAKI----EelILELKKDY--TIVIVTH------NMqqAARVsdytAFFYLGELVEFGPTEQIFTNP 244
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-221 |
8.16e-32 |
|
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: 119.64 E-value: 8.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVFQ 83
Cdd:cd03253 3 FENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYpHMTVFENMAFGlklrKVNKKEIEqkVNEAAEILGLTEYLGRKPKA-----------LSGGQRQRVALGRAIVRD 152
Cdd:cd03253 83 DTVLF-NDTIGYNIRYG----RPDATDEE--VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 153 AKVFLMDEPLSNLDaklrVQMRTEILKLHKRL--NTTTIYVTHDQTEALTmASRIVVLKDGDIMQVGTPRE 221
Cdd:cd03253 156 PPILLLDEATSALD----THTEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-223 |
8.46e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.96 E-value: 8.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 7 EHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDG---ERMNDVEPKNRDIAMVFQ 83
Cdd:PRK13633 13 KYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NyalyPH-----MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK13633 93 N----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 159 DEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTmASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-225 |
3.97e-31 |
|
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: 124.59 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 12 TYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVFQNYALY 88
Cdd:TIGR03375 472 AYPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 89 pHMTVFENMAFGLklRKVNKKEIEqkvnEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:TIGR03375 552 -YGTLRDNIALGA--PYADDEEIL----RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 158 MDEPLSNLDaklrvqMRTEiLKLHKRLN-----TTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:TIGR03375 625 LDEPTSAMD------NRSE-ERFKDRLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
5.01e-31 |
|
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: 117.15 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK---NRDIAM 80
Cdd:cd03224 1 LEVENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFEN--MAFGLKLRKVNKKEIEqkvneaaEILG----LTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:cd03224 80 VPEGRRIFPELTVEENllLGAYARRRAKRKARLE-------RVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLhKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-222 |
5.33e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.19 E-value: 5.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAM 80
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFG----LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 157 LMDEPLSNLDAKLRVqmrtEILKLHKRLNT---TTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PRK11231 161 LLDEPTTYLDINHQV----ELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-213 |
5.46e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.59 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEpKNRDIAMVFQN- 84
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 85 -YALYPHmTVFENMAFGLKlrkvNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03226 81 dYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
1.19e-30 |
|
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: 122.22 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDN-NNTVVK---DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYI----DGERMNDVEPKN 75
Cdd:TIGR03269 280 IKVRNVSKRYISvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RD-----IAMVFQNYALYPHMTVFENM--AFGLKLRK---VNKKEIEQKV-----NEAAEILGlteylgRKPKALSGGQR 140
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGLELPDelaRMKAVITLKMvgfdeEKAEEILD------KYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 141 QRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPR 220
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 312828735 221 EI 222
Cdd:TIGR03269 514 EI 515
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-240 |
1.43e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.21 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 34 VFvGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVE------PKNRDIAMVFQNYALYPHMTVFENMAFGLKlrKVN 107
Cdd:PRK11144 29 IF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 108 KKEIEQKVneaaEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVQMRTEIL----KLHKR 183
Cdd:PRK11144 106 VAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD----LPRKRELLpyleRLARE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 184 LNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYdapncifvaqfiGSPAM 240
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW------------ASSAM 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-226 |
2.70e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 118.14 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEP-----KNRDIAMVFQN-YA-LYPHMTVFENMAFGLKLR-KVN 107
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqklLRQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 108 KKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNT 186
Cdd:PRK11308 127 AAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGL 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312828735 187 TTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK11308 207 SYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-221 |
6.24e-30 |
|
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: 120.83 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYD-NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEPKNRDIA 79
Cdd:TIGR03797 451 AIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHmTVFENMAFGLKLrkvnkkEIEQkVNEAAEILGLTEYLGRKP-----------KALSGGQRQRVALGRA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPL------TLDE-AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 149 IVRDAKVFLMDEPLSNLDAklRVQ-MRTEILklhKRLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDN--RTQaIVSESL---ERLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDE 670
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
7.43e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.74 E-value: 7.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYdNNNTVVKDFNLHITDKEfIV-FVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmndvepknrDI- 78
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE----------DIt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 ------------------AMVFQNyalyphMTVFEN-MAFgLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQ 139
Cdd:COG1137 69 hlpmhkrarlgigylpqeASIFRK------LTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 140 RQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKR----LntttiyVT-HDQTEALTMASRIVVLKDGDIM 214
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgigvL------ITdHNVRETLGICDRAYIISEGKVL 215
|
250
....*....|...
gi 312828735 215 QVGTPREIYDAPN 227
Cdd:COG1137 216 AEGTPEEILNNPL 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-208 |
7.53e-30 |
|
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: 119.70 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 12 TYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVFQNYALYP 89
Cdd:TIGR02857 330 AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 90 HmTVFENMAFGLKLRKvnkkeiEQKVNEAAEILGLTEY-----------LGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:TIGR02857 410 G-TIAENIRLARPDAS------DAEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 159 DEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDqTEALTMASRIVVL 208
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-222 |
1.05e-29 |
|
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: 114.41 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSG-DFYIDGERMNDV---EPKNRdIA 79
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdvwELRKR-IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MV---FQNYaLYPHMTVFENMA------FGLkLRKVNKKEIEqKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:COG1119 82 LVspaLQLR-FPRDETVLDVVLsgffdsIGL-YREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
1.59e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMnDVEPKN-----RDI 78
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSllevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQN-----YAlyPhmTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK13639 81 GIVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 154 KVFLMDEPLSNLDAklrvQMRTEILKLHKRLN---TTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCI 229
Cdd:PRK13639 157 EIIVLDEPTSGLDP----MGASQIMKLLYDLNkegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-225 |
4.21e-29 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 117.90 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY-DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAM 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHmTVFENMAFGlKLRKVNKKEIEqkvnEAAEILGLTEYLGRKPKA-----------LSGGQRQRVALGRAI 149
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEIE----RALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 150 VRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-223 |
5.29e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.26 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTV--VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEPKNRDIA 79
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNY-ALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 159 DEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTmASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
8.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEPKNRDIAMVFQN-YALYPHMTVFEN 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRKHIGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 97 MAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTE 176
Cdd:PRK13648 105 VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 177 ILKLHKRLNTTTIYVTHDQTEALTmASRIVVLKDGDIMQVGTPREIYD 224
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-226 |
8.20e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 114.03 E-value: 8.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE---RMNDVE--PKNRDIAMVFQN--YALYPHMT 92
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdllGMKDDEwrAVRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 93 VFENMAFGLKLR--KVNKKEIEQKVNEAAEILGLTEYL-GRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PRK15079 117 IGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 170 RVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-211 |
9.34e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.12 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE-----RMNDVEPKNRDI 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 159 DEPLSNLDAKLrvqmRTEILKLHKRLN---TTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK10908 162 DEPTGNLDDAL----SEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-222 |
1.09e-28 |
|
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: 116.68 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 16 NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVFQNYALYPHmTV 93
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMA-FGLKLRkvnkkeiEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:TIGR01842 409 AENIArFGENAD-------PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 162 LSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-235 |
1.10e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.98 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLE--HIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDI 78
Cdd:PRK10619 1 MSENKLNviDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 ---------------AMVFQNYALYPHMTVFEN-MAFGLKLRKVNKKEIEQKVNEAAEILGLTEYL-GRKPKALSGGQRQ 141
Cdd:PRK10619 80 kvadknqlrllrtrlTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 142 RVALGRAIVRDAKVFLMDEPLSNLDAKLrvqmRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
250
....*....|....*..
gi 312828735 219 PREIYDAPNCIFVAQFI 235
Cdd:PRK10619 236 PEQLFGNPQSPRLQQFL 252
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-223 |
1.44e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.41 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 24 NLHITDKEFIVFVGPSGCGKSTTLRMVAGL------ESITsGDFYIDG--ERMNDVEPKNRDIAMVFQ--NYALYPHmTV 93
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIV-GDYAIPAnlKKIKEVKRLRKEIGLVFQfpEYQLFQE-TI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRKVNKKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQ 172
Cdd:PRK13645 109 EKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 173 MRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
1.52e-28 |
|
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: 109.23 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY-DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-RD-IAM 80
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHmTVFENMafglklrkvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312828735 161 PLSNLDAKlRVQMRTEILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKDGDI 213
Cdd:cd03246 123 PNSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-214 |
1.69e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNT---VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVEPKNRD- 77
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ---DVATLDADa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 --------IAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAI 149
Cdd:PRK10535 80 laqlrrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 150 VRDAKVFLMDEPLSNLDAKLRVQMRTeILKLHKRLNTTTIYVTHDQTEAlTMASRIVVLKDGDIM 214
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-208 |
2.30e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.25 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 17 NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGermndvepkNRDIAMVFQNYAL---YPhMTV 93
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGL-----KLRKVNKkEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:NF040873 75 RDLVAMGRwarrgLWRRLTR-DDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312828735 169 LRVQMRTEILKLHKRlNTTTIYVTHDQtEALTMASRIVVL 208
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDL-ELVRRADPCVLL 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-211 |
2.86e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 109.18 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLES--ITSGDFYIDGERMNDVEPKNRdIAM 80
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03213 87 VPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 161 PLSNLDAKLRVQmrteILKLHKRL---NTTTIYVTHD-QTEALTMASRIVVLKDG 211
Cdd:cd03213 138 PTSGLDSSSALQ----VMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-211 |
3.98e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.87 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTY---DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE---RMND---VEPK 74
Cdd:PRK10584 7 VEVHHLKKSVgqgEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEearAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 75 NRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 155 VFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEAlTMASRIVVLKDG 211
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNG 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
6.68e-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: 107.13 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK---NRDIAM 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQnyalyphmtvfenmafglklrkvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-226 |
2.50e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 13 YDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--------DVEPKNRDIAMVFQN 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 85 YALYPHMTVFENMAFGLKLRKV-NKKEIEQKVNEAAEILGL----TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLntTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
5.79e-27 |
|
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: 106.60 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNR---D 77
Cdd:COG0410 1 MPMLEVENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMTVFENMAFGLKLRKvNKKEIEQKVneaAEILG----LTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADL---ERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 154 KVFLMDEPLSNLdAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG0410 156 KLLLLDEPSLGL-APLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-254 |
7.99e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.38 E-value: 7.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND---VEPKNRDIAM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQN-YALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDqTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAqfIGSPA 239
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG--LTPPS 237
|
250
....*....|....*
gi 312828735 240 MNMLNATVEMDGLKV 254
Cdd:PRK13644 238 LIELAENLKMHGVVI 252
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-222 |
1.09e-26 |
|
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: 110.99 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 16 NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGermNDVEPKNRDiamvfqnyALYPHM---- 91
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWDRE--------ELGRHIgylp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 92 --------TVFENMA-FGlklrkvnkkEIE-QKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRAIV 150
Cdd:COG4618 413 qdvelfdgTIAENIArFG---------DADpEKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-227 |
1.69e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 12 TYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEPKNRDIAMVFQN---YA 86
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNpddQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 87 LYPhmTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK13652 92 FSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 167 AKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPN 227
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-226 |
2.20e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.79 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTT----LRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVFQ- 83
Cdd:PRK15134 292 LKRTVDHN-VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 -NYALYPHMTVFENMAFGLKL--RKVNKKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK15134 371 pNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 160 EPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-260 |
2.30e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.36 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVK----DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYI------DGERMNDVEP 73
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 KNRDIAMVFQnyalYPHMTVFE-----NMAFGLKLRKVNKKEIEQKVNEAAEILGLT-EYLGRKPKALSGGQRQRVALGR 147
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 148 AIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDApn 227
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-- 234
|
250 260 270
....*....|....*....|....*....|....
