|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-325 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 582.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAM 80
Cdd:COG3839 1 MASLELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSPQM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 241 NFFDGELEKKDgkyqLKVGEATVVLGGKAQELltgkgvGERKVTVGIRPEHIAFaAAPGSDTVSSKVDVSEMMGSEVYLH 320
Cdd:COG3839 240 NLLPGTVEGGG----VRLGGVRLPLPAALAAA------AGGEVTLGIRPEHLRL-ADEGDGGLEATVEVVEPLGSETLVH 308
|
....*
gi 1934240323 321 VNAVG 325
Cdd:COG3839 309 VRLGG 313
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-320 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 516.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSPQM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 241 NFFDGELEKKDGKYQLKVGEATVVLGGKAQelltgkgVGERKVTVGIRPEHIafAAAPGSDTVSSKVDVSEMMGSEVYLH 320
Cdd:PRK11650 241 NLLDGRVSADGAAFELAGGIALPLGGGYRQ-------YAGRKLTLGIRPEHI--ALSSAEGGVPLTVDTVELLGADNLAH 311
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-321 |
2.00e-157 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 444.16 E-value: 2.00e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAM 80
Cdd:COG3842 3 MPALELENVSKRYGD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGspQM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 241 NFFDGELEKKDGkyqlkvgeATVVLGGKAQELLTGKGVGE-RKVTVGIRPEHIAFAAAPGSDTVSSKVDVSEMMGSEVYL 319
Cdd:COG3842 240 NLLPGTVLGDEG--------GGVRTGGRTLEVPADAGLAAgGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRY 311
|
..
gi 1934240323 320 HV 321
Cdd:COG3842 312 RV 313
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-322 |
4.33e-154 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 436.38 E-value: 4.33e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAM 80
Cdd:PRK11000 1 MASVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSPQM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 241 NF---FDGELEKKDGKYQLKVGEATVVlggkaqeLLTGKGV--GERkVTVGIRPEHIaFAAAPGSDTVSSKVDVSEMMGS 315
Cdd:PRK11000 240 NFlpvKVTATAIEQVQVELPNRQQVWL-------PVEGRGVqvGAN-MSLGIRPEHL-LPSDIADVTLEGEVQVVEQLGN 310
|
....*..
gi 1934240323 316 EVYLHVN 322
Cdd:PRK11000 311 ETQIHIQ 317
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.26e-145 |
|
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: 408.95 E-value: 1.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-292 |
5.05e-116 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 340.00 E-value: 5.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGspQMNFF 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIF 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 244 DGE-LEKKDGKyqlkvgEATVVLGGKAQELLTGKGVGE-RKVTVGIRPEHI 292
Cdd:PRK09452 252 DATvIERLDEQ------RVRANVEGRECNIYVNFAVEPgQKLHVLLRPEDL 296
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-325 |
6.50e-116 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 338.66 E-value: 6.50e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN-DVEPKDRDIAMV 81
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGspQMN 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 242 FFDGElekkdgkyqlkVGEATVVLGGkaQELLTGKGVGERKVTVGIRPEHIAFAAAP-GSDTVSSKVDVSEMMGSEVYLH 320
Cdd:COG1118 239 VLRGR-----------VIGGQLEADG--LTLPVAEPLPDGPAVAGVRPHDIEVSREPeGENTFPATVARVSELGPEVRVE 305
|
....*
gi 1934240323 321 VNAVG 325
Cdd:COG1118 306 LKLED 310
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
4.62e-115 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 331.89 E-value: 4.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIG 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 |
2.72e-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: 326.78 E-value: 2.72e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDnKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-301 |
8.71e-107 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 315.78 E-value: 8.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMND-----VEP 73
Cdd:NF040933 1 VTVRVENVTKIFKKGkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KDRDIAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAG 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 234 FIGspQMNFFDGELEkkdgkyqlkvgEATVVLGGKAQELLTGKGVGERKVTVGIRPEHIAFAAAPGSD 301
Cdd:NF040933 241 LIG--DINLLEGKVE-----------EEGLVDGNDLKIPLPNPKLEAGEVIIGIRPEDIDISESDMRL 295
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-315 |
2.69e-101 |
|
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: 301.57 E-value: 2.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA-FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGspQM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 241 NFFDGElekKDGKYQLKVGEATVVLGGKAQELLTGkgvgerkVTVGIRPEHIAFAAAPGSD-TVSSKVDVSEMMGS 315
Cdd:TIGR03265 239 NWLPGT---RGGGSRARVGGLTLACAPGLAQPGAS-------VRLAVRPEDIRVSPAGNAAnLLLARVEDMEFLGA 304
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-315 |
5.66e-99 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 295.48 E-value: 5.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGspQMNFF 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMG--DANIF 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 244 DGELEKKdgkyQLKVGEATVVLGGKAQelltgKGVGERKVTVGIRPEHIAFAAApGSDTVSSKVDVSEMMGS 315
Cdd:PRK11432 244 PATLSGD----YVDIYGYRLPRPAAFA-----FNLPDGECTVGVRPEAITLSEQ-GEESQRCTIKHVAYMGP 305
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-294 |
4.68e-97 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 289.78 E-value: 4.68e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKK 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 115 VREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 195 QTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSpqMNFFDGELEKKDGKYQLKVGEATVVLggKAQELLT 274
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERKSEQVVLAGVEGRRC--DIYTDVP 236
|
250 260
....*....|....*....|
gi 1934240323 275 gkGVGERKVTVGIRPEHIAF 294
Cdd:TIGR01187 237 --VEKDQPLHVVLRPEKIVI 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-237 |
2.89e-94 |
|
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: 279.61 E-value: 2.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVF 82
Cdd:cd03296 2 SIEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QSYALYPHMTVYENMAFALKLRKV----PKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 159 DEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGS 237
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-237 |
3.46e-94 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 281.59 E-value: 3.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQ 83
Cdd:COG1125 4 FENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEI--LDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGS 237
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
2.83e-93 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 277.74 E-value: 2.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRmndVEPKDRD 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP---VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-322 |
8.17e-93 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 279.65 E-value: 8.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKiyDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSY 85
Cdd:NF040840 4 IENLSK--DWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:NF040840 82 MLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 166 DAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSPqmNFFDG 245
Cdd:NF040840 162 DVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 246 ELEKKDGKYQLKVGEATVVLGGKAQElltgkgvgerKVTVGIRPEHIAFAAAP----GSDTVSSKVDVSEMMGSEVYLHV 321
Cdd:NF040840 240 VAEKGGEGTILDTGNIKIELPEEKKG----------KVRIGIRPEDITISTEKvktsARNEFKGKVEEIEDLGPLVKLTL 309
|
.
gi 1934240323 322 N 322
Cdd:NF040840 310 D 310
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-239 |
1.55e-88 |
|
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: 264.93 E-value: 1.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEI--LDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 160 EPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSPQ 239
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-208 |
2.79e-88 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 263.56 E-value: 2.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPkdrDIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIM 208
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-236 |
6.69e-86 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 258.19 E-value: 6.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:TIGR00968 1 IEIANISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:TIGR00968 80 HYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIG 236
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-236 |
1.37e-85 |
|
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: 257.26 E-value: 1.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKVtaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSY 85
Cdd:cd03299 3 VENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 166 DAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIG 236
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-301 |
1.46e-85 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 262.46 E-value: 1.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSY 85
Cdd:PRK11607 22 IRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 166 DAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGSpqMNFFDG 245
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEG 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 246 ELEKK--DG--------KYQLKV-GEATVVlggkaqelltgKGVgerKVTVGIRPEHIAFAAAPGSD 301
Cdd:PRK11607 259 VLKERqeDGlvidspglVHPLKVdADASVV-----------DNV---PVHVALRPEKIMLCEEPPAD 311
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-247 |
4.16e-79 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 244.99 E-value: 4.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNkvTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMV 81
Cdd:PRK10851 2 SIEIANIKKSFGR--TQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKL---RKVP-KEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGs 237
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG- 238
|
250
....*....|
gi 1934240323 238 pQMNFFDGEL 247
Cdd:PRK10851 239 -EVNRLQGTI 247
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-235 |
2.63e-77 |
|
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: 237.54 E-value: 2.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD------RDIAMVFQSYALYPH 90
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLR 170
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 171 NQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFI 235
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-235 |
3.20e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 238.46 E-value: 3.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD------RDIAMVFQSYALYPH 90
Cdd:COG4175 40 TVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLR 170
Cdd:COG4175 120 RTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 171 NQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFI 235
Cdd:COG4175 200 REMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-211 |
2.53e-73 |
|
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: 225.45 E-value: 2.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD--- 77
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 ---IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQ 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 155 VFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMtLGDRIVIMKDG 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-211 |
2.75e-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: 223.99 E-value: 2.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMND----VEPKDRDIAMV 81
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFalklrkvpkeeidkkvreaaeilditqyldrkpkALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:cd03229 82 FQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-236 |
4.44e-73 |
|
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: 4.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEP------KDRDIAMVFQSYALYPHMT 92
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 VYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 173 MRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIG 236
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-211 |
5.80e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 222.23 E-value: 5.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATV-SLKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR 76
Cdd:COG1136 1 MSPLlELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 77 D------IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIV 150
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQtEAMTLGDRIVIMKDG 211
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDG 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-229 |
1.12e-70 |
|
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: 219.13 E-value: 1.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQsyalYP-----HMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANL 229
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
5.28e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 214.93 E-value: 5.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDnKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRM--NDVEPKDRdIAMV 81
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVarDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-298 |
1.03e-68 |
|
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: 218.43 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMND------VEPKDRDIAMVFQSYALYPHMTVYE 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 NMAFALKLRKVPKEEIDkkVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLrnqmRA 175
Cdd:COG4148 97 NLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR----KA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 176 EII----KLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGfiGSPQMNFFDGELEKKD 251
Cdd:COG4148 171 EILpyleRLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAAHD 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 252 GKYQLkvgeATVVLGGkaQELL---TGKGVGERkVTVGIRPEHIAFAAAP 298
Cdd:COG4148 249 PDYGL----TRLALGG--GRLWvprLDLPPGTR-VRVRIRARDVSLALEP 291
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-217 |
9.39e-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: 211.00 E-value: 9.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIA---DKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVE------PKDRDIAMVFQSYALYPHMT 92
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 VYENMAFALKlRKVPKEEIDKkVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:cd03297 92 VRENLAFGLK-RKRNREDRIS-VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1934240323 173 MRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-214 |
1.43e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 205.67 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDI 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 159 DEPLSNLDAklrnQMRAEIIKLRQRIN---TTFIYVTHDQTEAMTLGDRIVIMKDGFIQ 214
Cdd:COG2884 162 DEPTGNLDP----ETSWEIMELLEEINrrgTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-236 |
1.96e-64 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 203.06 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNkvTAVHdFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSY 85
Cdd:COG3840 4 LDDLTYRYGD--FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFA----LKLRKVPKeeidKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:COG3840 81 NLFPHLTVAQNIGLGlrpgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIG 236
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
4.79e-64 |
|
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: 201.54 E-value: 4.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQsyalYP-HM----TVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
5.70e-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: 210.53 E-value: 5.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYD----NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD---- 75
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -RDIAMVFQ--SYALYPHMTVYENMAFALKLRKV-PKEEIDKKVREAAEI--LDiTQYLDRKPKALSGGQRQRVAIGRAI 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERvgLP-PDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
2.18e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 200.61 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDvEPKD-----RDI 78
Cdd:COG1126 2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFAL-KLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-224 |
1.22e-61 |
|
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: 196.35 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtaVH-DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD----- 77
Cdd:COG1127 6 IEVRNLTKSFGDRV--VLdGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALK-LRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 157 LMDEPLSNLD---AKLRNQMraeIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:COG1127 164 LYDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
6.00e-61 |
|
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: 194.64 E-value: 6.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDI 78
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSY--ALYPHMTVYENMAFALKLRKVPkeEIDKKVREAAEILDIT-QYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
3.07e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 193.54 E-value: 3.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRmndVEPKDRD 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP---VTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIM 208
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-227 |
1.26e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 188.73 E-value: 1.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDI 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYEN-MAFALK--------LRKVPKEEIDKkVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAI 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvLAGRLGrtstwrslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQ-MRAeIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIqqigtpqeVFDQPA 227
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGPP 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-224 |
4.22e-57 |
|
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: 184.63 E-value: 4.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtaVH-DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RD 77
Cdd:cd03261 1 IELRGLTKSFGGRT--VLkGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALK-LRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
6.20e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 192.04 E-value: 6.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATV-SLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS---EGDLVIGGKRMNDVEPKD 75
Cdd:COG1123 1 MTPLlEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 R--DIAMVFQS--YALYPhMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR 151
Cdd:COG1123 81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANL 229
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-225 |
2.18e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 182.75 E-value: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGG--KRMNDVEPKdRDIAMVFQ 83
Cdd:COG4555 4 VENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedVRKEPREAR-RQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:COG4555 162 GLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
3.29e-56 |
|
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: 181.55 E-value: 3.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK-VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDvEPKD--RDIAM 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAarQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
4.17e-56 |
|
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: 182.01 E-value: 4.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDN---KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD----- 75
Cdd:cd03258 2 IELKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 RDIAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-217 |
5.27e-56 |
|
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: 181.55 E-value: 5.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---- 76
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 77 -DIAMVFQSY--ALYPHMTVYENMAFALKLRKVP--KEEIDKKVREAAE-ILDITQYLDRKPKALSGGQRQRVAIGRAIV 150
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVgVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-229 |
1.67e-55 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 181.01 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFA----LKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 158 MDEPLSNLDakLRNQMRA-EIIK-LRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDqPANL 229
Cdd:COG1120 161 LDEPTSHLD--LAHQLEVlELLRrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT-PELL 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
2.16e-55 |
|
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: 179.26 E-value: 2.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK----DRDIA 79
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHMTVYENMAFAL-KLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 159 DEPLSNLDAklrnQMRAEIIKLRQRI---NTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03262 160 DEPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-228 |
7.66e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 178.75 E-value: 7.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDI----A 79
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHMTVYENMAFA-LKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 159 DEPLSNLDAKLRNqmraEIIKLRQRINT---TFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:PRK09493 161 DEPTSALDPELRH----EVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-211 |
2.35e-54 |
|
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: 176.67 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDI 78
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 159 DEPLSNLDAklrnQMRAEIIKLRQRIN---TTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:TIGR02673 162 DEPTGNLDP----DLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-211 |
2.67e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.55 E-value: 2.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVF 82
Cdd:COG4619 2 ELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QSYALYPhMTVYENMAFALKLRKvpKEEIDKKVREAAEILDITQ-YLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-228 |
4.37e-54 |
|
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: 176.99 E-value: 4.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDIAM 80
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENM---AFALK------LRKVPKEEIdKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR 151
Cdd:cd03256 83 IFQQFNLIERLSVLENVlsgRLGRRstwrslFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIqqigtpqeVFDQPAN 228
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VFDGPPA 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-238 |
1.08e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 179.12 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD----- 75
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 RDIAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 156 FLMDEPLSNLDAklrnQMRAEIIKLRQRIN----TTFIYVTHDqteaM----TLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:COG1135 162 LLCDEATSALDP----ETTRSILDLLKDINrelgLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
250
....*....|.