gi 312828735 228 cifvAQFIGSPAMNMLNATVEMDGL-KVGTHHFK 260
Cdd:PRK13643 235 ----VDFLKAHELGVPKATHFADQLqKTGAVTFE 264
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
2.60e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.97 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNyalyPH-----MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK13647 85 FQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 157 LMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPR 220
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-226 |
3.34e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.24 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 13 YDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL-----ESITSGDFYIDGE-----RMNDVEPKnRDIAMVF 82
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHniyspRTDTVDLR-KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPhMTVFENMAFGLKLRKVNKKEIEQKVNE----AAEILG-LTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkslkGASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 158 MDEPLSNLDAKLRVQMRTEILKLHKRLntTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
3.39e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.96 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdnnNTVV--KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKN-RD--- 77
Cdd:COG3845 6 LELRGITKRF---GGVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP---VRIRSpRDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 --IAMVFQNYALYPHMTVFENMAFGL---KLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRD 152
Cdd:COG3845 80 lgIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 153 AKVFLMDEPLSNLdaklrvqmrT--------EILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:COG3845 160 ARILILDEPTAVL---------TpqeadelfEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-226 |
5.69e-26 |
|
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: 108.62 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTT----LRMVAGLESITSGDFYIDGERMNDVEPKN------RDIAM 80
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQN--YALYPHMTVFENMAFGLKL-RKVNKKEIEQKVNEAAEILGLTE---YLGRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG4172 97 IFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 155 VFLMDEPLSNLDAKLRVQmrteILKL----HKRLNTTTIYVTHDqteaLT----MASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:COG4172 177 LLIADEPTTALDVTVQAQ----ILDLlkdlQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-194 |
7.07e-26 |
|
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: 108.60 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNyalyPHM---TVFENMAFGlklrkvNKKEIEQKVNEAAEILGLTEYLGRKP-----------KALSGGQRQRVALGR 147
Cdd:TIGR02868 415 AQD----AHLfdtTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312828735 148 AIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLntTTIYVTHD 194
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-226 |
1.24e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.46 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMVFQNYAL-------- 87
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaaSRRVASVPQDTSLsfefdvrq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 88 ------YPHMTVFENMAfglklrkvnkKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK09536 97 vvemgrTPHRSRFDTWT----------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 162 LSNLDakLRVQMRTeiLKLHKRL---NTTTIYVTHDqteaLTMASR----IVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK09536 167 TASLD--INHQVRT--LELVRRLvddGKTAVAAIHD----LDLAARycdeLVLLADGRVRAAGPPADVLTAD 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-211 |
1.72e-25 |
|
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: 101.78 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 16 NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdgermndvepkNRDIAMVFQNyALYPHMTVFE 95
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----------PGSIAYVSQE-PWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGLKLRKvnkkEIEQKVNEAA------EILG---LTEyLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:cd03250 85 NILFGKPFDE----ERYEKVIKACalepdlEILPdgdLTE-IGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312828735 167 AKLRVQMRTEILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKDG 211
Cdd:cd03250 160 AHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-221 |
3.26e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEP----KNRdiAMVFQNYAL-YP 89
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaelaRRR--AVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 90 hMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVR------DAKVFLMDEPLS 163
Cdd:PRK13548 91 -FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 164 NLDakLRVQMRTeiLKLHKRL----NTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:PRK13548 170 ALD--LAHQHHV--LRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-226 |
4.94e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.48 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN-----DVEPKNRDIAMVFQN-YA-LYPHMTVFENMAFGLKL 103
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLRV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 104 RKV-NKKEIEQKVNEAAEILGLT-EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLH 181
Cdd:PRK10261 431 HGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQ 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312828735 182 KRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK10261 511 RDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-223 |
7.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.13 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 22 DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDvEPKNRDI-------AMVFQnyalYPHMTVF 94
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-TSKNKDIkqirkkvGLVFQ----FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 95 E-----NMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYL-GRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK13649 100 EetvlkDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 169 LRVQMRTEILKLHkRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13649 180 GRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-235 |
9.54e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.77 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 16 NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE--------RMNDVEPKnrdIAMVFQNYAL 87
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsRLYTVRKR---MSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 88 YPHMTVFENMAFGLKLR-KVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK11831 96 FTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 167 AKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNcIFVAQFI 235
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFL 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-213 |
9.92e-25 |
|
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: 100.30 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGermndvepknRDIAMVFQNYALYPHMTVFENM 97
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGLGGGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 98 AFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEI 177
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 312828735 178 LKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-226 |
1.60e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 100.14 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL----ESITSGDFYIDGERMNDVEPKNRDIAMVFQN--YALYPHMTV 93
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRKVNKKEIEQKVNEAAEILGL---TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 171 VQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-208 |
1.68e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.79 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMV 81
Cdd:PRK10247 8 LQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYPHmTVFENMAFGLKLRkvNKKEIEQKVNEAAEILGLTEYLGRKP-KALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIR--NQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEaLTMASRIVVL 208
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-218 |
1.75e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.54 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 24 NLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITsGDFYIDGERMNDVEPKN--RDIAMVFQNYALyPHMTVFENMAFGl 101
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 102 klrkvNKKEIEQKVNEAAEILGLTEYLGRKPKAL-----------SGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK11174 447 -----NPDASDEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 171 VQMRTEILKLHKRlnTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK11174 522 QLVMQALNAASRR--QTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-198 |
1.94e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.63 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 13 YDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESI-----TSGDFYIDGERMND--VEPKN--RDIAMVFQ 83
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYApdVDPVEvrRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHmTVFENMAFGLKLR--KVNKKE-IEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINgyKGDMDElVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLD--AKLRVQmrtEILKLHKRlNTTTIYVTHDQTEA 198
Cdd:PRK14243 178 PCSALDpiSTLRIE---ELMHELKE-QYTIIIVTHNMQQA 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-226 |
2.66e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEPKNRDIAMVFQN--YALYPHMTVFE 95
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGLKLR-KVNKKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQM 173
Cdd:PRK15112 109 ILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312828735 174 RTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK15112 189 INLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-194 |
3.64e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdgermndvePKNRDIAMVFQNY 85
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 86 ALYPHMTVFENMAFGLK--------LRKVNKK------------------------EIEQKVNEAAEILGLT-EYLGRKP 132
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAelraleaeLEELEAKlaepdedlerlaelqeefealggwEAEARAEEILSGLGFPeEDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 133 KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrvqmrtE-ILKLHKRLNT---TTIYVTHD 194
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------EsIEWLEEFLKNypgTVLVVSHD 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-221 |
4.11e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.70 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLesiTSGD-------------FYIDGERMND 70
Cdd:PRK09984 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDksagshiellgrtVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 71 VEPKNRDIAMVFQNYALYPHMTVFENMAFGLK---------LRKVNKKEiEQKVNEAAEILGLTEYLGRKPKALSGGQRQ 141
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 142 RVALGRAIVRDAKVFLMDEPLSNLDAK-LRVQMRTeiLKLHKRLNTTTIYVTHDQTE-ALTMASRIVVLKDGDIMQVGTP 219
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPEsARIVMDT--LRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSS 237
|
..
gi 312828735 220 RE 221
Cdd:PRK09984 238 QQ 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
5.56e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.81 E-value: 5.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDV---EPKNRD 77
Cdd:PRK10895 1 MATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMTVFENMAFGLKLRK-VNKKEIEQKVNEAAE---ILGLTEYLGrkpKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEefhIEHLRDSMG---QSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 154 KVFLMDEPLSNLDAKLRVQMRTEIlkLHKRLNTTTIYVT-HDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRII--EHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-226 |
7.16e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 103.10 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVePKNR---DIAMVFQNYALYpHMTVFE 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAfgLKLRKVNKKEIEQKVNEAA---EILGLT-EY---LGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR03796 572 NLT--LWDPTIPDADLVRACKDAAihdVITSRPgGYdaeLAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPE 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 169 lrvqmrTE--ILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:TIGR03796 650 ------TEkiIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
8.61e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.96 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESItSGDFYIDG----------ERMNDVEP 73
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqniyERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 KNRDIAMVFQNYALYPhMTVFENMAFGLKL----RKVNKKEIEQKVNEAAEILG-LTEYLGRKPKALSGGQRQRVALGRA 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 149 IVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKD-----GDIMQVGTPREIY 223
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
...
gi 312828735 224 DAP 226
Cdd:PRK14258 245 NSP 247
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-167 |
8.67e-24 |
|
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: 97.73 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL---ESITSGDFYIDGERMNDVEPKNRdIAMVFQNYALYPHMTVFE 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 96 NMAFG--LKLRKVNKKEIEQKVNEAAEI--LGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03234 101 TLTYTaiLRLPRKSSDAIRKKRVEDVLLrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-222 |
1.53e-23 |
|
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: 102.13 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVV-KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAM 80
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHmTVFENMAFGlklrkvNKKEIEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRAI 149
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALC------NPGAPFEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 150 VRDAKVFLMDEPLSNLDAK----LRVQMRtEILKlhkrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYEsealIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.81e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.72 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRD-IAM 80
Cdd:PRK13537 6 APIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMA-----FGLklrkvNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLvfgryFGL-----SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
2.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.38 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMnDVEPKN-----RDI 78
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQ--NYALYPhMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLtEYLGRKPK-ALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPThCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-225 |
3.44e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 10 KKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGermndvepknR-----DIAMVFQn 84
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------RvsallELGAGFH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 85 yalyPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:COG1134 101 ----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 165 LDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:COG1134 177 GDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-213 |
3.98e-23 |
|
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: 96.00 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMVFQNYALYPHmTVFEN 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 97 MAFGLKLRKVNK-KEIEQKVNEAAEI----LGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:cd03248 108 IAYGLQSCSFECvKEAAQKAHAHSFIselaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312828735 172 QMRTEILKLHKRlnTTTIYVTHdQTEALTMASRIVVLKDGDI 213
Cdd:cd03248 188 QVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
5.01e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdGERMNdvepknrdIAMVFQ 83
Cdd:COG0488 316 LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYA-LYPHMTVFENMafglklRKVNKKEIEQKVneaaeilglTEYLGR---------KP-KALSGGQRQRVALGRAIVRD 152
Cdd:COG0488 386 HQEeLDPDKTVLDEL------RDGAPGGTEQEV---------RGYLGRflfsgddafKPvGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 153 AKVFLMDEPLSNLDaklrVQMRTEILKLhkrLNT---TTIYVTHDQtEAL-TMASRIVVLKDGDI 213
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETLEALEEA---LDDfpgTVLLVSHDR-YFLdRVATRILEFEDGGV 507
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-227 |
7.80e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.95 E-value: 7.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 16 NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEP----KNRdiAMVFQNYALYPHM 91
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelaRRR--AVLPQHSSLAFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 92 TVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV-------RDAKVFLMDEPLSN 164
Cdd:COG4559 91 TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 165 LDakLRVQMRT-EILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPN 227
Cdd:COG4559 171 LD--LAHQHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-253 |
9.94e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 22 DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN-DVEPKN-----RDIAMVFQnyalYPHMTVFE 95
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNlkklrKKVSLVFQ----FPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 N-----MAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRK-PKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PRK13641 101 NtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 170 RVQMrTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIfVAQFIGSPAMNMLNATVEM 249
Cdd:PRK13641 181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL-KKHYLDEPATSRFASKLEK 258
|
....