gi 1934240323 228 NLFVAGFIGSP 238
Cdd:COG1135 234 SELTRRFLPTV 244
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-210 |
4.75e-53 |
|
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: 174.54 E-value: 4.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY--DNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPkdrDIAM 80
Cdd:NF040729 2 LKIQNISKTFinNKKENEVlKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP---DRGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKD 210
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSR 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-229 |
1.03e-52 |
|
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: 174.16 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGkrMNDVEPKD-----RD 77
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlweirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRD 152
Cdd:TIGR04520 79 VGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAmTLGDRIVIMKDGFIQQIGTPQEVFDQPANL 229
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-226 |
3.01e-52 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 171.88 E-value: 3.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPkdrDIAMVFQSYALYPHMTVYENMAFAL 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 102 K--LRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIK 179
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 180 LRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV-FDQP 226
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
3.43e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 171.59 E-value: 3.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDI-----SEGDLVIGGKRMNDVEPKD--- 75
Cdd:cd03260 1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -RDIAMVFQSYALYPhMTVYENMAFALKLRKV-PKEEIDKKVREAAEILDITQYLDRKPKA--LSGGQRQRVAIGRAIVR 151
Cdd:cd03260 80 rRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRIntTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-229 |
7.74e-52 |
|
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: 172.25 E-value: 7.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYD----NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD---- 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -RDIAMVFQsyalYPHM-----TVYENMAFALKLRKVPKEEIDKKVREAAEILDIT-QYLDRKPKALSGGQRQRVAIGRA 148
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
.
gi 1934240323 229 L 229
Cdd:TIGR04521 237 L 237
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-267 |
1.62e-51 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 173.76 E-value: 1.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVE------PKDRDIAMVFQSYALYPHMTVYE 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 NMAFALKLRKVPkeeiDKKVREAA--EILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQM 173
Cdd:TIGR02142 95 NLRYGMKRARPS----ERRISFERviELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 174 RAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAgfiGSPQMNFFDGELEKKDGK 253
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQGSLIEGVVAEHDQH 247
|
250
....*....|....
gi 1934240323 254 YQLkvgeATVVLGG 267
Cdd:TIGR02142 248 YGL----TALRLGG 257
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
5.57e-51 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 171.39 E-value: 5.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED---ISEGDLVIGGKRMNDVEPKD-- 75
Cdd:COG0444 2 LEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 ----RDIAMVFQ-SY-ALYPHMTVYENMAFALKL-RKVPKEEIDKKVREAAEILDIT---QYLDRKPKALSGGQRQRVAI 145
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 146 GRAIVRDPQVFLMDEPLSNLDAklrnQMRAEII----KLRQRINTTFIYVTHDqteamtLG------DRIVIMKDGFIQQ 215
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDV----TIQAQILnllkDLQRELGLAILFITHD------LGvvaeiaDRVAVMYAGRIVE 231
|
250
....*....|..
gi 1934240323 216 IGTPQEVFDQPA 227
Cdd:COG0444 232 EGPVEELFENPR 243
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-213 |
1.22e-50 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 167.28 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 11 KIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSYALYPH 90
Cdd:cd03298 5 KIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENMAFA----LKLRKVPKEEIDKkvreAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:cd03298 85 LTVEQNVGLGlspgLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1934240323 167 AKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-226 |
1.97e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 167.50 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN---DVEPKD---- 75
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -RDIAMVFQSYALYPHMTVYENMAFA-LKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMrAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTpQEVFDQP 226
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQP 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-226 |
2.01e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.50 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN---DVEPKD---- 75
Cdd:PRK11124 2 SIQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -RDIAMVFQSYALYPHMTVYENMAFA-LKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:PRK11124 81 rRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMrAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTpQEVFDQP 226
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQP 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
8.59e-50 |
|
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: 163.34 E-value: 8.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDvEPKD--RDIAMV 81
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEvkRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAfalklrkvpkeeidkkvreaaeilditqyldrkpkaLSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-234 |
1.39e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 170.21 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGG---KRMNDVEPKD---RDIAMVFQSYALYPHMT 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREvrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 VYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 173 MRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGF 234
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
2.63e-49 |
|
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: 163.88 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 23 FNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSYALYPHMTVYENMAF--- 99
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLglh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 -ALKLRKVPKEeidkKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEII 178
Cdd:TIGR01277 97 pGLKLNAEQQE----KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1934240323 179 KLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
5.36e-49 |
|
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: 162.96 E-value: 5.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 159 DEPLSNLDAklrnQMRAEIIKLRQRIN---TTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03292 161 DEPTGNLDP----DTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-206 |
1.58e-47 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 158.93 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGK---RMNDVEPKD--RD-IA 79
Cdd:TIGR03608 1 LKNISKKFGDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKfrREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMD 159
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 160 EPLSNLDAKLRNqmraEIIKLRQRIN---TTFIYVTHDqTEAMTLGDRIV 206
Cdd:TIGR03608 160 EPTGSLDPKNRD----EVLDLLLELNdegKTIIIVTHD-PEVAKQADRVI 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-225 |
8.19e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 167.70 E-value: 8.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:COG2274 474 IELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFAlklrkvpKEEI-DKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRA 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG-------DPDAtDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDqTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-225 |
7.68e-46 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 155.53 E-value: 7.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDIAMV 81
Cdd:TIGR02315 5 ENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENM---AFALK------LRKVPKEEIdKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRD 152
Cdd:TIGR02315 85 FQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
1.28e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDVEPKDRDIAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPH--MTVYENMAFAL----KLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQ 154
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 155 VFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQiGTPQEVFDqPANL 229
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLT-PENL 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-194 |
2.48e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 153.41 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKkIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL--EDIS-EGDLVIGGKRMNDVEPKDRDIAMV 81
Cdd:COG4136 3 SLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKlRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....
gi 1934240323 162 LSNLDAKLRNQMRAEII-KLRQRiNTTFIYVTHD 194
Cdd:COG4136 161 FSKLDAALRAQFREFVFeQIRQR-GIPALLVTHD 193
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
6.72e-45 |
|
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: 160.69 E-value: 6.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIA 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALyPHMTVYENMAFAlkLRKVPKEEIdkkvREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRA 148
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLG--RPDASDEEL----EAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDqTEAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-250 |
8.34e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 154.44 E-value: 8.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKV----TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDI 78
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 ----AMVFQ--SYALYPHmTVYENMAFALKLRKVPKEEIDKKVREAAEI--LDITQYLDRKPKALSGGQRQRVAIGRAIV 150
Cdd:PRK13637 82 rkkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLF 230
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
250 260
....*....|....*....|
gi 1934240323 231 VAGfIGSPQMNFFDGELEKK 250
Cdd:PRK13637 241 SIG-LAVPQVTYLVRKLRKK 259
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
8.56e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 150.09 E-value: 8.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVF 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QsyalyphmtvyenmafalklrkvpkeeidkkvreaaeilditqyldrkpkaLSGGQRQRVAIGRAIVRDPQVFLMDEPL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1934240323 163 SNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-227 |
3.02e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 154.12 E-value: 3.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYD----------NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEP 73
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KD-----RDIAMVFQ-SYA-LYPHMTVYENMAFALKL-RKVPKEEIDKKVREAAEI--LDiTQYLDRKPKALSGGQRQRV 143
Cdd:COG4608 88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELvgLR-PEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 144 AIGRAIVRDPQVFLMDEPLSNLDAklrnQMRAEII----KLRQRINTTFIYVTHDqteamtLG------DRIVIMKDGFI 213
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDV----SIQAQVLnlleDLQDELGLTYLFISHD------LSvvrhisDRVAVMYLGKI 236
|
250
....*....|....
gi 1934240323 214 QQIGTPQEVFDQPA 227
Cdd:COG4608 237 VEIAPRDELYARPL 250
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-217 |
3.68e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 151.75 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEpkdRDIAMVFQSY 85
Cdd:PRK11247 15 LNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFALKlrkvpkeeidKKVREAA-EILDITQYLDRK---PKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:PRK11247 91 RLLPWKKVIDNVGLGLK----------GQWRDAAlQALAAVGLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGfiqQIG 217
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-198 |
1.20e-43 |
|
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: 148.78 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDV-EPKDRDIAM 80
Cdd:COG4133 1 MMLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDArEDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDkkVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEA 198
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
2.05e-43 |
|
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: 148.67 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGkrmNDV--EPKD--RDIAMVF 82
Cdd:cd03265 4 ENLVKKYGD-FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVvrEPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 163 SNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-227 |
2.75e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 148.58 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 23 FNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSYALYPHMTVYENMAF--- 99
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 -ALKLRKVPKEeidkKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMR---A 175
Cdd:PRK10771 98 pGLKLNAAQRE----KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLtlvS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 176 EIIKLRQrinTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:PRK10771 174 QVCQERQ---LTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
3.10e-43 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 146.37 E-value: 3.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK-VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMafalklrkvpkeeidkkvreaaeilditqyldrkpkaLSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDqTEAMTLGDRIVIMKDG 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
3.47e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 156.48 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFAlklrkvpKEEI-DKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRA 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTH--DQTEAMtlgDRIVIMKDGFIQQIGTPQE 221
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHrlSTIRNA---DRILVLDDGRIVEQGTHEE 560
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-237 |
3.56e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.49 E-value: 3.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RD 77
Cdd:PRK11153 4 LKNISKVFpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 158 MDEPLSNLDAKLRNQmraeIIKLRQRINT----TFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAG 233
Cdd:PRK11153 164 CDEATSALDPATTRS----ILELLKDINRelglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....
gi 1934240323 234 FIGS 237
Cdd:PRK11153 240 FIQS 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-211 |
1.22e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 147.92 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRmndVEPKDRDIAMVFQSYALYPHMTVYENMA 98
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGPGAERGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 99 FALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEII 178
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLL 172
|
170 180 190
....*....|....*....|....*....|...