gi 312828735 250 DGLK 253
Cdd:PRK13641 259 GGFK 262
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-223 |
1.60e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDG----ERMND--VEPKNRDIAMVFQnyalYPHMTV 93
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDkyIRPVRKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FEN-----MAFGLKLRKVNKKEIEQKVNEAAEILGLT-EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK13646 99 FEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 168 KLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-225 |
1.80e-22 |
|
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: 99.04 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEpknRDIAMVF 82
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNY-ALYPHM---TVFENMAFGLKlRKVNKKEIEQKVnEAAEI--------LGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:TIGR01193 550 INYlPQEPYIfsgSILENLLLGAK-ENVSQDEIWAAC-EIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 151 RDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRlntTTIYVTHDQTEAlTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-228 |
2.15e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDN--NNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIA 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHmTVFENMAFGLklrkvNKKEIEQKVNEAAE------ILGLTE----YLGRKPKALSGGQRQRVALGRAI 149
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGL-----TDTPDEEIMAAAKAanahdfIMEFPNgydtEVGEKGSQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 150 VRDAKVFLMDEPLSNLDAklrvQMRTEILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNC 228
Cdd:TIGR00958 633 VRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
2.33e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNN----TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGD---FYIDGE--------- 66
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKnkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 67 --------------RMNDVEPKNRDIAMVFQ--NYALYpHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTE-YLG 129
Cdd:PRK13651 82 kvleklviqktrfkKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 130 RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrvQMRTEILKLHKRLNT---TTIYVTHDQTEALTMASRIV 206
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNKqgkTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*.
gi 312828735 207 VLKDGDIMQVGTPREI 222
Cdd:PRK13651 237 FFKDGKIIKDGDTYDI 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-226 |
2.39e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.33 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL---ESITSGDFYIDG-ERMNDVEPK-NR----DIAMV 81
Cdd:PRK09473 23 STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGrEILNLPEKElNKlraeQISMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQN--YALYPHMTVFENMAFGLKLRK-VNKKE-IEQKVN--EAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK09473 103 FQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEaFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-265 |
2.55e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN----TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL-----ESITSGDFYI-----DGERMN 69
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskyGTIQVGDIYIgdkknNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 70 DVEPKN--------RDIAMVFQ--NYALYPHmTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTE-YLGRKPKALSGG 138
Cdd:PRK13631 102 NPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 139 QRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMrTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 312828735 219 PREIYDAPNCIFVAQFIGSPAMNMLNATVEMDglkvgTHHFKLHNKK 265
Cdd:PRK13631 260 PYEIFTDQHIINSTSIQVPRVIQVINDLIKKD-----PKYKKLYQKQ 301
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-217 |
2.67e-22 |
|
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: 92.38 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRD-IAMV 81
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQNYALYpHMTVFENmafglklrkvnkkeieqkvneaaeilglteyLGRKpkaLSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03247 81 NQRPYLF-DTTLRNN-------------------------------LGRR---FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 162 LSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVG 217
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-225 |
2.68e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 93.76 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVEPKNRDIAMVFQNYAL---YP---HMTVFENMAFGLKLR 104
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPisvAHTVMSGRTGHIGWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 105 KVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMrTEILKLHKRL 184
Cdd:TIGR03771 84 RRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFIELAGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312828735 185 NTTTIYVTHDQTEALTMASRiVVLKDGDIMQVGTPREIYDA 225
Cdd:TIGR03771 163 GTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDP 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-211 |
3.08e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 37 GPSGCGKSTTLRMVAGLESITSGDFYIDGERM---NDVEPKNRDIAMVFQNYALYPHMTVFENMAFGL---KLRKVNKKE 110
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELHLVPEMTVAENLYLGQlphKGGIVNRRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 111 IEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlrvqmRTEIL-KLHKRL---NT 186
Cdd:PRK11288 117 LNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR-----EIEQLfRVIRELraeGR 191
|
170 180
....*....|....*....|....*
gi 312828735 187 TTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK11288 192 VILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-225 |
3.38e-22 |
|
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: 93.70 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDNNNTVV-KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMVF 82
Cdd:cd03252 3 FEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYpHMTVFENMAFGlklrkvNKKEIEQKVNEAAEILGLTEY-----------LGRKPKALSGGQRQRVALGRAIVR 151
Cdd:cd03252 83 QENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFiselpegydtiVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 152 DAKVFLMDEPLSNLDAKL-RVQMRTeilkLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:cd03252 156 NPRILIFDEATSALDYESeHAIMRN----MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-214 |
7.01e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.78 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-RDIAMVF-QNYALYPHMTVFE 95
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRT 175
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 312828735 176 EILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIM 214
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-219 |
1.39e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 96.62 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERM-NDVEPKNRDIAMVFQNYALYPHMTVFENMA 98
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 99 FGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEIL 178
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312828735 179 KLhkRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTP 219
Cdd:TIGR01257 1106 KY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-222 |
1.51e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 95.86 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYpHMTVFENMAFGLKlRKVNKKEIEQ--KVNEAAEIL-----GLTEYLGRKPKALSGGQRQRVALGRAIVRD 152
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-EQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 153 AKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-227 |
3.07e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 23 FNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESiTSGDFYIDGERMNDVEPKN--RDIAMVFQNYALYPHMTVFENMAFG 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 101 LKlRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVR-------DAKVFLMDEPLSNLDaklrVQM 173
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD----VAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 174 RTEILKLHKRLNT---TTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPN 227
Cdd:COG4138 169 QAALDRLLRELCQqgiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-223 |
5.22e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN----DVEPKNRDIAMVFQNyalyPHMTVF 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 95 -----ENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PRK13638 92 ytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312828735 170 RVQMRTEILKLHKRLNTTTIyVTHDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-226 |
5.59e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.00 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVFQNYALYPHMTVFENMAFGL-----KLRKVNK 108
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELVAIGRypwhgALGRFGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 109 KEiEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTT 188
Cdd:PRK10575 123 AD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTV 201
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 312828735 189 IYVTHDqteaLTMASR----IVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK10575 202 IAVLHD----INMAARycdyLVALRGGEMIAQGTPAELMRGE 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-224 |
6.36e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.07 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN-RDIAMVF-QNYALYPHMTVFENm 97
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFaRRIGVVFgQRSQLWWDLPAIDS- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 98 aFGL--KLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRT 175
Cdd:COG4586 117 -FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 176 EILKLHKRLNTTTIYVTHDQT--EALtmASRIVVLKDGdimqvgtpREIYD 224
Cdd:COG4586 196 FLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHG--------RIIYD 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-193 |
1.50e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRdIAMVFQNYALYPHMTVF 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 95 ENMAFGLKLRKVNKKEIEqkvnEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlRVQMR 174
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALF 166
|
170
....*....|....*....
gi 312828735 175 TEILKLHKRLNTTTIYVTH 193
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-282 |
1.62e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK---NRDIAM 80
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFG-LKLRKV------NKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 154 KVFLMDEPLSNLDAKlRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDimQVGTpREIYDAPNCIFVAQ 233
Cdd:PRK09700 165 KVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGS--SVCS-GMVSDVSNDDIVRL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 312828735 234 FIGSPAMNMLNATVEMDGLKVGTHHFKLHN---KKFEKLKAAGY-LDKEIILG 282
Cdd:PRK09700 241 MVGRELQNRFNAMKENVSNLAHETVFEVRNvtsRDRKKVRDISFsVCRGEILG 293
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-221 |
1.87e-20 |
|
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: 92.58 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIA 79
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYpHMTVFENMAFGlklR-KVNKKEIEQkVNEAAEILGLTEYL-----------GRKpkaLSGGQRQRVALGR 147
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG---RpDASEEEVEA-AARAAQIHDFIESLpdgydtrvgerGLK---LSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 148 AIVRDAKVFLMDEPLSNLDaklrvqMRTE--ILKLHKRL--NTTTIYVTH------DqtealtmASRIVVLKDGDIMQVG 217
Cdd:COG5265 508 TLLKNPPILIFDEATSALD------SRTEraIQAALREVarGRTTLVIAHrlstivD-------ADEILVLEAGRIVERG 574
|
....
gi 312828735 218 TPRE 221
Cdd:COG5265 575 THAE 578
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-218 |
2.35e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.33 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 7 EHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAMVFQN 84
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 85 YALYpHMTVFENMAFGlklrKVNKKEIEqkVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRAIVRDA 153
Cdd:PRK13657 418 AGLF-NRSIEDNIRVG----RPDATDEE--MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 154 KVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-218 |
2.92e-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: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNR---DIAM 80
Cdd:TIGR03410 1 LEVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYPHMTVFENMAFGLKLRKVNKKEIEqkvneaAEILG----LTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRKIP------DEIYElfpvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 157 LMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-209 |
3.31e-20 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 87.60 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 12 TYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEpKNRDIAMVFQNYALYPH 90
Cdd:PRK13543 18 AFSRNEEpVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 91 MTVFENMAFglkLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlR 170
Cdd:PRK13543 97 LSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-G 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 312828735 171 VQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLK 209
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-224 |
1.77e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMND-VEPKNRDIAMVF 82
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENM-AFGLKLRkVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK13536 121 QFDNLDLEFTVRENLlVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 162 LSNLDAKLRvQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYD 224
Cdd:PRK13536 200 TTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-236 |
2.25e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSG-----DFYIDGERM---NDVEPKNRDIAMVFQNYALYP 89
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 90 hMTVFENMAFGLKLRK-VNKKEI----EQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKlVPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 165 LDAKLRVQMRTEILKLHKRLntTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIFVAQFIG 236
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-218 |
2.27e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.50 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 2 AELKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDV-EPKNRD-I 78
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAALRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHmTVFENMAFGL------KLRKV-NKKEIEQKVNEAAeilGLTEYLGRKPKALSGGQRQRVALGRAIVR 151
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAApnasdeALIEVlQQVGLEKLLEDDK---GLNAWLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 152 DAKVFLMDEPLSNLDAklrvqmRTE--ILKL---HKRlNTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK11160 493 DAPLLLLDEPTEGLDA------ETErqILELlaeHAQ-NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGT 556
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-193 |
2.96e-19 |
|
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: 84.72 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK-NRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNKK 109
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFWAAIHGGAQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 110 EIEqkvnEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlRVQMRTEILKLHKRLNTTTI 189
Cdd:TIGR01189 107 TIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLARGGIVL 181
|
....