gi 1934240323 179 KLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PRK11248 173 KLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-223 |
1.41e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 148.24 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
1.37e-41 |
|
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: 144.11 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDVEPKDRD--- 77
Cdd:COG4181 9 IELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 ------IAMVFQSYALYPHMTVYENMAFALKLRKVPkeeiDKKVReAAEILD---ITQYLDRKPKALSGGQRQRVAIGRA 148
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRR----DARAR-ARALLErvgLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAmTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
1.40e-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: 142.57 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVF 82
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QsyalyphmtvyenmafalklrkvpkeeidkkvreAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPL 162
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 163 SNLDakLRNQMR--AEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03214 126 SHLD--IAHQIEllELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
2.14e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 145.26 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKVT--AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRM--NDVEPKDR 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 77 DIAMVFQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR 151
Cdd:PRK13650 82 KIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEaMTLGDRIVIMKDGFIQQIGTPQEVFDQPANL 229
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
5.57e-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: 140.09 E-value: 5.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHMTVYENM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 98 AFALKLRKVPKEEIDKKVREAAEILDITQYLDRK----PKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
5.02e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.28 E-value: 5.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVT-AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDI 78
Cdd:PRK13632 6 VMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:PRK13632 86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAmTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-211 |
5.32e-40 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 139.27 E-value: 5.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDkkvrEAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-213 |
6.56e-40 |
|
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: 139.21 E-value: 6.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDVEPKDRDIAMVFQS 84
Cdd:cd03235 1 EVEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 YAL---YPhMTVYENMAFAL-----KLRKVPKEEiDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:cd03235 77 RSIdrdFP-ISVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
6.98e-40 |
|
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: 139.25 E-value: 6.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtAVHDFNLEIaDKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVI-GGKRMNDVEPKDRDIAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 163 SNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
7-211 |
1.51e-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: 138.64 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR------D 77
Cdd:TIGR02211 5 ENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLgDRIVIMKDG 211
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-227 |
2.01e-39 |
|
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: 138.72 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---DIAMVFQSYALYPHMTV 93
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFALKLRKVP----------KEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03219 93 LENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGfiQQI--GTPQEVFDQPA 227
Cdd:cd03219 173 GLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQG--RVIaeGTPDEVRNNPR 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-211 |
2.45e-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: 2.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK---VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDvEPKD--RDI 78
Cdd:cd03266 2 ITADALTKRFRDVkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 159 DEPLSNLDAKLRNQMRaEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03266 161 DEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-237 |
2.52e-39 |
|
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: 139.19 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-------- 75
Cdd:TIGR03005 1 VRFSDVTKRFGI-LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpade 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -------RDIAMVFQSYALYPHMTVYENMAFALKLRK-VPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGR 147
Cdd:TIGR03005 80 khlrqmrNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 148 AIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239
|
250
....*....|
gi 1934240323 228 NLFVAGFIGS 237
Cdd:TIGR03005 240 EERTREFLSK 249
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-221 |
2.56e-39 |
|
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: 145.68 E-value: 2.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDN-KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDI 78
Cdd:COG4987 332 PSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYpHMTVYENMAFAlklrkvpKEEI-DKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIG 146
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 147 RAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTeAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEE 555
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-228 |
3.58e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 136.13 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 11 KIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS-----EGDLVIGGKRM--NDVEPKD--RDIAMV 81
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEvrREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKLRKV--PKEEIDKKVR----EAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK14267 91 FQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-252 |
4.17e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.07 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIG------GKRMNDVEPKDRDIAMVFQ--SYALYPH 90
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKPLRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 mTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQ-YLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKL 169
Cdd:PRK13634 102 -TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 170 RNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGfIGSPQMNFFDGELEK 249
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIG-LDLPETVKFKRALEE 259
|
...
gi 1934240323 250 KDG 252
Cdd:PRK13634 260 KFG 262
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-228 |
6.81e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.55 E-value: 6.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDI-----SEGDLVIGGKrmnDVEPKDRD- 77
Cdd:COG1117 12 IEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGE---DIYDPDVDv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 ------IAMVFQSYALYPhMTVYENMAFALKLRKV-PKEEIDKKV----REAA---EILDItqyLDRKPKALSGGQRQRV 143
Cdd:COG1117 88 velrrrVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVeeslRKAAlwdEVKDR---LKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 144 AIGRAIVRDPQVFLMDEPLSNLD----AKLrnqmraE--IIKLRQRIntTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDpistAKI------EelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
|
250
....*....|.
gi 1934240323 218 TPQEVFDQPAN 228
Cdd:COG1117 236 PTEQIFTNPKD 246
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-227 |
6.94e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 137.70 E-value: 6.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVE------PKDRDIAMVFQSYALYPHMTVYE 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 NMAFALKlrKVPKEEIDKKVreaaEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRA 175
Cdd:PRK11144 96 NLRYGMA--KSMVAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 176 EIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
2.90e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 133.72 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIG----------GKRMND 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 71 VEPKDRDIAMVFQSYALYPHMTVYEN-MAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAI 149
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-237 |
3.45e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 133.77 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIY-DNKVtaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGK-------RMNDVEP 73
Cdd:COG4598 7 PALEVRDLHKSFgDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdRDGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KDRD--------IAMVFQSYALYPHMTVYENMAFA-LKLRKVPKEEidkkVREAAEIL----DITQYLDRKPKALSGGQR 140
Cdd:COG4598 85 ADRRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAE----AIERAEALlakvGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 141 QRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNqmraEIIKLRQ------RintTFIYVTHDQTEAMTLGDRIVIMKDGFIQ 214
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVG----EVLKVMRdlaeegR---TMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
250 260
....*....|....*....|...
gi 1934240323 215 QIGTPQEVFDQPANLFVAGFIGS 237
Cdd:COG4598 234 EQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-211 |
4.41e-37 |
|
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: 132.02 E-value: 4.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMnDVEPKDRdIAMVFQ 83
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03269 158 GLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-226 |
9.77e-37 |
|
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: 137.89 E-value: 9.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDiSEGDLVIGGKRMNDVEPKD-----RDIAMVFQS-YA-LYP 89
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 90 HMTVYENMAFALKL--RKVPKEEIDKKVREA-AEI-LDiTQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:COG4172 378 RMTVGQIIAEGLRVhgPGLSAAERRARVAEAlEEVgLD-PAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 166 DAKLRNQMRAEIIKLRQRINTTFIYVTHDQT--EAMTlgDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:COG4172 457 DVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRALA--HRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-215 |
1.02e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.86 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDV------EPKDRDIAMVFQSYALYPHMTV 93
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQM 173
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1934240323 174 RAEIIKLRQRINTTFIYVTHDQTEAMTLgDRIVIMKDGFIQQ 215
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-222 |
1.66e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.63 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDnKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---DIAMV 81
Cdd:cd03224 2 EVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYEN--MAFALKLRKVPKEEIDkkvreaaEILDI----TQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:cd03224 81 PEGRRIFPELTVEENllLGAYARRRAKRKARLE-------RVYELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
3.88e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.92 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-RD--IAM 80
Cdd:COG1129 5 LEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKeeIDKK--VREAAEIL-----DITqyLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGL--IDWRamRRRARELLarlglDID--PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 154 QVFLMDEPLSNLDAK----LRNQMRaeiiKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGfiQQIGT 218
Cdd:COG1129 160 RVLILDEPTASLTEReverLFRIIR----RLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG--RLVGT 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
5.87e-36 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 135.70 E-value: 5.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY----DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDL-VIGGKR---MNDVEPKD 75
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 RD-----IAMVFQSYALYPHMTVYENMAFALKLrKVPKEEIDKKV-----------REAAEILDitqyldRKPKALSGGQ 139
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAvitlkmvgfdeEKAEEILD------KYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 140 RQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTP 219
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....*.
gi 1934240323 220 QEVFDQ 225
Cdd:TIGR03269 513 EEIVEE 518
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
1.52e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.49 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVT-AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK13648 88 VFQN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
1.64e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 128.88 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL-----EDISEGDLVIGGK---RMNDVE 72
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQdifKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 73 PKDRdIAMVFQSYALYPHMTVYENMAFALKLRKV--PKEEIDKKVREAAEIL----DITQYLDRKPKALSGGQRQRVAIG 146
Cdd:PRK14247 80 LRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 147 RAIVRDPQVFLMDEPLSNLDAKlrNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPE--NTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-273 |
2.25e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNdvePKDRD-IAmv 81
Cdd:COG4152 1 MLELKGLTKRFGDK-TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRrIG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 fqsY-----ALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:COG4152 75 ---YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGfiQQI--GTPQEVFDQ-PANLFVAG 233
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKG--RKVlsGSVDEIRRQfGRNTLRLE 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1934240323 234 FIGSPQM--NFFD-GELEKKDGKYQLKVGEatvvlGGKAQELL 273
Cdd:COG4152 229 ADGDAGWlrALPGvTVVEEDGDGAELKLED-----GADAQELL 266
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
2.45e-35 |
|
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: 128.12 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFALKlrkvpkEEIDKKVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRAI 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIyVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-233 |
2.68e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.15 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL---EDISEGDLVIGG-----KRMNDVEPK 74
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGitltaKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 75 drdIAMVFQSY-ALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:PRK13640 86 ---VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAmTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAG 233
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIG 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-227 |
3.45e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 128.65 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDN--------KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGK---RMN 69
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 70 DVEPKD--RDIAMVFQSY--ALYPHMTVYENMAFALK-LRKVPKEEIDKKVREAAEILDIT-QYLDRKPKALSGGQRQRV 143
Cdd:PRK10419 81 RAQRKAfrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 144 AIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFI--QQIGTPQE 221
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKL 240
|
....*.
gi 1934240323 222 VFDQPA 227
Cdd:PRK10419 241 TFSSPA 246
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
5.53e-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: 126.96 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIA 79
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHmTVYENMAFAlklRKVPKEEidkKVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRA 148
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTeamTL--GDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS---TIknADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-223 |
5.77e-35 |
|
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: 127.51 E-value: 5.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEG-DLVIGGKRMNDVEPKD--RDIAM 80
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VfqSYAL----YPHMTVyENM----AFA-LKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR 151
Cdd:COG1119 83 V--SPALqlrfPRDETV-LDVvlsgFFDsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-227 |
5.86e-35 |
|
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: 128.00 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDIAMVFQ-SY-ALYPH 90
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENMAFALK-LRKVPKEEIDKKVREAAEILDI-TQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK 168
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 169 LRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG-FIQQIGTPQEV-FDQPA 227
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEECDVAQLLsFKHPA 245
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-208 |
1.99e-34 |
|
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: 131.64 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHmTVYENMAFAlklRKVPKEEIDKKVREAAEILDITQYL--------DRKPKALSGGQRQRVAIGRAIVRD 152
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLA---RPDASDAEIREALERAGLDEFVAALpqgldtpiGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDqTEAMTLGDRIVIM 208
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-213 |
2.81e-34 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 125.01 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDN-KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFALKLRKvpkeeiDKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAI 149
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 150 VRDPQVFLMDEPLSNLDaklrnqMRAE---IIKLRQ-RINTTFIYVTHdQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03245 156 LNDPPILLLDEPTSAMD------MNSEerlKERLRQlLGDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
6.29e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.20 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYD----NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDV--EPKD-- 75
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVtkLPEYkr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -RDIAMVFQSYAL--YPHMTVYENMAFALK------LRK-VPKEEIDkKVREAAEILDI--TQYLDRKPKALSGGQRQRV 143
Cdd:COG1101 79 aKYIGRVFQDPMMgtAPSMTIEENLALAYRrgkrrgLRRgLTKKRRE-LFRELLATLGLglENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 144 AIGRAIVRDPQVFLMDEPLSNLDAKlrnqMRAEIIKLRQRI----NTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPK----TAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-229 |
2.26e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.27 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:COG4604 2 IEIKNVSKRYGGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFAL----KLRkvPKEEIDKKVREAAEILDIT----QYLDrkpkALSGGQRQRVAIGRAIVRDP 153
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRfpysKGR--LTAEDREIIDEAIAYLDLEdladRYLD----ELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPANL 229
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII-TPEVL 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-221 |
2.36e-33 |
|
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: 123.03 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK--VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIA 79
Cdd:cd03249 1 IEFKNVSFRYPSRpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPhMTVYENMAFALKlrkvpkEEIDKKVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRA 148
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKP------DATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTeamTL--GDRIVIMKDGFIQQIGTPQE 221
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS---TIrnADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-228 |
2.63e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.35 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 12 IYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS-----EGDLVIGGK-----RMNDVEPKdRDIAMV 81
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHniyspRTDTVDLR-KEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPhMTVYENMAFALKLRKVP-KEEIDKKVREA---AEILD-ITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSlkgASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRIntTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-226 |
1.09e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 123.66 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR-----DIAMVFQS--YALYPHM 91
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 92 TVYENMAFALKLR--KVPKEEIDKKVREA-AEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK 168
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 169 LRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
1.49e-32 |
|
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: 118.69 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD---RDIAM 80
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQsyalyphmtvyenmafalklrkvpkeeidkkvreaaeilditqyldrkpkaLSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGfiQQIGT 218
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-225 |
1.77e-32 |
|
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: 127.29 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:TIGR03375 464 IEFRNVSFAYpGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFAlklrkVPKEEiDKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAI 149
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALG-----APYAD-DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 150 VRDPQVFLMDEPLSNLDaklrnqMRAEiIKLRQRIN-----TTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMD------NRSE-ERFKDRLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQVLE 688
|
.
gi 1934240323 225 Q 225
Cdd:TIGR03375 689 A 689
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
3.96e-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: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYpHMTVYENMAFAlKLrKVPKEEidkkVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRAIV 150
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG-RP-DATDEE----VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQE 221
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
1.03e-31 |
|
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: 118.55 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDnKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---D 77
Cdd:COG0410 1 MPMLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENM---AFALKLRKVPKEEIDkkvreaaEILDI----TQYLDRKPKALSGGQRQRVAIGRAIV 150
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLllgAYARRDRAEVRADLE-------RVYELfprlKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-249 |
1.69e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.04 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGG---KRMNDVEPKDRDIAM 80
Cdd:PRK13633 10 VSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK13633 90 VFQN----PDnqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGfI 235
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIG-L 243
|
250
....*....|....
gi 1934240323 236 GSPQMNFFDGELEK 249
Cdd:PRK13633 244 DVPQVTELAYELKK 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-234 |
2.28e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.66 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 14 DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN--DVEPKDRDIAMVFQSY-ALYPH 90
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLR 170
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 171 NQMRAEIIKLRQRINTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGF 234
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-213 |
4.01e-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: 116.20 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNdvePKDR--DIAMVF 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERrkSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QS--YALYPHmTVYENMAFALKlrkvpkeEIDKKVREAAEIL---DITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:cd03226 78 QDvdYQLFTD-SVREELLLGLK-------ELDAGNEQAETVLkdlDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 158 MDEPLSNLDAKlrnQMR--AEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03226 150 FDEPTSGLDYK---NMErvGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-227 |
4.76e-31 |
|
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: 116.49 E-value: 4.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 8 NVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---DIAMVFQS 84
Cdd:cd03218 5 NLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 YALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSN 164
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 165 LDAKLRNQMRAEIIKLRQR-INttfIYVT-HDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-222 |
5.14e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.67 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKvTAVHDFNLEIADKEfIV-LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvepkdrDI- 78
Cdd:COG1137 1 MMTLEAENLVKSYGKR-TVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE----------DIt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 ------------------AMVFQsyalypHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQR 140
Cdd:COG1137 69 hlpmhkrarlgigylpqeASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 141 QRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQR-INttfIYVT-HDQTEamTLG--DRIVIMKDGFIQQI 216
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIG---VLITdHNVRE--TLGicDRAYIISEGKVLAE 217
|
....*.
gi 1934240323 217 GTPQEV 222
Cdd:COG1137 218 GTPEEI 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-213 |
2.19e-30 |
|
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: 113.80 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKVTA-----VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED--ISEGDLVIGGKRMNDVEP 73
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKsgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KDRdIAMVFQSYALYPHMTVYENMAFALKLRKvpkeeidkkvreaaeilditqyldrkpkaLSGGQRQRVAIGRAIVRDP 153
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHD-QTEAMTLGDRIVIMKDGFI 213
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-226 |
3.54e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 3.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDI---------------AMVFQSYALYPHMTVYE 95
Cdd:PRK10619 32 DVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrllrtrlTMVFQHFNLWSHMTVLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 NMAFA----LKLRKVPKEEIDKKVREAAEILDITQylDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLrn 171
Cdd:PRK10619 112 NVMEApiqvLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL-- 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 172 qmRAEIIKLRQRI---NTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK10619 188 --VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
3.77e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.13 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIsEGDLVIGGK----------RMNDVEP 73
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRveffnqniyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KDRDIAMVFQSYALYPhMTVYENMAFALKLRK-VPKEEIDKKVREA---AEILD-ITQYLDRKPKALSGGQRQRVAIGRA 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESAlkdADLWDeIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKD-----GFIQQIGTPQEVF 223
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
....*
gi 1934240323 224 DQPAN 228
Cdd:PRK14258 245 NSPHD 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-215 |
4.66e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.11 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGK---RMND---VEPKDRDIAMVFQSYALYPHMTVYENMAFALKLR 104
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEearAKLRAKHVGFVFQSFMLIPTLNALENVELPALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 105 KVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRI 184
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREH 196
|
170 180 190
....*....|....*....|....*....|.
gi 1934240323 185 NTTFIYVTHDQTEAMTLgDRIVIMKDGFIQQ 215
Cdd:PRK10584 197 GTTLILVTHDLQLAARC-DRRLRLVNGQLQE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-227 |
8.79e-30 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 118.63 E-value: 8.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 14 DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTT----LRMIAGLEDISEGDLVIGGKRMNDVEPKD------RDIAMVFQ 83
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 --SYALYPHMTVYENMAFALKL-RKVPKEEIDKKVREAAE---ILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:COG4172 100 epMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLErvgIPDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDqteamtLG------DRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD------LGvvrrfaDRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-225 |
2.71e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGkrmndvepkdR-----DIA 79
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------RvsallELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQsyalyPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMD 159
Cdd:COG1134 97 AGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 160 EPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-217 |
3.19e-29 |
|
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: 111.47 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGkrmndvepkdRDIAMVFQSYALYPHMTVYE 95
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGLGGGFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 NMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRA 175
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1934240323 176 EIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIG 217
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-228 |
4.17e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.57 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 12 IYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDI-----SEGDLVIGGKRMND--VEPKD--RDIAMVF 82
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYApdVDPVEvrRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QSYALYPHmTVYENMAFALKLR--KVPKEE-IDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMD 159
Cdd:PRK14243 98 QKPNPFPK-SIYDNIAYGARINgyKGDMDElVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 160 EPLSNLD--AKLRNQmraEIIK-LRQRIntTFIYVTHDQTEAMTLGDRIVIM---------KDGFIQQIGTPQEVFDQPA 227
Cdd:PRK14243 177 EPCSALDpiSTLRIE---ELMHeLKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQ 251
|
.
gi 1934240323 228 N 228
Cdd:PRK14243 252 Q 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-223 |
5.19e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 13 YDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQ------- 83
Cdd:PRK11231 12 YGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQhhltpeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 -------SYALYPHMTVYENMAfalklrkvpkEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:PRK11231 91 itvrelvAYGRSPWLSLWGRLS----------AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 157 LMDEPLSNLDakLRNQmrAEIIKLRQRINT---TFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK11231 161 LLDEPTTYLD--INHQ--VELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-228 |
8.33e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 110.54 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED----ISEGDLVIGGKRMNDVEPKDRDIAMVFQS--YALYP--- 89
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPlft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 90 ---HMTvyENMAFALKLRKVPKEEIDKKVrEAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:TIGR02770 81 mgnHAI--ETLRSLGKLSKQARALILEAL-EAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 167 AKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPAN 228
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-249 |
1.23e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGG------KRMNDVEPKDRDIAMVFQsyalYPHM- 91
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQKEIKPVRKKVGVVFQ----FPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 92 ----TVYENMAFALKLRKVPKEEIDKKVREAAEILDIT-QYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK13643 97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 167 AKlrnqMRAEIIKLRQRIN---TTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPANLFVAGFIGSPQMNFF 243
Cdd:PRK13643 177 PK----ARIEMMQLFESIHqsgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLKAHELGVPKATHF 251
|
....*.
gi 1934240323 244 DGELEK 249
Cdd:PRK13643 252 ADQLQK 257
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
1.63e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRmndVEPKD-RD----- 77
Cdd:COG3845 6 LELRGITKRFGG-VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP---VRIRSpRDaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFAL---KLRKVPKEEIDKKVREAAEilditQY-----LDRKPKALSGGQRQRVAIGRAI 149
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSE-----RYgldvdPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 150 VRDPQVFLMDEPLSNLD----AKLRNQMRaeiiKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:COG3845 157 YRGARILILDEPTAVLTpqeaDELFEILR----RLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-223 |
2.40e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.87 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKV----TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGG-------KRMNDVEPK 74
Cdd:PRK13645 9 LDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 75 DRDIAMVFQ--SYALYPHmTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQ-YLDRKPKALSGGQRQRVAIGRAIVR 151
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-225 |
4.53e-28 |
|
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: 114.04 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHmTVYENMAFAlKLRKVPKEEIdkkvREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRAI 149
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEI----ERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTeAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-235 |
5.77e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.37 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 12 IYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRM---NDVEPKD-----RDIAMVFQ 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDaiklrKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVP-KEEIDKKVREAAEIL----DITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 159 DEPLSNLDAKLRNQMRAEIIKLRQRIntTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFI 235
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-211 |
7.85e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.04 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-----RDI 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAaeiLDITQYLDRK---PKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA---LDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 156 FLMDEPLSNLDAKLRNqmraEIIKLRQ---RINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PRK10908 159 LLADEPTGNLDDALSE----GILRLFEefnRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-255 |
9.99e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.94 E-value: 9.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYD----NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL-----EDISEGDLVIGGK-----RMN 69
Cdd:PRK13631 22 LRVKNLYCVFDekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskyGTIQVGDIYIGDKknnheLIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 70 DVEPKD--------RDIAMVFQ--SYALYPHmTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQ-YLDRKPKALSGG 138
Cdd:PRK13631 102 NPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 139 QRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMrAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGT 218
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
250 260 270
....*....|....*....|....*....|....*..
gi 1934240323 219 PQEVFDQPANLFVAGFIGSPQMNFFDgELEKKDGKYQ 255
Cdd:PRK13631 260 PYEIFTDQHIINSTSIQVPRVIQVIN-DLIKKDPKYK 295
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-261 |
1.51e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMnDVEPKD-----RDIAMV 81
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSllevrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQS---YALYPhmTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:PRK13639 84 FQNpddQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 159 DEPLSNLDAklrnQMRAEIIKLRQRIN---TTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP-----ANLF 230
Cdd:PRK13639 162 DEPTSGLDP----MGASQIMKLLYDLNkegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIetirkANLR 237
|
250 260 270
....*....|....*....|....*....|....
gi 1934240323 231 VagfigsPQMNFFDGELEKKDG---KYQLKVGEA 261
Cdd:PRK13639 238 L------PRVAHLIEILNKEDNlpiKMGYTIGEA 265
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-211 |
1.94e-27 |
|
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: 106.97 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKiyDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED---ISEGDLVIGGKRMNDVEPKDRdIAM 80
Cdd:cd03234 9 VGLKAKNW--NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFA--LKLRKVPKEEIDKKVREAAEILD--ITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 157 LMDEPLSNLDAKLRNQMraeIIKLRQ--RINTTFIYVTHD-QTEAMTLGDRIVIMKDG 211
Cdd:cd03234 166 ILDEPTSGLDSFTALNL---VSTLSQlaRRNRIVILTIHQpRSDLFRLFDRILLLSSG 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-227 |
3.79e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.38 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVE--PKDRDI-AM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQS-YALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 160 EPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDqTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
4.92e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.20 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN--DVEPKDRDI 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQS---YALYPhmTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-208 |
7.22e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGkrmndvepkDRDIAMVFQSYAL---YPhMTVY 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 ENMAFALKLRKVPKEEIDKKVR----EAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLR 170
Cdd:NF040873 76 DLVAMGRWARRGLWRRLTRDDRaavdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1934240323 171 NQMRAeIIKLRQRINTTFIYVTHDQTEAMtLGDRIVIM 208
Cdd:NF040873 156 ERIIA-LLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-226 |
1.11e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.33 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN-----DVEPKDRDIAMVFQS-YA-LY 88
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDpYAsLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 89 PHMTVYENMAFALKLRKV-PKEEIDKKVREAAEILDIT-QYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 167 AKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-229 |
1.74e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALyphmtvye 95
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSL-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 nmAFALKLRKV----------PKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIV-------RDPQVFLM 158
Cdd:COG4559 87 --AFPFTVEEVvalgraphgsSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 159 DEPLSNLDakLRNQ---MRAeiikLRQ--RINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPANL 229
Cdd:COG4559 165 DEPTSALD--LAHQhavLRL----ARQlaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL-TDELL 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-226 |
1.90e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.59 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIYDNK---------VTAVHD--FNLEiADKEFIVlVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDVEPKD 75
Cdd:PRK11308 9 IDLKKHYPVKrglfkperlVKALDGvsFTLE-RGKTLAV-VGESGCGKSTLARLLTMIETPTGGELYYQGQ---DLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 --------RDIAMVFQS-YA-LYPHMTVYENMAFALKLR-KVPKEEIDKKVREAAEILDI-TQYLDRKPKALSGGQRQRV 143
Cdd:PRK11308 84 peaqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 144 AIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
...