gi 312828735 190 YVTH 193
Cdd:TIGR01189 182 LTTH 185
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
3-222 |
3.02e-19 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 89.18 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN--RDIAM 80
Cdd:TIGR01192 334 AVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESlrKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 81 VFQNYALYpHMTVFENMAFGlklrkvNKKEIEQKVNEAAEILGLTEYL-----------GRKPKALSGGQRQRVALGRAI 149
Cdd:TIGR01192 414 VFQDAGLF-NRSIRENIRLG------REGATDEEVYEAAKAAAAHDFIlkrsngydtlvGERGNRLSGGERQRLAIARAI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 150 VRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAH-RLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
4.97e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.72 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYDNNNT---VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL----ESITSGDFYIDGERMNDVEP 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 KNR------DIAMVFQN--YALYPHMTVFENMAFGLKLRKV-NKKEIEQKVNEAAEILGLTEYLGR---KPKALSGGQRQ 141
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 142 RVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*
gi 312828735 222 IYDAP 226
Cdd:PRK11022 241 IFRAP 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-211 |
8.47e-19 |
|
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: 83.92 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 12 TYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFY-----IDGERMNDVEPKNR-DIAMVFQNY 85
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRySVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 86 ALYpHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEI----LGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03290 89 WLL-NATVEENITFGSPFNKQRYKAVTDACSLQPDIdllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312828735 162 LSNLDAKLRVQ-MRTEILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKDG 211
Cdd:cd03290 168 FSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-226 |
1.39e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDG------------------ERMNDVepKNRDIAMV 81
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielseqsaAQMRHV--RGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 82 FQN--YALYPHMTVFENMAFGLKLRKVNKKEieQKVNEAAEILGLT------EYLGRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASRE--EAMVEAKRMLDQVripeaqTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 154 KVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-213 |
1.54e-18 |
|
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: 82.09 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK---NRDIAMV---FQNYALYPHMT 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 93 VFENMAFGLklrkvnkkeieqkvneaaeilglteylgrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQ 172
Cdd:cd03215 95 VAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312828735 173 MRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:cd03215 143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-207 |
6.99e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 82.07 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDnnntvvkDFNLHIT-----DKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVEPKNRDIAMVFQ 83
Cdd:cd03237 6 MKKTLG-------EFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---TVSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 nyalyphMTVFENMAFGLKlrkvNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03237 76 -------GTVRDLLSSITK----DFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312828735 164 NLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVV 207
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-213 |
7.44e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEfIV-FVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKN-RD-----IAMVFQN---YALY 88
Cdd:COG1129 267 VVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKP---VRIRSpRDairagIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 89 PHMTVFENMAFGL--KLRK---VNKKEIEQKVNEAAEILGL-TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG1129 343 LDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 163 SNLD--AKlrvqmrTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:COG1129 423 RGIDvgAK------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-219 |
1.07e-17 |
|
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: 81.00 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTY-DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTT----LRMVagleSITSGDFYIDGERMNDVEPKN-- 75
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNYALYPHmTVFENMA-FGLKlrkvnkkeIEQKVNEAAEILGLTEYLGRKPKAL-----------SGGQRQRV 143
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNLDpFGEY--------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRtEILKlHKRLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTP 219
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQ-KTIR-EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-218 |
1.41e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.00 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK--NRDIAMVFQ 83
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHmTVFENMAFGlklRKVNkkeiEQKVNEAAEILGLTEY-----------LGRKPKALSGGQRQRVALGRAIVRD 152
Cdd:PRK10790 423 DPVVLAD-TFLANVTLG---RDIS----EEQVWQALETVQLAELarslpdglytpLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 153 AKVFLMDEPLSNLDAKLRvQMRTEILKLhKRLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK10790 495 PQILILDEATANIDSGTE-QAIQQALAA-VREHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-229 |
1.97e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDG---ERMNDVEPKNRDIAMVFQNYALYPHMTVFEN 96
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhiEGLPGHQIARMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 97 MAFG-------------LKLRKVNKKEIEqKVNEAA---EILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11300 101 LLVAqhqqlktglfsglLKTPAFRRAESE-ALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCI 229
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-225 |
3.13e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtVVK--DFNLHitDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRD---I 78
Cdd:PRK15439 12 LCARSISKQYSGVE-VLKgiDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 79 AMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEaaeiLGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAA----LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 159 DEPLSNLDAKLRVQMRTEILKLHKrLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDA 225
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-214 |
5.47e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAELKLEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN---RD 77
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMTVFENMAFGLKLrkVNKKEIEQKVNEAAEILG-LTEYLGRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 157 LMDEPLSNLDAKLRVQMRTEILKLhkRLNTTTIY-VTHDQTEALTMASRIVVLKDGDIM 214
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL--REQGMTIFlVEQNANQALKLADRGYVLENGHVV 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-193 |
7.23e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.78 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdgermndvePKNRDIAMVFQNyalyPHM--- 91
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQR----PYLplg 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 92 TVFENMAFGLKLRKVNKKEIEqkvnEAAEILGLTEYLGR------KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:COG4178 441 TLREALLYPATAEAFSDAELR----EALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*....
gi 312828735 166 DAKLRVQMRTeilKLHKRL-NTTTIYVTH 193
Cdd:COG4178 517 DEENEAALYQ---LLREELpGTTVISVGH 542
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-218 |
8.18e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.68 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 14 DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDV---EPKNRdIAMVFQNYALYPH 90
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSWRSR-LAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 91 mTVFENMAFGLKlrKVNKKEIEQKVNEAA---EILGL-----TEyLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK10789 404 -TVANNIALGRP--DATQQEIEHVARLASvhdDILRLpqgydTE-VGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 163 SNLDAklrvqmRTEILKLHK----RLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGT 218
Cdd:PRK10789 480 SAVDG------RTEHQILHNlrqwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGN 532
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-227 |
1.98e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 12 TYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRdIAMVFQNYAL---Y 88
Cdd:PRK15056 15 TWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 89 P-------HMTVFENMAFglkLRKVNKKEiEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK15056 94 PvlvedvvMMGRYGHMGW---LRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 162 LSNLDaklrVQMRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKdGDIMQVGTPREIYDAPN 227
Cdd:PRK15056 170 FTGVD----VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAEN 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-224 |
2.21e-16 |
|
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: 80.76 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 24 NLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmndvepknrdIAMVFQNyALYPHMTVFENMAFGLKL 103
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 104 rkvnKKEIEQKVNEAAEILGLTEYL--------GRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRT 175
Cdd:TIGR00957 726 ----NEKYYQQVLEACALLPDLEILpsgdrteiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 176 EILKLHKRL-NTTTIYVTHDQTeALTMASRIVVLKDGDIMQVGTPREIYD 224
Cdd:TIGR00957 802 HVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-243 |
2.66e-16 |
|
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: 80.83 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNT-VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDvepknrDIAMVF 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMAFG-------LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 156 FLMDEPLSNLDAKLRVQMRTEILKLhKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI-YDAPNCIFVAQF 234
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkSKFGDGYIVTMK 2170
|
....*....
gi 312828735 235 IGSPAMNML 243
Cdd:TIGR01257 2171 IKSPKDDLL 2179
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-221 |
3.47e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTL-----RMVAGLEsiTSGDFYIDGERMNDVEPKNRDiAMVFQNYALYPHMTVFENMAFGLKLR- 104
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 105 --KVNKKEIEQKVNEAAEILGLTE-------YLGRKpKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlrvqMRT 175
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLQALGLRKcantrigVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF----MAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 176 EILKLHKRLNT--TTIYVTHDQ--TEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:TIGR00955 204 SVVQVLKGLAQkgKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
3.74e-16 |
|
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: 79.46 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNtVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESI--TSGDF-----------YID------ 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgYVErpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 65 ------GERM--------NDVEPKNRD----IAMVFQ-NYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLT 125
Cdd:TIGR03269 80 epcpvcGGTLepeevdfwNLSDKLRRRirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 126 EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHdQTEALT-MASR 204
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDK 238
|
250
....*....|....*...
gi 312828735 205 IVVLKDGDIMQVGTPREI 222
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-227 |
4.53e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 23 FNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESiTSGDFYIDGERMNDVEP-------------KNRDIAM-VFQNYALY 88
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAaelarhraylsqqQTPPFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 89 PHmtvfenmafglklRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVR-------DAKVFLMDEP 161
Cdd:PRK03695 94 QP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 162 LSNLDAKLRVQMRTeILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAPN 227
Cdd:PRK03695 161 MNSLDVAQQAALDR-LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-226 |
7.84e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 14 DNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL-----ESITSGDFYIDGERM-NDVEPKNR-----DIAMVF 82
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLlHASEQTLRgvrgnKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QN--YALYPHMTVFENMAFGLKLRKVNKKEIEQkvneaAEILGLTEYLGRK---------PKALSGGQRQRVALGRAIVR 151
Cdd:PRK15134 99 QEpmVSLNPLHTLEKQLYEVLSLHRGMRREAAR-----GEILNCLDRVGIRqaakrltdyPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 152 DAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-208 |
7.90e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 24 NLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK-NRDIAMVFQNYALYPHMTVFENMAFGLK 102
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDLLYLGHQPGIKTELTALENLRFYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 103 LRKVNKkeiEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlRVQMRTEILKLHK 182
Cdd:PRK13538 101 LHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GVARLEALLAQHA 176
|
170 180
....*....|....*....|....*.