gi 1934240323 224 DQP 226
Cdd:PRK11308 244 NNP 246
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-224 |
3.19e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 103.78 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 25 LEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNdvePKDRDIAMVFQSYAL---YP---HMTVYENMA 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQRHEFawdFPisvAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 99 FALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEII 178
Cdd:TIGR03771 78 GHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1934240323 179 KLRQRiNTTFIYVTHDQTEAMTLGDRIVIMkDGFIQQIGTPQEVFD 224
Cdd:TIGR03771 158 ELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQD 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
4.26e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMnDVEPKD-----RDI 78
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQS--YALYPhMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-214 |
6.75e-26 |
|
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: 103.18 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD-RDIAMVF-QSYALYPHMTVY 94
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 ENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMR 174
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1934240323 175 AEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQ 214
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-229 |
7.54e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 7.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALyphmtvye 95
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 nmAFALKLRKV----------PKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR------DPQVFLMD 159
Cdd:PRK13548 88 --SFPFTVEEVvamgraphglSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 160 EPLSNLDakLRNQ---MRAeiikLRQRI---NTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPANL 229
Cdd:PRK13548 166 EPTSALD--LAHQhhvLRL----ARQLAherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-TPETL 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-230 |
7.76e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 107.62 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 24 NLEIADKEFIVLVGPSGCGKSTTLRMIAGLedIS-EGDLVIGGKRMNDVEPKD--RDIAMVFQSYALyPHMTVYENMAFA 100
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 101 lklrkvpKEEI-DKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK 168
Cdd:PRK11174 447 -------NPDAsDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 169 LRNQ-MRAeIIKLRQRinTTFIYVTH--DQTEAMtlgDRIVIMKDGFIQQIGTPQEVFDQPaNLF 230
Cdd:PRK11174 520 SEQLvMQA-LNAASRR--QTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGDYAELSQAG-GLF 577
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-247 |
8.85e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 104.81 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 14 DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL---EDISEGDLVIGGKRMNDVEPKD------RDIAMVFQS 84
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 --YALYPHMTVYENMAFALKLRK--VPKEEIDKKVR--EAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMEVLMLHKgmSKAEAFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 159 DEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLFVAGFIGS- 237
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAv 265
|
250
....*....|
gi 1934240323 238 PQMNFFDGEL 247
Cdd:PRK09473 266 PRLDAEGESL 275
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.51e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD-IAM 80
Cdd:PRK13537 6 APIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDE 160
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 161 PLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-250 |
1.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKV----TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN------DVEP 73
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KDRDIAMVFQsyalYPHM-----TVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYL-DRKPKALSGGQRQRVAIGR 147
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 148 AIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPA 227
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF-QDV 236
|
250 260
....*....|....*....|...
gi 1934240323 228 NLFVAGFIGSPQMNFFDGELEKK 250
Cdd:PRK13649 237 DFLEEKQLGVPKITKFAQRLADR 259
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-197 |
2.29e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHmTVYENM 97
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 98 AFALKLRKvpkeeidKKVREAAEILDITQY------LDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRN 171
Cdd:PRK10247 102 IFPWQIRN-------QQPDPAIFLDDLERFalpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
gi 1934240323 172 QMRAEIIKLRQRINTTFIYVTHDQTE 197
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-235 |
2.29e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMafalklrKVPKEE-IDKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRA 148
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNI-------RVGRPDaTDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIyVTHDQT---EAmtlgDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKG-RTTFI-IAHRLStvrNA----DRILVFDNGRVVESGSFDELVAR 559
|
250
....*....|...
gi 1934240323 226 P---ANLFVAGFI 235
Cdd:PRK13657 560 GgrfAALLRAQGM 572
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
18-211 |
3.63e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.06 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---DIAMVFQSYALYPHMTVY 94
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 ENMAFALKLRKVPKEEIDKKVREAAEILdiTQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMR 174
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIG 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1934240323 175 AEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:TIGR03410 172 RVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-221 |
3.83e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.98 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRmndVEPKDRDIAM----VFQSYALYPHMTV 93
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDAGDIATRRrvgyMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQM 173
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1934240323 174 RAEIIKL-RQRINTTFIyVTHDQTEAMTLgDRIVIMKDGFIQQIGTPQE 221
Cdd:NF033858 437 WRLLIELsREDGVTIFI-STHFMNEAERC-DRISLMHAGRVLASDTPAA 483
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-225 |
9.18e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.44 E-value: 9.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGkrmNDVEPKDRDiamvfqsyALYPHM---- 91
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWDRE--------ELGRHIgylp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 92 --------TVYENMA-FAlklrkvpkEEIDKKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAIVR 151
Cdd:COG4618 413 qdvelfdgTIAENIArFG--------DADPEKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 152 DPQVFLMDEPLSNLD----AKLrnqMRAeIIKLRQRiNTTFIYVTHDQTeAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:COG4618 485 DPRLVVLDEPNSNLDdegeAAL---AAA-IRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-211 |
9.72e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 101.70 E-value: 9.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvEP-KDR-----DIAMVF-QSYALYP 89
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-----VPfKRRkefarRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 90 HMTVYENmaFAL--KLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDA 167
Cdd:COG4586 110 DLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1934240323 168 KLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-222 |
1.14e-24 |
|
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: 103.97 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHmTV 93
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAfalKLRKVPKEEidkKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAIVRDPQVFLMDEPL 162
Cdd:TIGR01842 409 AENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 163 SNLDAKLRNQMRAEIIKLRQRINTTfIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITV-VVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
1.37e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSyalyPH-----MTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:PRK13647 85 FQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
1.89e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK----VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEG-------------------- 59
Cdd:PRK13651 3 IKVKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 60 ---DLVIG---GKRMNDVEPKDRDIAMVFQ--SYALYpHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQ-YLDR 130
Cdd:PRK13651 83 vleKLVIQktrFKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 131 KPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAklrnQMRAEIIKLRQRINT---TFIYVTHDQTEAMTLGDRIVI 207
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLNKqgkTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*
gi 1934240323 208 MKDGFIQQIGTPQEV 222
Cdd:PRK13651 238 FKDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-225 |
2.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.24 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDN----KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMND------VE 72
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 73 PKDRDIAMVFQsyalYPHMTVYEN-----MAFALKLRKVPKEEI-DKKVREAAEILDITQYLDRKPKALSGGQRQRVAIG 146
Cdd:PRK13646 82 PVRKRIGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVkNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 147 RAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-230 |
2.44e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.25 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 10 KKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTT----LRMIAglediSEGDLVIGGKRMNDVEPKD-----RDIAM 80
Cdd:PRK15134 293 KRTVDHNV-VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQ--SYALYPHMTVYENMAFALKlrkVPKEEIDKKVREAAEILDITQY-LD-----RKPKALSGGQRQRVAIGRAIVRD 152
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLR---VHQPTLSAAQREQQVIAVMEEVgLDpetrhRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLF 230
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-226 |
2.75e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.48 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN--DVEPKDRDIAMVFQ--SYALYPHMT 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 VYENMAFALKLrkvpKEEIDKKVREAAEILDITQ------YLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK15112 106 ISQILDFPLRL----NTDLEPEQREKQIIETLRQvgllpdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 167 AKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-223 |
3.48e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.81 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDV---EPKDRD 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALKLRK-VPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 157 LMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIyVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLI-TDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
21-221 |
3.49e-24 |
|
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: 103.11 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 21 HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN--DVEPKDRDIAMVFQSYALYPHmTVYENMA 98
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFENIA 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 99 FALKLrkvPKEEIDKKVREAAEILDITQ-------YLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDaklrN 171
Cdd:TIGR03797 549 GGAPL---TLDEAWEAARMAGLAEDIRAmpmgmhtVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----N 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 172 QMRAEIIKLRQRINTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQE 221
Cdd:TIGR03797 622 RTQAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-257 |
5.47e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKVT----AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN------DVE 72
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 73 PKDRDIAMVFQsyalYPHM-----TVYENMAFALKLRKVPKEEIDKKVREAAEILDI-TQYLDRKPKALSGGQRQRVAIG 146
Cdd:PRK13641 82 KLRKKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 147 RAIVRDPQVFLMDEPLSNLDAKLRNQMrAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
250 260 270
....*....|....*....|....*....|.
gi 1934240323 227 aNLFVAGFIGSPQMNFFDGELEKkdGKYQLK 257
Cdd:PRK13641 237 -EWLKKHYLDEPATSRFASKLEK--GGFKFS 264
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-219 |
5.67e-24 |
|
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: 102.78 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYD-NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRM-NDVEPKDRDIAMV 81
Cdd:TIGR01257 929 VCVKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTP 219
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-213 |
5.88e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIY---DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDVEPKDRD- 77
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ---DVATLDADa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 --------IAMVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAI 149
Cdd:PRK10535 80 laqlrrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIyVTHDQTEAMTlGDRIVIMKDGFI 213
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-194 |
1.00e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIggkrmndvePKDRDIAMVFQSY 85
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFALK-LRKVPKE-------------------------------EIDKKVREAAEILDITQ-YLDRKP 132
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAeLRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEeDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 133 KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK----LRNQmraeiikLRQRiNTTFIYVTHD 194
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEF-------LKNY-PGTVLVVSHD 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-223 |
1.40e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.77 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 23 FNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN----DVEPKDRDIAMVFQSyalyPHMTVY---- 94
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIFytdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 -ENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQM 173
Cdd:PRK13638 96 dSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 174 RAEIIKLRQRINTTFIyVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK13638 176 IAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-211 |
1.58e-23 |
|
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: 94.98 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMV 81
Cdd:cd03246 2 EVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYPHmTVYENMafalklrkvpkeeidkkvreaaeilditqyldrkpkaLSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 162 LSNLDAKlRNQMRAEIIKLRQRINTTFIYVTHdQTEAMTLGDRIVIMKDG 211
Cdd:cd03246 124 NSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDG 171
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-226 |
1.89e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.14 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGK--------RMNDVEPKdrdIAMVFQSYALYPHMTV 93
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrsRLYTVRKR---MSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFALKLR-KVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:PRK11831 102 FDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 173 MRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-249 |
2.07e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.36 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNKVTaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDL-VIGGKRMNDVEPKDRDIA 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHMTVYENMA-----FALKLRKVpkEEIDKKVREAAEilditqyLDRKPKA----LSGGQRQRVAIGRAIV 150
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLvfgryFGMSTREI--EAVIPSLLEFAR-------LESKADArvsdLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQpanlf 230
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE----- 262
|
250
....*....|....*....
gi 1934240323 231 vagFIGSPQMNFFDGELEK 249
Cdd:PRK13536 263 ---HIGCQVIEIYGGDPHE 278
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-211 |
3.01e-23 |
|
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: 95.58 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVI--GGKRMNDVEPKDRDIAMVFQSYALY----- 88
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 89 ---PHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYL-DRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSN 164
Cdd:COG4778 103 rviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 165 LDAKLRNQMRAEIIKLRQRiNTTFIYVTHDqTEAM-TLGDRIVIMKDG 211
Cdd:COG4778 183 LDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-225 |
5.73e-23 |
|
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: 95.25 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK--DRDIAMVFQSYALYpHMTVYEN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 97 MAFAlklRKVPKEEidkKVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:cd03252 96 IALA---DPGMSME---RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 166 DAklrnQMRAEIIKLRQRI--NTTFIYVTHDQTEAMTlGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:cd03252 170 DY----ESEHAIMRNMHDIcaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
7.25e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.70 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR---DIAM 80
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFA-LKLRKVPKEEID--KKVREAAEIL----DITQYLDRKPKALSGGQRQRVAIGRAIVRDP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrHLTKKVCGVNIIdwREMRVRAAMMllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
9.26e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.73 E-value: 9.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIggkrmndvePKDRDIAMVFQ-SY--------AL-YP 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrPYlplgtlreALlYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 90 HMTvyenmafalklRKVPKEEIdKKVREAAEILDITQYLDRK---PKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:COG4178 450 ATA-----------EAFSDAEL-REALEAVGLGHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180
....*....|....*....|....*...