gi 312828735 183 RLNTTTIYVTHDQTEALTMASRIVVL 208
Cdd:PRK13538 177 EQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
21-226 |
8.89e-16 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 76.02 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 21 KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDF-YIDGERMND-----VEPKNRDIA-----MVFQNYALYP 89
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELelyqlSEAERRRLMrtewgFVHQNPRDGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 90 HMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEY-LGR---KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR02323 100 RMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRiddLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 166 DAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:TIGR02323 180 DVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-211 |
9.85e-16 |
|
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: 75.55 E-value: 9.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNN------TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGD-FYIDGERMNDV---EP 73
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSiLVRHDGGWVDLaqaSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 knRDIAMVFQNYALY--------PHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKA-LSGGQRQRVA 144
Cdd:COG4778 85 --REILALRRRTIGYvsqflrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPAtFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 145 LGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLhKRLNTTTIYVTHDQ--TEALtmASRIVVLKDG 211
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEevREAV--ADRVVDVTPF 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-166 |
9.93e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPknRDIA-------MVfQNYALYPH 90
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDA--GDIAtrrrvgyMS-QAFSLYGE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 91 MTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:NF033858 354 LTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-250 |
2.88e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGL--ESITSGDFYIDGERMndVEPKNRDIAMVFQNYALYPHMTVFENMAFGLKLRKVNK 108
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKP--TKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 109 KEIEQKVNEAAEI---LGLTE----YLGRK-PKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKL 180
Cdd:PLN03211 173 LTKQEKILVAESViseLGLTKcentIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312828735 181 HKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREiydapnCIFVAQFIG-SPAMNMLNATVEMD 250
Cdd:PLN03211 253 AQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD------AMAYFESVGfSPSFPMNPADFLLD 317
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-195 |
4.46e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDgermndvepknrdiamvFQNYALYPHMTVFENM 97
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 98 AfglklrkvnkkeIEQKVNEAAEIL---GLTE---YLgRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:COG2401 107 G------------RKGDFKDAVELLnavGLSDavlWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....
gi 312828735 172 QMRTEILKLHKRLNTTTIYVTHDQ 195
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHY 197
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
6.92e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTT----LRMV-AGLESiTSGDFYIDGERMNDVEPKNRDIAMVFQN--YALYPhmt 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 93 vFENMAFGLK--LRKVNKKEIEQKVNEAAEILGLTE---YLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDa 167
Cdd:PRK10418 95 -LHTMHTHARetCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 168 kLRVQMRteILKLHKRLNTT----TIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK10418 173 -VVAQAR--ILDLLESIVQKralgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
1.08e-14 |
|
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: 70.56 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFyidgermndVEPKNRDIAMVFQ 83
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------TWGSTVKIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 nyalyphmtvfenmafglklrkvnkkeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 312828735 164 NLDAKLRVQMRTEIlklhKRLNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:cd03221 100 HLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-196 |
1.42e-14 |
|
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: 70.65 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdgermndvePKNRDIAMVFQ 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NyalyPHMTVfenmafGLkLRkvnkkeieqkvneaaEILglteylgRKP--KALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03223 72 R----PYLPL------GT-LR---------------EQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|....*
gi 312828735 162 LSNLDaklrVQMRTEILKLHKRLNTTTIYVTHDQT 196
Cdd:cd03223 119 TSALD----EESEDRLYQLLKELGITVISVGHRPS 149
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-174 |
1.53e-14 |
|
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: 71.37 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK-NRDIAMVFQNYALYPHMTVFENMAFglkLRKVNKK 109
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRF---WHADHSD 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 110 EieqKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD----AKLRVQMR 174
Cdd:cd03231 104 E---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMA 169
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-245 |
1.85e-14 |
|
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: 72.97 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 17 NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmndvepknrdIAMVFQNYALYPHmTVFEN 96
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 97 MAFGLKLRKVNKKEIEQKVNEAAEILGLTE----YLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQ 172
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEkdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 173 M-RTEILKLHKrlNTTTIYVThDQTEALTMASRIVVLKDGDIMQVGTPREIYDA-PNciFVAQFIGSPAMNMLNA 245
Cdd:cd03291 198 IfESCVCKLMA--NKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLrPD--FSSKLMGYDTFDQFSA 267
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-170 |
2.53e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 70.67 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 13 YDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNrdIAMVFQNYALYPHMT 92
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 93 VFENMAFGLKLrkVNKKEIeqkVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK13541 87 VFENLKFWSEI--YNSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-288 |
3.33e-14 |
|
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: 66.45 E-value: 3.33e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312828735 236 GSPAMNMLNATVEMDGLKVGTHHFKLHNKKFEKLKAAGYLDKEIILGIRAEDI 288
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGGVTLPLPEGQVLALKLYVGKEVILGIRPEHI 53
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-194 |
4.89e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.45 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdGERMndvepknrDIAMvFQNY--ALYPHMTVFE 95
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL--------EVAY-FDQHraELDPEKTVMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGlklrkvnKKEIEqkVN-EAAEILG-LTEYL-----GRKP-KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDa 167
Cdd:PRK11147 403 NLAEG-------KQEVM--VNgRPRHVLGyLQDFLfhpkrAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD- 472
|
170 180 190
....*....|....*....|....*....|.
gi 312828735 168 klrvqmrTEILKLHKRLNT----TTIYVTHD 194
Cdd:PRK11147 473 -------VETLELLEELLDsyqgTVLLVSHD 496
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-211 |
4.93e-14 |
|
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: 69.98 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGlesITSGDFYIDGE-RMNDVEPK------NRDIAMVFQNYAL 87
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDiHYNGIPYKefaekyPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 88 YPHMTVFENMAFGLKLRKvnkkeieqkvneaaeilglTEYLgrkpKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03233 95 FPTLTVRETLDFALRCKG-------------------NEFV----RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312828735 168 KLRVQMRTEILKLHKRLNTTTIyVTHDQT--EALTMASRIVVLKDG 211
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEG 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-210 |
6.91e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 5 KLEHIKKT--------YDNNNTV--VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYI-DGERMNDVEP 73
Cdd:PTZ00265 376 KLKDIKKIqfknvrfhYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 K--NRDIAMVFQN-------------YALYPhMTVFENMA---------------------------FGLKLRKVNKKE- 110
Cdd:PTZ00265 456 KwwRSKIGVVSQDpllfsnsiknnikYSLYS-LKDLEALSnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNEl 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 111 IEQKVN----EAAEILGLTE-----------------YLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PTZ00265 535 IEMRKNyqtiKDSEVVDVSKkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 312828735 170 RVQMRTEILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKD 210
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAH-RLSTIRYANTIFVLSN 654
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
7.05e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 1 MAE--LKLEHIKKTYDnnntVVK---DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL--ESITSGDFYIDGErmnDVEP 73
Cdd:PRK13549 1 MMEylLEMKNITKTFG----GVKaldNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGE---ELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 KN-RD-----IAMVFQNYALYPHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEIL---GLTEYLGRKPKALSGGQRQRVA 144
Cdd:PRK13549 74 SNiRDteragIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqlKLDINPATPVGNLGLGQQQLVE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 145 LGRAIVRDAKVFLMDEPLSNLDAKlRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-195 |
7.55e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLES--ITSGDFYIDGERMNDVEPKNRD---IAMVFQNYALYP 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 90 HMTV--FENMAFGLKLRKVNKKEIE-----QKVNEAAEILGLTE-YLGRK-PKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:CHL00131 98 GVSNadFLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 312828735 161 PLSNLDAKLRVQMRTEILKLhKRLNTTTIYVTHDQ 195
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKL-MTSENSIILITHYQ 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-207 |
8.87e-14 |
|
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: 72.51 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDnnntvvkDFNLH-----ITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDF-----------YIDGERmndve 72
Cdd:COG1245 347 LTKSYG-------GFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYISPDY----- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 73 pknrdiamvfqnyalypHMTVFENmafglkLRKVNKKEIEQKV--NEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIV 150
Cdd:COG1245 415 -----------------DGTVEEF------LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 151 RDAKVFLMDEPLSNLDaklrVQMRTEILKLHKRL----NTTTIYVTHDqteaLTM----ASRIVV 207
Cdd:COG1245 472 RDADLYLLDEPSAHLD----VEQRLAVAKAIRRFaenrGKTAMVVDHD----IYLidyiSDRLMV 528
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-230 |
9.05e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 7 EHIKKTYDNNNTVVKDFNLHITDKEfivfvgpSGCGKSTTLRMvaglesiTSGDFYIDGERMNDVEPKN-RDIAMVFQNY 85
Cdd:PTZ00265 1239 EQDYQGDEEQNVGMKNVNEFSLTKE-------GGSGEDSTVFK-------NSGKILLDGVDICDYNLKDlRNLFSIVSQE 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 86 ALYPHMTVFENMAFGlklRKVNKKEIEQKVNEAAEILGLTEYL--------GRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:PTZ00265 1305 PMLFNMSIYENIKFG---KEDATREDVKRACKFAAIDEFIESLpnkydtnvGPYGKSLSGGQKQRIAIARALLREPKILL 1381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 158 MDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHdQTEALTMASRIVVLKDGD-----IMQVGTPREIYDAPNCIF 230
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVY 1458
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
9.71e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 9.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL--ESITSGDFYIDGERM-----NDVEPKNr 76
Cdd:TIGR02633 2 LEMKGIVKTFGGV-KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkasniRDTERAG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 77 dIAMVFQNYALYPHMTVFENMAFG----LKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKA-LSGGQRQRVALGRAIVR 151
Cdd:TIGR02633 80 -IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 152 DAKVFLMDEPLSNLDAKlRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDimQVGT 218
Cdd:TIGR02633 159 QARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-166 |
1.11e-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: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIdGERMndvepknrDIAMVFQ 83
Cdd:TIGR03719 323 IEAENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NY-ALYPHMTVFENMAFGLKLRKVNKKEIeqkvNEAAeilglteYLGR----------KPKALSGGQRQRVALGRAIVRD 152
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGLDIIKLGKREI----PSRA-------YVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....
gi 312828735 153 AKVFLMDEPLSNLD 166
Cdd:TIGR03719 462 GNVLLLDEPTNDLD 475
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-193 |
2.15e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYD-NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN-DVEPKNRDIAMVFQ 83
Cdd:PRK13540 2 LDVIELDFDyHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENMAFGLKLRKVNkkeieQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGA-----VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 312828735 164 NLDAKLRVQMRTEIlKLHKRLNTTTIYVTH 193
Cdd:PRK13540 157 ALDELSLLTIITKI-QEHRAKGGAVLLTSH 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-222 |
2.72e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 22 DFNLHITDKEFIVFVGPSGCGKSTTLRMVAG-LESITSGDFYIDGErmndvepknrdIAMVFQNYALYpHMTVFENMAFG 100
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 101 LKLrkvNKKEIEQKVNEAA-----EIL---GLTEyLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQ 172
Cdd:PLN03130 703 SPF---DPERYERAIDVTAlqhdlDLLpggDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 173 MRTEILKLHKRlNTTTIYVThDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PLN03130 779 VFDKCIKDELR-GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-222 |
4.65e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 17 NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAG--LESITS------GDFYIDGE-----------RMNDVEPKNRD 77
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEplaaidaprlaRLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYAL-----YPHMtvfenmafglklRKVNKKEIEQK--VNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAI- 149
Cdd:PRK13547 94 PAFAFSAREIvllgrYPHA------------RRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 150 --------VRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
.
gi 312828735 222 I 222
Cdd:PRK13547 242 V 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-221 |
4.94e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 20 VKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKN---RDIAMVFQNY---ALYPHMTV 93
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 FENMAFGLKLRK---------VNKKEiEQKVNEAA-EILGLT-EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK09700 359 AQNMAISRSLKDggykgamglFHEVD-EQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 163 SNLDaklrVQMRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPRE 221
Cdd:PRK09700 438 RGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-194 |
5.15e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFyidgermnDVEPKNRDIAMVFQNYALYPHmtvFENMAFGlKLRKVNK------- 108
Cdd:COG1245 105 LGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDY---FKKLANG-EIKVAHKpqyvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 109 --------KEIEQKVNE------AAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMR 174
Cdd:COG1245 173 pkvfkgtvRELLEKVDErgkldeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVA 252
|
170 180
....*....|....*....|
gi 312828735 175 TEILKLHKRlNTTTIYVTHD 194
Cdd:COG1245 253 RLIRELAEE-GKYVLVVEHD 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-245 |
6.16e-13 |
|
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: 70.32 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmndvepknrdIAMVFQNYALYPHmTVFENMA 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 99 FGLKLRK------VNKKEIEQKVNEAAEILGLTeyLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVQ 172
Cdd:TIGR01271 509 FGLSYDEyrytsvIKACQLEEDIALFPEKDKTV--LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VV 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 173 MRTEILK--LHKRL-NTTTIYVThDQTEALTMASRIVVLKDGDIMQVGTPREIY-DAPNciFVAQFIGSPAMNMLNA 245
Cdd:TIGR01271 583 TEKEIFEscLCKLMsNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEAFDNFSA 656
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-194 |
7.46e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 67.78 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFyidgermnDVEPKNRDIAMVFQNYALYPHMTVFEN----------------MAF 99
Cdd:cd03236 32 VGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFRGSELQNYFTKLLEgdvkvivkpqyvdlipKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 100 GLKLRKV-NKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEIL 178
Cdd:cd03236 104 KGKVGELlKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIR 183
|
170
....*....|....*.
gi 312828735 179 KLHKRLNtTTIYVTHD 194
Cdd:cd03236 184 ELAEDDN-YVLVVEHD 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-194 |
9.00e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDnnntvvkDFNLH-----ITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFyidgermnDVEPKnrdIAMVFQ 83
Cdd:PRK13409 346 LTKKLG-------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK---ISYKPQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 84 NYALYPHMTVFENmafglkLRKVNKK-EIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK13409 408 YIKPDYDGTVEDL------LRSITDDlGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190
....*....|....*....|....*....|..
gi 312828735 163 SNLDAKLRVQMRTEILKLHKRLNTTTIYVTHD 194
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
31-226 |
1.26e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGLESITSG--DFYIDGERMNDV----EPKNR-----DIAMVFQNYA--LYPHMTVFEN- 96
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGevHYRMRDGQLRDLyalsEAERRrllrtEWGFVHQHPRdgLRMQVSAGGNi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 97 ----MAFGLKlrkvNKKEIEQkvnEAAEILGLTEY-LGR---KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDak 168
Cdd:PRK11701 113 gerlMAVGAR----HYGDIRA---TAGDWLERVEIdAARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-- 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 169 LRVQMRteILKLHKRL----NTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYDAP 226
Cdd:PRK11701 184 VSVQAR--LLDLLRGLvrelGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDP 243
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-226 |
2.18e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGlesITSGDFYIDGERM--NDVE-----PK------NRDIAMVFQN- 84
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---ITKDNWHVTADRFrwNGIDllklsPRerrkiiGREIAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 85 -YALYPHMTVFE-------NMAFGLKL--RKVNKKEieqkvnEAAEIL---GLTEY---LGRKPKALSGGQRQRVALGRA 148
Cdd:COG4170 99 sSCLDPSAKIGDqlieaipSWTFKGKWwqRFKWRKK------RAIELLhrvGIKDHkdiMNSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 149 IVRDAKVFLMDEPLSNLDAKLRVQmrteILKLHKRLN----TTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREIYD 224
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQ----IFRLLARLNqlqgTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
..
gi 312828735 225 AP 226
Cdd:COG4170 249 SP 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-166 |
3.65e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 7 EHIKKTYDNNntvvkdfnLHITDKEF------IVFV-GPSGCGKSTTLRMVAGLESITSGDFYIdGERMndvepknrDIA 79
Cdd:PRK11819 328 ENLSKSFGDR--------LLIDDLSFslppggIVGIiGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNY-ALYPHMTVFENMAFGLKLRKVNKKEieqkVNEAAeilglteYLGR----------KPKALSGGQRQRVALGRA 148
Cdd:PRK11819 391 YVDQSRdALDPNKTVWEEISGGLDIIKVGNRE----IPSRA-------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 312828735 149 IVRDAKVFLMDEPLSNLD 166
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-224 |
3.77e-12 |
|
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: 64.47 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 15 NNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLES--ITSGDFYIDGERMNDVEPKNR---DIAMVFQNYALYP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 90 HMTvfeNMAFglkLRKVNKKeieqkvneaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKl 169
Cdd:cd03217 91 GVK---NADF---LRYVNEG-------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 170 RVQMRTEILKLHKRLNTTTIYVTHDQTEALTM-ASRIVVLKDGDIMQVGtPREIYD 224
Cdd:cd03217 139 ALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELAL 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-211 |
4.15e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 25 LHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE----RMNDVEPKN-------------RDIAMVFQNYAL 87
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivaRLQQDPPRNvegtvydfvaegiEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 88 YPHMTVFENMAFGL-KLRKVNKK-------EIEQKVNEAAEILGLTeylGRKP-KALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK11147 104 ISHLVETDPSEKNLnELAKLQEQldhhnlwQLENRINEVLAQLGLD---PDAAlSSLSGGWLRKAALGRALVSNPDVLLL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312828735 159 DEPLSNLDaklrVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK11147 181 DEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-211 |
5.38e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHitdkefiVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN---DVEPKNRDIAMVFQNYAL 87
Cdd:PRK10982 12 KALDNVNLKVRPHSIH-------ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 88 YPHMTVFENMAFGLKLRK---VNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312828735 165 LDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-213 |
6.25e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDgermndvepknRDIAMVFQNyALYPHMTVFENMA 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------RSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 99 F-----GLKLRK-VNKKEIEQKVNEAAEilGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL--R 170
Cdd:PTZ00243 743 FfdeedAARLADaVRVSQLEADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeR 820
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312828735 171 VqMRTEIL-KLHKRlntTTIYVTHdQTEALTMASRIVVLKDGDI 213
Cdd:PTZ00243 821 V-VEECFLgALAGK---TRVLATH-QVHVVPRADYVVALGDGRV 859
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-222 |
1.04e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEfIVFV-GPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNRDIAMVF 82
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 ------QNYALYPHMTVFENMAFGL-------KLRKVNKKEIEQKVNEAAEilgltEY------LGRKPKALSGGQRQRV 143
Cdd:COG3845 337 yipedrLGRGLVPDMSVAENLILGRyrrppfsRGGFLDRKAIRAFAEELIE-----EFdvrtpgPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-213 |
1.06e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGErmnDVEPKNRD----- 77
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEdyrkl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNYALYPHMtvfenmafglkLRKVNKKEIEQKVNEAAEILGLTEYL----GR--KPKaLSGGQRQRVALGRAIVR 151
Cdd:PRK10522 399 FSAVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHKLeledGRisNLK-LSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 152 DAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQtEALTMASRIVVLKDGDI 213
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQL 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-194 |
1.14e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLESITSGDFyidgermnDVEPKNRDIAMVFQNYALYphmTVFENMAFGlKLRKVNK------- 108
Cdd:PRK13409 105 LGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSWDEVLKRFRGTELQ---NYFKKLYNG-EIKVVHKpqyvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 109 --------KEIEQKVNEA------AEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMR 174
Cdd:PRK13409 173 pkvfkgkvRELLKKVDERgkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
170 180
....*....|....*....|
gi 312828735 175 TEILKLHKrlNTTTIYVTHD 194
Cdd:PRK13409 253 RLIRELAE--GKYVLVVEHD 270
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-217 |
1.28e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAG-----LESITSGDFYiDGERMNDVEPKNR-DIAMVF 82
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITY-DGITPEEIKKHYRgDVVYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPHMTVFENMAFGLKLRK-------VNKKEIEQKVNE-AAEILGLTEYLGRKP-----KALSGGQRQRVALGRAI 149
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAARCKTpqnrpdgVSREEYAKHIADvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 150 VRDAKVFLMDEPLSNLDAKLRVQMrTEILKLHKRLNTTTIYVTHDQT--EALTMASRIVVLKDGDIMQVG 217
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEF-IRALKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFG 293
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
2.94e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.43 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 27 ITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNdVEPknrdiamvfqnyalyphmtvfenmafglklrkv 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKP--------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 107 nkkeieQKVNeaaeilglteylgrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNT 186
Cdd:cd03222 68 ------QYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|..