gi 1934240323 167 AKLRNQMRAeiiKLRQRI-NTTFIYVTH 193
Cdd:COG4178 518 EENEAALYQ---LLREELpGTTVISVGH 542
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-226 |
9.79e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 9.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmnDVEPKD-----RDIAMVFQSYAL---- 87
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD---DVEALSaraasRRVASVPQDTSLsfef 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 88 ----------YPHMTVYENMAfalklrkvpkEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFL 157
Cdd:PRK09536 93 dvrqvvemgrTPHRSRFDTWT----------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 158 MDEPLSNLDakLRNQMRAeiIKLRQRI---NTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK09536 163 LDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
1.22e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.06 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRM---NDVEPKDRD 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENM---AFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQ 154
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 155 VFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-226 |
1.62e-22 |
|
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: 98.09 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVePKDR---DIAMVFQSYALYpHMTVYEN 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 97 MAfaLKLRKVPKEEIDKKVREAAeILDItqyLDRKPKA-----------LSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:TIGR03796 573 LT--LWDPTIPDADLVRACKDAA-IHDV---ITSRPGGydaelaegganLSGGQRQRLEIARALVRNPSILILDEATSAL 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 166 DAklrnQMRAEIIK-LRQRiNTTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:TIGR03796 647 DP----ETEKIIDDnLRRR-GCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-211 |
1.79e-22 |
|
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: 92.92 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVT----AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvepkdrdIA 79
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSyALYPHMTVYENMAFALKLRkvpKEEIDKKVREAAEILDITQYLDR-------KPKALSGGQRQRVAIGRAIVRD 152
Cdd:cd03250 70 YVSQE-PWIQNGTIRENILFGKPFD---EERYEKVIKACALEPDLEILPDGdlteigeKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHdQTEAMTLGDRIVIMKDG 211
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-236 |
1.81e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.78 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLED-IS----EGDLVIGGKRM---NDVEPKDRDIAMVFQSYALYPhMTVYENMAFALKLRK- 105
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDkVSgyrySGDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 106 VPKEEI----DKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLR 181
Cdd:PRK14271 131 VPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 182 QRIntTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANL----FVAGFIG 236
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-245 |
2.10e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.62 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTT----LRMI--AGLEDISEGDL-------VIGGKRMNDVEPKD---RDIA 79
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqAGGLVQCDKMLlrrrsrqVIELSEQSAAQMRHvrgADMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQS--YALYPHMTVYENMAFALKLRK-VPKEEidkKVREAAEILDITQ------YLDRKPKALSGGQRQRVAIGRAIV 150
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIAESIRLHQgASREE---AMVEAKRMLDQVRipeaqtILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLF 230
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
250
....*....|....*.
gi 1934240323 231 VAGFIGS-PQMNFFDG 245
Cdd:PRK10261 265 TRALLAAvPQLGAMKG 280
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-226 |
3.36e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.52 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVepKDRDIA---MV--FQSYALYPHMTV 93
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIArmgVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFA-------------LKL---RKVPKEEIDKkvreAAEILD---ITQYLDRKPKALSGGQRQRVAIGRAIVRDPQ 154
Cdd:PRK11300 98 IENLLVAqhqqlktglfsglLKTpafRRAESEALDR----AATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 155 VFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-228 |
3.42e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 97.12 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK--DRDIAM 80
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHmTVYENMAFALKlrKVPKEEidkkVREAAEILDITQYLDRKPK-----------ALSGGQRQRVAIGRAI 149
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNP--GAPFEH----VIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 150 VRDPQVFLMDEPLSNLDAK----LRNQMRaEIIKLRqrintTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYEsealIMRNMR-EICRGR-----TVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEELLAL 681
|
...
gi 1934240323 226 PAN 228
Cdd:TIGR01846 682 QGL 684
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-213 |
3.54e-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: 91.61 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVT-AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD-IAMV 81
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYALYpHMTVYENMAfalklrkvpkeeidkkvreaaeilditqyldrkpKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTeAMTLGDRIVIMKDGFI 213
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKI 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-222 |
5.52e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHMTV 93
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMA--------FALKLRKVPKEEIDKKVREAAeildITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:PRK10253 99 QELVArgryphqpLFTRWRKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 166 DAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-226 |
9.64e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK--VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK--DRDIA 79
Cdd:TIGR00958 479 IEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHmTVYENMAFALklRKVPKEEIDKKVREAAE---ILDITQYLD----RKPKALSGGQRQRVAIGRAIVRD 152
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAANAhdfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 153 PQVFLMDEPLSNLDAklrnQMRAEIIKLRQRINTTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:TIGR00958 636 PRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
1.21e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 90.18 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD---IAMV---FQSYALYPHMT 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 VYENMAfalklrkvpkeeidkkvreaaeildITQYLdrkpkalSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:cd03215 95 VAENIA-------------------------LSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1934240323 173 MRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03215 143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
2.26e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNVKKIYdNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD---RD 77
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMA----FAlklrkvPKEEIDKKVREAAEILdiTQYLDRKPK---ALSGGQRQRVAIGRAIV 150
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAmggfFA------ERDQFQERIKWVYELF--PRLHERRIQragTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIyVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL-VEQNANQALKLADRGYVLENGHV 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
3.67e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDV-EPKDRD-I 78
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAALRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHmTVYENMAFALK----------LRKVPKEeidkKVREAAEILDitQYLDRKPKALSGGQRQRVAIGRA 148
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPnasdealievLQQVGLE----KLLEDDKGLN--AWLGEGGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHDQTeAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQE 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-225 |
3.78e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVT-AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFALKlRKVPKEEIDKKVReAAEILDITQYLDR--------KPKALSGGQRQRVAIGRAIVRD 152
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYART-EQYSREQIEEAAR-MAYAMDFINKMDNgldtvigeNGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQriNTTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
4.36e-21 |
|
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: 93.58 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIA 79
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYpHMTVYENMAFAlklrkvPKEEIDKKVREAAEILDITQYLDRKP-----------KALSGGQRQRVAIGRA 148
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRinTTFIYVTHD 194
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-224 |
4.92e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.46 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 15 NKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL---EDISEGDLVIGGKRMNDVEPKDRDI-------AMVFQS 84
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrksrantGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 YALYPHMTVYENMAFAlKLRKVP---------KEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK09984 95 FNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 156 FLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEvFD 224
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FD 241
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-225 |
5.14e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 93.65 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVepkDRDIAMVFQSY-ALYPHM---TVY 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsgSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 ENMAFALKlRKVPKEEIDKKVrEAAEI-LDITQY-------LDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAAC-EIAEIkDDIENMplgyqteLSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 167 AKLRNQMRAEIIKLRQRintTFIYVTHDQTEAmTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-213 |
6.38e-21 |
|
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: 89.45 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK--VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK--DRDIA 79
Cdd:cd03248 12 VKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHmTVYENMAFALKlrKVPKEEIdKKVREAAEILDITQYL--------DRKPKALSGGQRQRVAIGRAIVR 151
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQ--SCSFECV-KEAAQKAHAHSFISELasgydtevGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRinTTFIYVTHdQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-221 |
9.38e-21 |
|
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: 9.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIA 79
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYpHMTVYENMAFAlklR-KVPKEEidkkVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGR 147
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG---RpDASEEE----VEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 148 AIVRDPQVFLMDEPLSNLDaklrnqMRAEiiklrQRINTTFIYVTHDQTeamTL-----------GDRIVIMKDGFIQQI 216
Cdd:COG5265 508 TLLKNPPILIFDEATSALD------SRTE-----RAIQAALREVARGRT---TLviahrlstivdADEILVLEAGRIVER 573
|
....*
gi 1934240323 217 GTPQE 221
Cdd:COG5265 574 GTHAE 578
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-211 |
1.68e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndVE----PKDRDia 79
Cdd:COG0488 316 LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET----VKigyfDQHQE-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 mvfqsyALYPHMTVYENMAfalklrkvpkeeidkKVREAAEILDITQYLDR---------KP-KALSGGQRQRVAIGRAI 149
Cdd:COG0488 389 ------ELDPDKTVLDELR---------------DGAPGGTEQEVRGYLGRflfsgddafKPvGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 150 VRDPQVFLMDEPLSNLDAklrnQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDG 505
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-226 |
2.15e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.80 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED----ISEGDLVIGGKRMNDVEPKDR------DIAMVFQS--YA 86
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 87 LYPHMTVYENMAFALKLRkvpkEEIDKKVRE--AAEIL------DITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVH----QGGNKKTRRqrAIDLLnqvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 159 DEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
3.84e-20 |
|
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: 90.63 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDI--SEGDL-------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 62 ----VIGGK---------RMNDVEPKD--RDIAMVFQ-SYALYPHMTVYENMAFALklrkvpkEEI----DKKVREAAEI 121
Cdd:TIGR03269 80 epcpVCGGTlepeevdfwNLSDKLRRRirKRIAIMLQrTFALYGDDTVLDNVLEAL-------EEIgyegKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 122 LDITQYLDRK---PKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHdQTEA 198
Cdd:TIGR03269 153 IEMVQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEV 231
|
250 260
....*....|....*....|....*
gi 1934240323 199 MT-LGDRIVIMKDGFIQQIGTPQEV 222
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEV 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-229 |
5.88e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 23 FNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDiSEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHMTVYENMAFA 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 101 LKlRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR-------DPQVFLMDEPLSNLD----AKL 169
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDvaqqAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 170 RNQMRaeiiKLRQRINTTfIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPANL 229
Cdd:COG4138 173 DRLLR----ELCQQGITV-VMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-193 |
6.33e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 24 NLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRdIAMVFQSYALYPHMTVYENMAFALKL 103
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 104 RKVPKEEIDkkvrEAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKlRNQMRAEIIKLRQR 183
Cdd:PRK13539 101 LGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELIRAHLA 175
|
170
....*....|
gi 1934240323 184 INTTFIYVTH 193
Cdd:PRK13539 176 QGGIVIAATH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-222 |
1.09e-19 |
|
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: 90.07 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKVT-AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKR-MNDVEPKDRDIAMVFQ 83
Cdd:TIGR01257 1940 LNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:TIGR01257 2020 FDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 164 NLDAKLRNQMRAEIIKLrQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-221 |
1.58e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLediSEGDLVIGGKRMNDVEPKDRDI-----AMVFQSYALYPHMTVYENMAFALKLRK 105
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGMPIDAKEmraisAYVQQDDLFIPTLTVREHLMFQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 106 vpKEEIDKKVREAA--EILD----------ITQYLDRKpKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKlrnqM 173
Cdd:TIGR00955 129 --PRRVTKKEKRERvdEVLQalglrkcantRIGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF----M 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 174 RAEIIKLRQRI---NTTFIYVTHDQT-EAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:TIGR00955 202 AYSVVQVLKGLaqkGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-211 |
4.30e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEfIV-LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD---RDIAMV---FQSYALYPHM 91
Cdd:COG1129 267 VVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 92 TVYENMAFAL--KLRK---VPKEEIDKKVREAAEILDI-TQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL 165
Cdd:COG1129 346 SIRENITLASldRLSRgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 166 D--AKlrnqmrAEIIKLrqrIN------TTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:COG1129 426 DvgAK------AEIYRL---IRelaaegKAVIVISSELPELLGLSDRILVMREG 470
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-227 |
4.69e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 18 TAVHDFNLEIADKEFIVLVGPSGCGKSTT----LRMIAGLEDI-SEGDLVIGGKRM-NDVEPKDR-----DIAMVFQS-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGESLlHASEQTLRgvrgnKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 YALYPHMTVYENMAFALKLRKVPKeeidkkvREAA--EILD------ITQYLDR---KPKALSGGQRQRVAIGRAIVRDP 153
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMR-------REAArgEILNcldrvgIRQAAKRltdYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-207 |
9.68e-19 |
|
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: 84.00 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 13 YDNKVTAVHDFNLE-----IADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLvigGKRMNDVEPKDRDIAMVFQsyal 87
Cdd:cd03237 3 YPTMKKTLGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 88 yphMTVYenmafALKLRKVPKEEIDKKVR-EAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:cd03237 76 ---GTVR-----DLLSSITKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1934240323 167 AKLRnQMRAEIIK-LRQRINTTFIYVTHDQTEAMTLGDRIVI 207
Cdd:cd03237 148 VEQR-LMASKVIRrFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-213 |
1.28e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEP---KDRDIAMVFQSYALYPHMTVYENMAFALKLRKVPKEEI 111
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 112 DKKVREAAEILDitqyLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD----AKLRNQMRAeiiKLRQRINTT 187
Cdd:PRK15439 122 KQLLAALGCQLD----LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpaetERLFSRIRE---LLAQGVGIV 194
|
170 180
....*....|....*....|....*.