gi 312828735 187 TTIYVTHDQTEALTMASRIVVL 208
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVF 145
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-222 |
3.18e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKST-TLRMVAGLESiTSGDFYIDGERMNDVEPKNrdiaMVFQnYALYPHMTVFENM 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFRINES-AEGEIIIDGLNIAKIGLHD----LRFK-ITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 98 AFGLKLRKVNKKEiEQKVNEAAEILGLTEYLGRKP-----------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:TIGR00957 1375 SLRMNLDPFSQYS-DEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 167 --------AKLRVQMRT-EILKLHKRLNTTTIYvthdqtealtmaSRIVVLKDGDIMQVGTPREI 222
Cdd:TIGR00957 1454 letdnliqSTIRTQFEDcTVLTIAHRLNTIMDY------------TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-223 |
3.64e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 17 NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLR-MVAGLESITSGDFYIDGErmndvepknrdIAMVFQNYALYpHMTVFE 95
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-----------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 96 NMAFGLKL------RKVNKKEIEQKVNEAAEiLGLTEyLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PLN03232 698 NILFGSDFeserywRAIDVTALQHDLDLLPG-RDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312828735 170 RVQMRTEILKlHKRLNTTTIYVThDQTEALTMASRIVVLKDGDIMQVGTPREIY 223
Cdd:PLN03232 776 AHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-234 |
4.69e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 6 LEHIKKTYdNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFyidgERmndvEPKNRdIAMVFQNY 85
Cdd:PRK09544 7 LENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KR----NGKLR-IGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 86 ALYPHM--TVFENMAFGLKLRKVNKKEIEQKVNEAaeilglteYLGRKP-KALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK09544 77 YLDTTLplTVNRFLRLRPGTKKEDILPALKRVQAG--------HLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 163 SNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQteALTMASRIVVL-KDGDIMQVGTPREIYDAPNciFVAQF 234
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL--HLVMAKTDEVLcLNHHICCSGTPEVVSLHPE--FISMF 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-213 |
9.91e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 31 EFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK---NRDIAMVFQNY---ALYPHMTVFENMA------ 98
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaiRAGIMLCPEDRkaeGIIPVHSVADNINisarrh 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 99 ---FGLKLRkvNKKEIEqkvNEAAEILGL---TEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVQ 172
Cdd:PRK11288 360 hlrAGCLIN--NRWEAE---NADRFIRSLnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID----VG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 312828735 173 MRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:PRK11288 431 AKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
1.05e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNnTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGlesitsgdfyidgermnDVEPK--------N 75
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-----------------ELEPDsgtvkwseN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNYALY--PHMTVFENMAfglKLRKvnKKEIEQKVNEaaeilglteYLGR----------KPKALSGGQRQRV 143
Cdd:PRK15064 382 ANIGYYAQDHAYDfeNDLTLFDWMS---QWRQ--EGDDEQAVRG---------TLGRllfsqddikkSVKVLSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDaklrvqMRT-EILKLH-KRLNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD------MESiESLNMAlEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-194 |
1.19e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESitsgDFyiDGERMNDvepKNRDIAMVFQNYALYPH 90
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK----DF--NGEARPQ---PGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 91 MTVFENMAFGL--------KLRKVNKK----------------------------EIEQKVNEAAEILglteylgRKP-- 132
Cdd:TIGR03719 83 KTVRENVEEGVaeikdaldRFNEISAKyaepdadfdklaaeqaelqeiidaadawDLDSQLEIAMDAL-------RCPpw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 133 ----KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlrvqmRTEILKLH-KRLNTTTIYVTHD 194
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-----SVAWLERHlQEYPGTVVAVTHD 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-211 |
2.92e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 37 GPSGCGKSTTLRMVAglESITSGdfYI-DGERMNDVEPKN----RDIAMVFQNYALYPHMTVFENMAFGLKLR---KVNK 108
Cdd:TIGR00956 796 GASGAGKTTLLNVLA--ERVTTG--VItGGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSK 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 109 KEIEQKVNEAAEILGLTEY----LGRKPKALSGGQRQRVALGRAIVRDAKVFL-MDEPLSNLDAklrvQMRTEILKLHKR 183
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYadavVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS----QTAWSICKLMRK 947
|
170 180 190
....*....|....*....|....*....|..
gi 312828735 184 LNTT--TIYVTHDQTEALTMAS--RIVVLKDG 211
Cdd:TIGR00956 948 LADHgqAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-219 |
1.96e-09 |
|
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: 57.04 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNN-NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMN--DVEPKNRDIA 79
Cdd:cd03369 6 EIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MVFQNYALYPHmTVFENmafglkLRKVNKKEIEQ-----KVNEAAEilglteylgrkpkALSGGQRQRVALGRAIVRDAK 154
Cdd:cd03369 86 IIPQDPTLFSG-TIRSN------LDPFDEYSDEEiygalRVSEGGL-------------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312828735 155 VFLMDEPLSNL----DAKLRVQMRTE-----ILKLHKRLNTTTIYvthdqtealtmaSRIVVLKDGDIMQVGTP 219
Cdd:cd03369 146 VLVLDEATASIdyatDALIQKTIREEftnstILTIAHRLRTIIDY------------DKILVMDAGEVKEYDHP 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-205 |
2.24e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 30 KEFIVFVGPSGCGKSTTLRMVAGLESITSGDF-YIDGERMNDVEPKNRdiamvfqnyalyphmtvfenmafglklrkvnk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 109 keieqkvneaaeilgLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEI-----LKLHKR 183
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSE 114
|
170 180
....*....|....*....|..
gi 312828735 184 LNTTTIYVTHDQTEALTMASRI 205
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-211 |
2.38e-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: 56.48 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLE--SITSGDFYIDGERMndvePKN--RDIAMVFQNYALYPHMTVFENMAFGLKLRkvnkkei 111
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKtaGVITGEILINGRPL----DKNfqRSTGYVEQQDVHSPNLTVREALRFSALLR------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 112 eqkvneaaeilglteylgrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrvQMRTEILKLHKRLNTT--TI 189
Cdd:cd03232 108 ----------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVRFLKKLADSgqAI 161
|
170 180
....*....|....*....|....
gi 312828735 190 YVTHDQTEALTMAS--RIVVLKDG 211
Cdd:cd03232 162 LCTIHQPSASIFEKfdRLLLLKRG 185
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-230 |
1.26e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 55.30 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNN-NTVVKDFNLHITDKEFIVFVGPSGCGKSTT----LRMVagleSITSGDFYIDGERMNDV--EPKN 75
Cdd:cd03288 19 EIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLplHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 76 RDIAMVFQNYALYPHmtvfeNMAFGLKlrkVNKKEIEQKVNEAAEILGLTEYLGRKPKAL-----------SGGQRQRVA 144
Cdd:cd03288 95 SRLSIILQDPILFSG-----SIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 145 LGRAIVRDAKVFLMDEPLSNLDaklrvqMRTEILkLHKRLNT-----TTIYVTHDQTEALTmASRIVVLKDGDIMQVGTP 219
Cdd:cd03288 167 LARAFVRKSSILIMDEATASID------MATENI-LQKVVMTafadrTVVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
|
250
....*....|.
gi 312828735 220 REIYDAPNCIF 230
Cdd:cd03288 239 ENLLAQEDGVF 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
95-222 |
2.04e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 95 ENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMR 174
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 312828735 175 TEILKLhKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:NF000106 185 DEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-161 |
2.26e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 35 FVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDvePKNRD-----IAMVFQ----NyaLYPHMTVFENMAFGLKLRK 105
Cdd:NF033858 32 LIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRavcprIAYMPQglgkN--LYPTLSVFENLDFFGRLFG 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 106 VNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:NF033858 108 QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-194 |
3.71e-08 |
|
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: 54.80 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 33 IVF-VGPSGCGKSTTLRMVAGLESITSGDFYIDGERmndVEPKNRD-----IAMVFQNYALYPHMTVFENMAFGLKLRK- 105
Cdd:COG4615 360 LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDRLLGLDGEADPARAREl 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 106 VNKKEIEQKVNEAAEILGLTeylgrkpkALSGGQRQRVALGRAIVRDAKVFLMDE------PlsnldaklrvQMR----T 175
Cdd:COG4615 437 LERLELDHKVSVEDGRFSTT--------DLSQGQRKRLALLVALLEDRPILVFDEwaadqdP----------EFRrvfyT 498
|
170
....*....|....*....
gi 312828735 176 EILKLHKRLNTTTIYVTHD 194
Cdd:COG4615 499 ELLPELKARGKTVIAISHD 517
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-217 |
6.46e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFyidgermndvePKNRDIAMVFQNYALY 88
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 89 PHMTVFENMAFGLKLRKVNKKEIEQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312828735 169 LRVQMRTEILKLhKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVG 217
Cdd:PRK13546 178 FAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
36-175 |
6.47e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 36 VGPSGCGKSTTLRMVAGLEsiTSGdfYIDGE-RMNDVEPKNRDIAMVF----QNYALYPHMTVFENMAFGLKLR---KVN 107
Cdd:PLN03140 912 MGVSGAGKTTLMDVLAGRK--TGG--YIEGDiRISGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSAFLRlpkEVS 987
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 108 KKEIEQKVNEAAE----------ILGLTEYLGrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK-LRVQMRT 175
Cdd:PLN03140 988 KEEKMMFVDEVMElveldnlkdaIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRT 1061
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-213 |
7.91e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 23 FNLHitDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPK---NRDIAMVFQNY---ALYPHMTVFEN 96
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglANGIVYISEDRkrdGLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 97 MAFgLKLRKVNKKEIeqKVNEAAEILGLTEYLG----RKPKA------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK10762 351 MSL-TALRYFSRAGG--SLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 312828735 167 aklrVQMRTEILKL---HKRLNTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:PRK10762 428 ----VGAKKEIYQLinqFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-193 |
8.12e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.98 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGE-RMNDVEPKNRDIAMVF 82
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 83 QNYALYPhMTVFEnmafgLKLRKVNKKEIEQKVneaaEILGLTEYLGRK---------PKALSGGQRQRVALGRAIVRDA 153
Cdd:TIGR00954 532 RDQIIYP-DSSED-----MKRRGLSDKDLEQIL----DNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312828735 154 KVFLMDEPLSnldaKLRVQMRTEILKLHKRLNTTTIYVTH 193
Cdd:TIGR00954 602 QFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-226 |
1.29e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGlesITSGDFYIDGERM--NDVE-----PKNR------D 77
Cdd:PRK15093 14 KTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMrfDDIDllrlsPRERrklvghN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 78 IAMVFQNyalyPHMTVFENMAFGLKLRK-----VNKKEIEQKVN----EAAEIL---GLTEY---LGRKPKALSGGQRQR 142
Cdd:PRK15093 91 VSMIFQE----PQSCLDPSERVGRQLMQnipgwTYKGRWWQRFGwrkrRAIELLhrvGIKDHkdaMRSFPYELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 143 VALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
....
gi 312828735 223 YDAP 226
Cdd:PRK15093 247 VTTP 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-215 |
1.59e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.16 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESiTSGDFYIDGERMNdvepknrdiAMVFQNYalyph 90
Cdd:cd03289 11 KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWN---------SVPLQKW----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 91 mtvfeNMAFGLKLRKV-------------NKKEIEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALG 146
Cdd:cd03289 76 -----RKAFGVIPQKVfifsgtfrknldpYGKWSDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 147 RAIVRDAKVFLMDEPLSNLDAkLRVQMRTEILKlhKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQ 215
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLK--QAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-221 |
5.44e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 18 TVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAG-LESI--TSGDFYIDGERMNDVEPKnRDIAMVFQNYALYPHMTVF 94
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSlkVSGEITYNGYRLNEFVPR-KTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 95 ENMAFGLK----------LRKVNKKEIEQKVNEAAE------------------------ILGL-----TEYLGRKPKAL 135
Cdd:PLN03140 258 ETLDFSARcqgvgtrydlLSELARREKDAGIFPEAEvdlfmkatamegvksslitdytlkILGLdickdTIVGDEMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 136 SGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMrTEILKLHKRLNTTTIYVTHDQ--TEALTMASRIVVLKDGDI 213
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI-VKCLQQIVHLTEATVLMSLLQpaPETFDLFDDIILLSEGQI 416
|
....*...
gi 312828735 214 MQVGtPRE 221
Cdd:PLN03140 417 VYQG-PRD 423
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-213 |
5.49e-07 |
|
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: 51.36 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKkTYDNNNTVVK---DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGL-ESITSGDFYIDGERMNDVEPKN---R 76
Cdd:TIGR02633 258 LEARNLT-CWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 77 DIAMVFQN---YALYPHMTVFENMAfglkLRKVNKKEIEQKVNEAAEILGLTEYLGR-KPKA---------LSGGQRQRV 143
Cdd:TIGR02633 337 GIAMVPEDrkrHGIVPILGVGKNIT----LSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQKA 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312828735 144 ALGRAIVRDAKVFLMDEPLSNLDaklrVQMRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVD----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-166 |
7.46e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 13 YDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAG-LESITSGDFYIDGERMNDVEPKNRDIAMVFQNYALYpHM 91
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLY-MM 596
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 92 TVFENMAfglklrkvnkkeiEQKVNEAAEILGLTEYLGRKPK-ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PLN03073 597 RCFPGVP-------------EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-222 |
8.57e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGER-----MNDVEpknRDIAMVFQNYALYPHMTV 93
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfgLTDLR---RVLSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 94 F------ENMAFGLkLRKVNKKEIEQKVNEAAeiLGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PLN03232 1328 FnidpfsEHNDADL-WEALERAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 168 KLRVQMRTEIlklHKRLNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PLN03232 1405 RTDSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-213 |
1.64e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 21 KDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGDFYIDGERMNDVEPKNR-DIAMVF-----QNYALYPHMT-- 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 93 ------VFENMAFGLKlRKVNKKEIEQ-------KVNEAAEILglteylgrkpKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK15439 360 wnvcalTHNRRGFWIK-PARENAVLERyrralniKFNHAEQAA----------RTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312828735 160 EPLSNLDaklrVQMRTEILKLHKRL---NTTTIYVTHDQTEALTMASRIVVLKDGDI 213
Cdd:PRK15439 429 EPTRGVD----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| TOBE |
pfam03459 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
299-353 |
2.20e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 427310 [Multi-domain] Cd Length: 60 Bit Score: 44.58 E-value: 2.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 299 PETQFESEVVVSELLGSEIMVHSTFQGM-ELISKL--DSRTQVM--TNDKITLAFDMNKC 353
Cdd:pfam03459 1 ARNQLPGTVTVIEPLGSEVEVRVDLGGGlTLTARItrDSAEELGlaPGDEVWALIKATKV 60
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-215 |
2.24e-06 |
|
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: 49.91 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESiTSGDFYIDGERMNDVEPKNRDIAmvfqnYALYPH 90
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-----FGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 91 MTVFENMAFGLKLRKVNKKEiEQKVNEAAEILGLTEYLGRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWS-DEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 312828735 160 EPLSNLDAkLRVQMRTEILKlHKRLNTTTIYVTHdQTEALTMASRIVVLKDGDIMQ 215
Cdd:TIGR01271 1379 EPSAHLDP-VTLQIIRKTLK-QSFSNCTVILSEH-RVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-194 |
3.16e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 11 KTYDNNNTVVKDFNLHitdkeF-----IVFVGPSGCGKSTTLRMVAGLESITSGDFYIDgermndvepKNRDIAMVFQNY 85
Cdd:PRK11819 14 KVVPPKKQILKDISLS-----FfpgakIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA---------PGIKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 86 ALYPHMTVFEN-------------------MAFGL-----------------KLRKVNKKEIEQKVNEAAEILGLTEylG 129
Cdd:PRK11819 80 QLDPEKTVRENveegvaevkaaldrfneiyAAYAEpdadfdalaaeqgelqeIIDAADAWDLDSQLEIAMDALRCPP--W 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312828735 130 RKP-KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlrvqmrtEILKLHKRLNT---TTIYVTHD 194
Cdd:PRK11819 158 DAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-230 |
3.24e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 19 VVKDFNLHITDKEFIVFVGPSGCGKSTTL----RMVagleSITSGDFYIDGERMND--VEPKNRDIAMVFQNYALYPHmT 92
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-T 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 93 VFENMAFGLKLRKvnkkeieQKVNEAAEILGLTEYL-----GRKPKALSGG------QRQRVALGRAIV-RDAKVFLMDE 160
Cdd:PTZ00243 1400 VRQNVDPFLEASS-------AEVWAALELVGLRERVaseseGIDSRVLEGGsnysvgQRQLMCMARALLkKGSGFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKrlNTTTIYVTHdQTEALTMASRIVVLKDGDIMQVGTPREIYDAPNCIF 230
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFS--AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-213 |
3.89e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 58 SGDFYIDGERM---NDVEPKNRDIAMVFQN---YALYPHMTVFENMAFGLkLRKVNKKEIeqkVNEAAEILGLTEYLGR- 130
Cdd:PRK13549 317 EGEIFIDGKPVkirNPQQAIAQGIAMVPEDrkrDGIVPVMGVGKNITLAA-LDRFTGGSR---IDDAAELKTILESIQRl 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 131 KPKA---------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVQMRTEILKLHKRL---NTTTIYVTHDQTEA 198
Cdd:PRK13549 393 KVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPEV 468
|
170
....*....|....*
gi 312828735 199 LTMASRIVVLKDGDI 213
Cdd:PRK13549 469 LGLSDRVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-222 |
5.85e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 24 NLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITSGdfyidgERMNDvepknrdiamvFQNyalyPHMTVFENMA----- 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG------ERQSQ-----------FSH----ITRLSFEQLQklvsd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 99 ----------------FGLKLRKVNKKEI--EQKVNEAAEILGLTEYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK10938 82 ewqrnntdmlspgeddTGRTTAEIIQDEVkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312828735 161 PLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDGDIMQVGTPREI 222
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-211 |
6.28e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 4 LKLEHIKKTYDNnntvVK---DFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLESITS--GDFYIDGERM-----NDVEp 73
Cdd:NF040905 2 LEMRGITKTFPG----VKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdiRDSE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 74 kNRDIAMVFQNYALYPHMTVFENMAFGlklRKVNKKEI---EQKVNEAAEIL---GLTEYLGRKPKALSGGQRQRVALGR 147
Cdd:NF040905 77 -ALGIVIIHQELALIPYLSIAENIFLG---NERAKRGVidwNETNRRARELLakvGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312828735 148 AIVRDAKVFLMDEP-----------LSNLDAKLRVQMRTEILKLHKrLNtttiyvthdqtEALTMASRIVVLKDG 211
Cdd:NF040905 153 ALSKDVKLLILDEPtaalneedsaaLLDLLLELKAQGITSIIISHK-LN-----------EIRRVADSITVLRDG 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
113-213 |
6.57e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 113 QKVNEAAEILGLTEYLGRKP-KALSGGQrQRVAL-GRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRLNTTTIY 190
Cdd:PRK10938 379 KLAQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLF 457
|
90 100
....*....|....*....|....
gi 312828735 191 VTHDQTEA-LTMASRIVVLKDGDI 213
Cdd:PRK10938 458 VSHHAEDApACITHRLEFVPDGDI 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
118-193 |
3.07e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 118 AAEIL-GLT---EYLGRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKrlntTTIYVTH 193
Cdd:PLN03073 324 AASILaGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-212 |
9.02e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 3 ELKLEHIKKTYDNNntvVKDFnlhitDKEFIVFVGPSGCGKSTTLRmvaGLESITSGD---FYIDGERMNDVEPKNRDIA 79
Cdd:cd03240 3 KLSIRNIRSFHERS---EIEF-----FSPLTLIVGQNGAGKTTIIE---ALKYALTGElppNSKGGAHDPKLIREGEVRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 80 MV---FQN-----YALYPHMTVFENMAFglklrkvnkkeIEQKvneaaEILGLteyLGRKPKALSGGQRQ------RVAL 145
Cdd:cd03240 72 QVklaFENangkkYTITRSLAILENVIF-----------CHQG-----ESNWP---LLDMRGRCSGGEKVlasliiRLAL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 146 GRAIVRDAKVFLMDEPLSNLDA-KLRVQMRtEILKLHKRL-NTTTIYVTHDQtEALTMASRIV-VLKDGD 212
Cdd:cd03240 133 AETFGSNCGILALDEPTTNLDEeNIEESLA-EIIEERKSQkNFQLIVITHDE-ELVDAADHIYrVEKDGR 200
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
91-229 |
1.18e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 91 MTVFENMAF--GLKLRKVNKKEIEQKVNEAAEIL------GLtEYL--GRKPKALSGGQRQRVALGRAI------Vrdak 154
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLgflidvGL-DYLslSRAAGTLSGGEAQRIRLATQIgsgltgV---- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 155 VFLMDEPLSNLDAK--LRVqMRTeiLKLHKRLNTTTIYVTHDQtEALTMASRIVVL------KDGDIMQVGTPREIYDAP 226
Cdd:TIGR00630 511 LYVLDEPSIGLHQRdnRRL-INT--LKRLRDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEILANP 586
|
...
gi 312828735 227 NCI 229
Cdd:TIGR00630 587 DSL 589
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-211 |
1.01e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 134 ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVQMRTEILKLHKRlNTTTIYVTHDQTEALTMASRIVVLKDG 211
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-89 |
2.10e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 2.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312828735 17 NTVVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVAGLE--SITSGDFYIDGERMNDVEPKNR---DIAMVFQnyalYP 89
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YP 87
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
136-222 |
2.22e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 136 SGGQRQRVALGRAIVRDAKVFLMDEPLSNL----DAKLRVQMRTE-----ILKLHKRLNTttiyvthdqteaLTMASRIV 206
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVdvrtDALIQKTIREEfksctMLIIAHRLNT------------IIDCDRIL 1443
|
90
....*....|....*.
gi 312828735 207 VLKDGDIMQVGTPREI 222
Cdd:PLN03130 1444 VLDAGRVVEFDTPENL 1459
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
9-196 |
3.69e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.07 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 9 IKKTYDNNntvVKDFNLHITDKEFIVFVGPSGCGKSTTLRMVaglesitsgdFYIDGERM-NDVEPKNrdiamvfqnyal 87
Cdd:cd03238 3 VSGANVHN---LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------LYASGKARlISFLPKF------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312828735 88 YPHMTVFENmafglKLRKVNKkeieqkvneaaeiLGLtEY--LGRKPKALSGGQRQRVALGRAIVRDAK--VFLMDEPLS 163
Cdd:cd03238 58 SRNKLIFID-----QLQFLID-------------VGL-GYltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPST 118
|
170 180 190
....*....|....*....|....*....|...
gi 312828735 164 NLDAKLRVQMRTEILKLhKRLNTTTIYVTHDQT 196
Cdd:cd03238 119 GLHQQDINQLLEVIKGL-IDLGNTVILIEHNLD 150
|
|
| |