gi 1934240323 188 FIyvTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:PRK15439 195 FI--SHKLPEIRQLADRISVMRDGTI 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-177 |
2.96e-18 |
|
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: 81.25 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 25 LEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK-DRDIAMVFQSYALYPHMTVYENMAFalkL 103
Cdd:TIGR01189 21 FTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHF---W 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 104 RKVPKEEiDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD----AKLRNQMRAEI 177
Cdd:TIGR01189 98 AAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvALLAGLLRAHL 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-213 |
3.40e-18 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 81.15 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 1 MATVSLKNV---KKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS---EGDLVIGGKRMND-VEP 73
Cdd:cd03233 1 ASTLSWRNIsftTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 74 KDRDIAMVFQSYALYPHMTVYENMAFALKLRKvpkeeiDKKVReaaeilditqyldrkpkALSGGQRQRVAIGRAIVRDP 153
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRCKG------NEFVR-----------------GISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 154 QVFLMDEPLSNLDAKLRNQMrAEIIKLRQRI--NTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEI-LKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-219 |
4.30e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.04 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 21 HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED--ISEGDLVIGGKRMNDVEPKDR---DIAMVFQSYALYPHMTVYE 95
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 ---NMAFALKLRKVPKEEIDKKVREAAEILDITQ-YLDRKPKA-LSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD---- 166
Cdd:COG0396 97 flrTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidal 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 167 ---AKLRNQMRAEiiklrqriNTTFIYVTH-----DQTEAmtlgDRIVIMKDGFIQQIGTP 219
Cdd:COG0396 177 rivAEGVNKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGK 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-222 |
4.31e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK--DRDIAMVFQSYALYPHMTVYENMAF-------ALKLRK 105
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVAIgrypwhgALGRFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 106 VPKEEidkKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRIN 185
Cdd:PRK10575 122 AADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERG 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 1934240323 186 TTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:PRK10575 199 LTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-225 |
9.26e-18 |
|
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: 84.23 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvepkdrdIAMVFQSyALYPHMTVYENMAF 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 ALKLrkvpKEEIDKKVREAAEILDITQYL---DR-----KPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRN 171
Cdd:TIGR00957 722 GKAL----NEKYYQQVLEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 172 QMRAEIIKLRQRI-NTTFIYVTHDQTeAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:TIGR00957 798 HIFEHVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-209 |
1.49e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 2 ATVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRdIAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 82 FQSYAL---YP-------HMTVYENMAFalkLRKvPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVR 151
Cdd:PRK15056 84 PQSEEVdwsFPvlvedvvMMGRYGHMGW---LRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1934240323 152 DPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMK 209
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-211 |
1.67e-17 |
|
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: 79.68 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD------IAMVFQSYALYpH 90
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENMAFALKLRKvpkeEIDKKVREAAEI---LDITQYLDR-----KPKALSGGQRQRVAIGRAIVRDPQVFLMDEPL 162
Cdd:cd03290 93 ATVEENITFGSPFNK----QRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 163 SNLDAKLRNQ-MRAEIIKLRQRINTTFIYVTHdQTEAMTLGDRIVIMKDG 211
Cdd:cd03290 169 SALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-226 |
4.78e-17 |
|
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: 79.10 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLvigGKRMND---------VEPK 74
Cdd:TIGR02323 4 LQVSGLSKSYGGGK-GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSgaelelyqlSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 75 DRDIA-----MVFQSYALYPHMTVYENMAFALKLRKVPKEEIDKkVREAA----EILDITQ-YLDRKPKALSGGQRQRVA 144
Cdd:TIGR02323 80 RRRLMrtewgFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGN-IRATAqdwlEEVEIDPtRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 145 IGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLD 238
|
..
gi 1934240323 225 QP 226
Cdd:TIGR02323 239 DP 240
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-226 |
5.50e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.30 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 14 DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHm 91
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 92 TVYENMAfaLKLRKVPKEEIDKKVREAA---EILDITQYLD----RKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSN 164
Cdd:PRK10789 404 TVANNIA--LGRPDATQQEIEHVARLASvhdDILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 165 LDAKLRNQmraeIIK-LRQ-RINTTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQP 226
Cdd:PRK10789 482 VDGRTEHQ----ILHnLRQwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-219 |
8.56e-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: 77.92 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIY-DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTT----LRMIagleDISEGDLVIGGKRMNDVEPKD--R 76
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 77 DIAMVFQSYALYPHmTVYENMAfalklrkvPKEEI-DKKVREAAEILDITQYLDRKPKAL-----------SGGQRQRVA 144
Cdd:cd03244 79 RISIIPQDPVLFSG-TIRSNLD--------PFGEYsDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 145 IGRAIVRDPQVFLMDEPLSNLDAKLRNQMRaEIIKlRQRINTTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTP 219
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQ-KTIR-EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-223 |
1.03e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 57 SEGDLVIGGKRMNDVEPKD-RDIAMVFQSYALYPHMTVYENMAFAlklrkvpKEEIDKK-VREAAEILDITQYLDRKP-- 132
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATREdVKRACKFAAIDEFIESLPnk 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 133 ---------KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHdQTEAMTLGD 203
Cdd:PTZ00265 1348 ydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1426
|
170 180
....*....|....*....|....*
gi 1934240323 204 RIVIMKD-----GFIQQIGTPQEVF 223
Cdd:PTZ00265 1427 KIVVFNNpdrtgSFVQAHGTHEELL 1451
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-211 |
1.80e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.77 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN---DVEPKDRDIAMVFQSYALYPHMTV 93
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFALKLRKVPKEEIDKKVREAAEI---LDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLR 170
Cdd:PRK10982 91 MDNMWLGRYPTKGMFVDQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1934240323 171 NQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PRK10982 171 NHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-226 |
2.89e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.27 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKVtAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIggkRMNDVEPKD--------- 75
Cdd:PRK11701 8 SVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY---RMRDGQLRDlyalseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 76 -----RDIAMVFQSYALYPHMTV-----------------YENM-AFALK-LRKVpkeEIDkkvreAAEIlditqylDRK 131
Cdd:PRK11701 84 rrllrTEWGFVHQHPRDGLRMQVsaggnigerlmavgarhYGDIrATAGDwLERV---EID-----AARI-------DDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 132 PKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD----AKLRNQMRAeiikLRQRINTTFIYVTHDQTEAMTLGDRIVI 207
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250
....*....|....*....
gi 1934240323 208 MKDGFIQQIGTPQEVFDQP 226
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDP 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-222 |
3.30e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 14 DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVF------QSYAL 87
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 88 YPHMTVYENMAFaLKLRKVP--------KEEIDKKVREAAEILDI-TQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:COG3845 348 VPDMSVAENLIL-GRYRRPPfsrggfldRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 159 DEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-196 |
4.00e-16 |
|
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: 74.50 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIggkrmndvePKDRDIAMVFQSyalyPHMTvyenmaf 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 ALKLRkvpkeeidkkvreaaEILditqyldRKP--KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAei 177
Cdd:cd03223 77 LGTLR---------------EQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ-- 132
|
170
....*....|....*....
gi 1934240323 178 iKLRQRInTTFIYVTHDQT 196
Cdd:cd03223 133 -LLKELG-ITVISVGHRPS 149
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
7.02e-16 |
|
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: 73.25 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLviggkrmndvepkdrdiamvfq 83
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 syalyphmtvyenmafalklrkvpkeEIDKKVREAaeilditqYLDRkpkaLSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:cd03221 58 --------------------------TWGSTVKIG--------YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 164 NLDAKLRNQMRAEIIKLRQrintTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-175 |
7.19e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK-DRDIAMVFQSYALYPHMTVYENMAFALKLRKvpke 109
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFWHADHS---- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 110 eiDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD----AKLRNQMRA 175
Cdd:cd03231 103 --DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMAG 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-218 |
2.19e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS--EGDLVIGGKRMNDVEPKDRD---IAM 80
Cdd:PRK13549 8 MKNITKTFGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTEragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAFALKLRKVPKEEIDKKVREAAEIL-----DITQYLdrKPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:PRK13549 87 IHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqlklDINPAT--PVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 156 FLMDEPLSNLDAKlRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGfiQQIGT 218
Cdd:PRK13549 165 LILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGT 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-193 |
3.56e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.61 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNK--VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIG-GKRMNDVEPK--DRDI 78
Cdd:PTZ00265 383 IQFKNVRFHYDTRkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHmTVYENMAFALKLRK--------------VPKEEIDKK-------------------------VREAA 119
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLYSLKdlealsnyynedgnDSQENKNKRnscrakcagdlndmsnttdsnelieMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 120 EILDITQYLDRKPKAL-----------------------SGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAE 176
Cdd:PTZ00265 542 QTIKDSEVVDVSKKVLihdfvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*..
gi 1934240323 177 IIKLRQRINTTFIYVTH 193
Cdd:PTZ00265 622 INNLKGNENRITIIIAH 638
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
4.01e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNkVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL--EDISEGDLVIGG---KRMNDVEPKDRDI 78
Cdd:TIGR02633 2 LEMKGIVKTFGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGsplKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYALYPHMTVYENMAFALKL-RKVPKEEIDKKVREAAEILDITQyLDRKPKA-----LSGGQRQRVAIGRAIVRD 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEItLPGGRMAYNAMYLRAKNLLRELQ-LDADNVTrpvgdYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 153 PQVFLMDEPLSNLDAKlRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGfiQQIGT 218
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-168 |
5.95e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 21 HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNdvepKDRDiamVFQSYALY--------PHMT 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 93 VYENMAFALKLRKVPKEEidkKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK 168
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-221 |
6.51e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKV--TAVHDFNLEIADKEFIVLVGPSGCGKSTTLR-MIAGLEDISEGDLVIGGKrmndvepkdrdIAM 80
Cdd:PLN03130 615 ISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----------VAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFALKLRKvpkEEIDKKVREAA-----EIL---DITQYLDRKPKaLSGGQRQRVAIGRAIVRD 152
Cdd:PLN03130 684 VPQVSWIF-NATVRDNILFGSPFDP---ERYERAIDVTAlqhdlDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 153 PQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVThDQTEAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFDKCIKDELR-GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-248 |
7.58e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 73.17 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLviggkrmnDVEPKDRDIAMVFQSYALYPHMT--VYENMAFALKLRKV---PK- 108
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFRGSELQNYFTklLEGDVKVIVKPQYVdliPKa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 109 -----EEIDKKVREAA------EILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMrAEI 177
Cdd:cd03236 103 vkgkvGELLKKKDERGkldelvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA-ARL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 178 IKLRQRINTTFIYVTHDQTEAMTLGDRIVIMkdgfiqqIGTPQE--VFDQPA------NLFVAGFIGSPQMNFFDGELE 248
Cdd:cd03236 182 IRELAEDDNYVLVVEHDLAVLDYLSDYIHCL-------YGEPGAygVVTLPKsvregiNEFLDGYLPTENMRFREESIE 253
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-194 |
2.09e-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: 73.67 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLviggkrmnDVEPKDRDIAMVFQSYALYPHMT-VYENmafalKLR--------- 104
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG-----EIKvahkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 105 KVPK----------EEID--KKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:COG1245 171 LIPKvfkgtvrellEKVDerGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN 250
|
170 180
....*....|....*....|..
gi 1934240323 173 MrAEIIKLRQRINTTFIYVTHD 194
Cdd:COG1245 251 V-ARLIRELAEEGKYVLVVEHD 271
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-211 |
3.55e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLediSEGDLVIGGKRMNDVEPKD---RDIAMVFQSYALYPHMTVYENMAFALKLRkVP 107
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRETLVFCSLLR-LP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 108 KE-EIDKKVREAAEIL--------DITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEII 178
Cdd:PLN03211 171 KSlTKQEKILVAESVIselgltkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190
....*....|....*....|....*....|...
gi 1934240323 179 KLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:PLN03211 251 SLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-229 |
9.83e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 23 FNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDiSEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHMTVYENMAFA 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 101 LKlRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRV-------AIGRAIVRDPQVFLMDEPLSNLDAKLRNQM 173
Cdd:PRK03695 94 QP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 174 RAEIIKL-RQRIntTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFdQPANL 229
Cdd:PRK03695 173 DRLLSELcQQGI--AVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL-TPENL 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-184 |
1.00e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.42 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDIS--EGDLVIGGKRMNDVEPkdRDIAMVFQSYALYPHMTVYENMAFALKLRkvpkeeid 112
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREALRFSALLR-------- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 113 kkvreaaeilditqyldrkpkALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAklrnQMRAEIIKLRQRI 184
Cdd:cd03232 108 ---------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVRFLKKL 154
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-240 |
1.08e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLviggKRmndvEPKDRdIAMVFQ 83
Cdd:PRK09544 5 VSLENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KR----NGKLR-IGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SYALYPHM--TVYENMAFALKLRKVPKEEIDKKVREAaeilditQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEP 161
Cdd:PRK09544 75 KLYLDTTLplTVNRFLRLRPGTKKEDILPALKRVQAG-------HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 162 LSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMkDGFIQQIGTPQEVFDQPANLFVAGFIGSPQM 240
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPEFISMFGPRGAEQL 225
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-250 |
1.09e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 70.70 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGledISEGDLVIGGKRM--NDVE-----PKDR------DIAMVF 82
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---ITKDNWHVTADRFrwNGIDllklsPRERrkiigrEIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 Q--SYALYPHMTVYENMAFALklrkvPKEEI---------DKKvREAAEIL------DITQYLDRKPKALSGGQRQRVAI 145
Cdd:COG4170 96 QepSSCLDPSAKIGDQLIEAI-----PSWTFkgkwwqrfkWRK-KRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 146 GRAIVRDPQVFLMDEPLSNLDAKLRNQmraeIIKLRQRIN----TTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQE 221
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQ----IFRLLARLNqlqgTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
250 260 270
....*....|....*....|....*....|
gi 1934240323 222 VFDQPANLFVAGFIGS-PQmnfFDGELEKK 250
Cdd:COG4170 246 ILKSPHHPYTKALLRSmPD---FRQPLPHK 272
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-223 |
1.24e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVT--AVHDFNLEIADKEFIVLVGPSGCGKSTTLR-MIAGLEDISEGDLVIGGKrmndvepkdrdIAM 80
Cdd:PLN03232 615 ISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-----------VAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYpHMTVYENMAFALKLRKvpkeeidKKVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRAI 149
Cdd:PLN03232 684 VPQVSWIF-NATVRENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVThDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-210 |
1.39e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGledisegdlviggkRMNDVEPKDRDiamVFQSYALYPHMTVYENMAfal 101
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCV---DVPDNQFGREASLIDAIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 102 klrkvpkeeIDKKVREAAEILDITQYLD-----RKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAE 176
Cdd:COG2401 108 ---------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170 180 190
....*....|....*....|....*....|....
gi 1934240323 177 IIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKD 210
Cdd:COG2401 179 LQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-216 |
1.43e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 9 VKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD---RDIAMVFQSY 85
Cdd:PRK09700 268 VRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ---ALYPHMTVYENMAFALKLRK--------VPKEEIDKKVREAA-EILDIT-QYLDRKPKALSGGQRQRVAIGRAIVRD 152
Cdd:PRK09700 348 rdnGFFPNFSIAQNMAISRSLKDggykgamgLFHEVDEQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 153 PQVFLMDEPLSNLDAKlrnqMRAEIIKLRQRI---NTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQI 216
Cdd:PRK09700 428 PEVIIFDEPTRGIDVG----AKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-227 |
2.36e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGleDISE----------GDLVIGGK-----------RMNDVEPKDRDI 78
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEplaaidaprlaRLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 79 AMVFQSYAL-----YPHMtvyeNMAFALKLRkvpkeeiDKKVREAA-EILDITQYLDRKPKALSGGQRQRVAIGRAI--- 149
Cdd:PRK13547 95 AFAFSAREIvllgrYPHA----RRAGALTHR-------DGEIAWQAlALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 150 ------VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVF 223
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
....
gi 1934240323 224 dQPA 227
Cdd:PRK13547 244 -TPA 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-194 |
4.52e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNL-----EIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLviggkrmnDVEPKdrdIAMVFQSYALYPHMTVYEN 96
Cdd:PRK13409 352 DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK---ISYKPQYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 97 mafalkLRKVP--------KEEIDKKvreaaeiLDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK 168
Cdd:PRK13409 421 ------LRSITddlgssyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*...
gi 1934240323 169 LRnQMRAEIIK--LRQRINTTFIyVTHD 194
Cdd:PRK13409 488 QR-LAVAKAIRriAEEREATALV-VDHD 513
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-227 |
6.13e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTlrmIAGLEDI-------SEGDLVIGGKRMNDVEPKDRDIAMVFQS--YALYPH 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLT---CAAALGIlpagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVyenMAFALK-LRKVPKEEIDKKVREAAE---ILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK10418 96 HTM---HTHAREtCLALGKPADDATLTAALEavgLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 167 AKLrnQMRaeIIKLRQRINTT----FIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPA 227
Cdd:PRK10418 173 VVA--QAR--ILDLLESIVQKralgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-194 |
6.22e-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: 69.43 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNL-----EIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLviggkrmndvePKDRDIamvfqSY------ALYPh 90
Cdd:COG1245 353 GFSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKI-----SYkpqyisPDYD- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVYENmafalkLRKVPKEEIDKKVREAaEI---LDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDA 167
Cdd:COG1245 416 GTVEEF------LRSANTDDFGSSYYKT-EIikpLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180
....*....|....*....|....*....
gi 1934240323 168 KLRNQMrAEIIK--LRQRINTTFIyVTHD 194
Cdd:COG1245 489 EQRLAV-AKAIRrfAENRGKTAMV-VDHD 515
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-225 |
8.85e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPK--DRDIAM 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHmTVYENMAFAlklRKVPKEeidkKVREAAEILDITQYLDRKPKA-----------LSGGQRQRVAIGRAI 149
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG---RDISEE----QVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRinTTFIYVTHdQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-222 |
1.12e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLEDIS----EGDLVIGGKRMNDVEPKDR-DIAMVFQSYALYPHMTVYENMAFALKLRK 105
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAARCKT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 106 -------VPKEEIDKKVRE-AAEILDITQYLDRKP-----KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAklrnQ 172
Cdd:TIGR00956 168 pqnrpdgVSREEYAKHIADvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS----A 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 173 MRAEIIKLRQRI-----NTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:TIGR00956 244 TALEFIRALKTSanildTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKA 298
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-211 |
1.22e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLED---ISEGDLVIGGKRMNdvEPKDRDIAMVFQSYALYPHMTVYENMAFALKLR---KVPK 108
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSK 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 109 EEIDKKVREAAEILDITQYLDrkpkALSG--------GQRQRVAIGRAIVRDPQVFL-MDEPLSNLDAklrnQMRAEIIK 179
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYAD----AVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS----QTAWSICK 943
|
170 180 190
....*....|....*....|....*....|....*.
gi 1934240323 180 L-RQRINT-TFIYVTHDQTEAMTLG--DRIVIMKDG 211
Cdd:TIGR00956 944 LmRKLADHgQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-194 |
2.33e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGgkrmndvepKDRDIAMVFQS 84
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------PGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 YALYPHMTVYENMAFAL-KLRKV-------------PKEEIDKKVREAAEILDITQY-----LDRK----------P--- 132
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVaEIKDAldrfneisakyaePDADFDKLAAEQAELQEIIDAadawdLDSQleiamdalrcPpwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 133 ---KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAK----LRNQMraeiiklrQRINTTFIYVTHD 194
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHL--------QEYPGTVVAVTHD 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-166 |
2.50e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.26 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 31 EFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEpKDRDIAMVFQSYALYPHMTVYENMAFALKL-----RK 105
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLENLHFLCGLhgrraKQ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934240323 106 VPKEeidkkvreAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK13543 117 MPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-225 |
2.70e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDnKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDL-VIGGKrMNDvePKDRD----- 77
Cdd:NF033858 2 ARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD-MAD--ARHRRavcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYA--LYPHMTVYENMAFALKLRKVPKEEidkkvREA--AEILDIT---QYLDRKPKALSGGQRQRVAIGRAIV 150
Cdd:NF033858 78 IAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAE-----RRRriDELLRATglaPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLR-QRINTTFIYVTHDQTEAMTLgDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRaERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-214 |
3.03e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLViggkrmndvepKDRDIAMVFQSyALYPHMTVYENMAF 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 ALKLRKvpkEEIDKKVREAAEILDITQY-------LDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQ 172
Cdd:PTZ00243 744 FDEEDA---ARLADAVRVSQLEADLAQLgggleteIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1934240323 173 MRAEIIKLRQRiNTTFIYVTHdQTEAMTLGDRIVIMKDGFIQ 214
Cdd:PTZ00243 821 VVEECFLGALA-GKTRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-246 |
4.76e-12 |
|
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: 65.26 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvepkdrdIAMVFQSYALYPHmTVYENMAFAL 101
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 102 KLrkvpKEEIDKKVREAAEIL-DITQYLDRKPKA-------LSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQM 173
Cdd:cd03291 123 SY----DEYRYKSVVKACQLEeDITKFPEKDNTVlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 174 -RAEIIKLRQriNTTFIYVThDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANlFVAGFIGSPQMNFFDGE 246
Cdd:cd03291 199 fESCVCKLMA--NKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLMGYDTFDQFSAE 268
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-219 |
1.50e-11 |
|
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: 62.81 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHmTVYEN 96
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 97 MafalklrKVPKEEIDKKVREAaeiLDITQYLDRkpkaLSGGQRQRVAIGRAIVRDPQVFLMDEPLSNL----DAKLRNQ 172
Cdd:cd03369 102 L-------DPFDEYSDEEIYGA---LRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQKT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 173 MRAE-----IIKLRQRINTTFIYvthdqteamtlgDRIVIMKDGFIQQIGTP 219
Cdd:cd03369 168 IREEftnstILTIAHRLRTIIDY------------DKILVMDAGEVKEYDHP 207
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-292 |
1.54e-11 |
|
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: 58.75 E-value: 1.54e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 236 GSPQMNFFDGELEKKDgkYQLKVGEATVVLGGKAQELLTGKgvGERKVTVGIRPEHI 292
Cdd:pfam17912 1 GSPPMNFLPATVVEDG--LLVLGGGVTLPLPEGQVLALKLY--VGKEVILGIRPEHI 53
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-222 |
1.93e-11 |
|
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: 62.16 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED--ISEGDLVIGGKRMNDVEPKDR---DIAMVFQSYALYPHMTVy 94
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIPGVKN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 enmafalklrkvpkeeidkkvreaaeiLDITQYLDrkpKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD-------A 167
Cdd:cd03217 95 ---------------------------ADFLRYVN---EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalrlvA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 168 KLRNQMRAEiiklrqriNTTFIYVTH-----DQTEAmtlgDRIVIMKDGFIQQIGTPQEV 222
Cdd:cd03217 145 EVINKLREE--------GKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKELA 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-175 |
3.13e-11 |
|
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: 64.19 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIYDNKVTaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGgkrmndvepKDRDIAMVFQSY- 85
Cdd:TIGR03719 326 ENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVKLAYVDQSRd 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 86 ALYPHMTVYENMAFALKLRKVPKEEIDKKvreaaeilditQYLDR----------KPKALSGGQRQRVAIGRAIVRDPQV 155
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIKLGKREIPSR-----------AYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180
....*....|....*....|
gi 1934240323 156 FLMDEPLSNLDAklrNQMRA 175
Cdd:TIGR03719 465 LLLDEPTNDLDV---ETLRA 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
35-166 |
3.16e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMN-DVEPKDRDIAMVFQSYALYPHMTVYENMAFALKLRKVpKEEIDK 113
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPG-AVGITE 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1934240323 114 KVReaaeILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK13540 111 LCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-207 |
4.98e-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: 60.66 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 26 EIADKEFIVLVGPSGCGKSTTLRMIAGLEdisegdlviggkrmndvEPKDRDIAMVFQSYALYPhmtvyenmafalklrk 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------------IPNGDNDEWDGITPVYKP---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 106 vpkeeidkkvreaaeilditQYLDrkpkaLSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRIN 185
Cdd:cd03222 68 --------------------QYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 1934240323 186 TTFIYVTHDQTEAMTLGDRIVI 207
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-171 |
5.51e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.04 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVtaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNdvepkdrDIAMVFQ 83
Cdd:PRK13541 2 LSLHQLQFNIEQKN--LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-------NIAKPYC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SY-----ALYPHMTVYENMAFALKLRKVPkeeidKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:PRK13541 73 TYighnlGLKLEMTVFENLKFWSEIYNSA-----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170
....*....|...
gi 1934240323 159 DEPLSNLDAKLRN 171
Cdd:PRK13541 148 DEVETNLSKENRD 160
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-218 |
5.76e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVK-KIYDNKVtaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLE--DISEGDLVIGGKRMNDVEPKDRDIAMVF 82
Cdd:CHL00131 10 IKNLHaSVNENEI--LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 QSYAlYP-HMTVYENM-----AFALKLRKVPKEEID-----KKVREAAEILDITQ-YLDRK-PKALSGGQRQRVAIGRAI 149
Cdd:CHL00131 88 LAFQ-YPiEIPGVSNAdflrlAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 150 VRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRqRINTTFIYVTHDQteamTLGDRIV-----IMKDGFIQQIGT 218
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLM-TSENSIILITHYQ----RLLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-213 |
7.10e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 21 HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIA-MVF-----QSYALYPHMTVY 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 ENMAFALKLRKVPKEEI--DKKVREAAEI----LDI-TQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDA 167
Cdd:PRK11288 350 DNINISARRHHLRAGCLinNRWEAENADRfirsLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1934240323 168 KLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:PRK11288 430 GAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-216 |
7.59e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 3 TVSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAM 80
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQSYALYPHMTVYENMAfalklrkVPKEEIDK---------KVR-EAAEILDITqyldrkpkaLSGGQRQRVAIGRAIV 150
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKP-------ANPALVEKwlerlkmahKLElEDGRISNLK---------LSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 151 RDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQtEAMTLGDRIVIMKDGFIQQI 216
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSEL 530
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-166 |
8.62e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 25 LEIADKEFIVLVGPSGCGKSTTLRMIAG---LED---ISEGDLVIGgkRMNDVEPKDRDiamvfqsyalyphMTVYENMA 98
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriIYEQDLIVA--RLQQDPPRNVE-------------GTVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 99 FALK------------LRKVPKEEIDKKVREAA---EILD----------ITQYL-------DRKPKALSGGQRQRVAIG 146
Cdd:PRK11147 89 EGIEeqaeylkryhdiSHLVETDPSEKNLNELAklqEQLDhhnlwqlenrINEVLaqlgldpDAALSSLSGGWLRKAALG 168
|
170 180
....*....|....*....|
gi 1934240323 147 RAIVRDPQVFLMDEPLSNLD 166
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLD 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-208 |
9.78e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAG--------LEDISEGDLVIggKRmndvepkdrdiamvFQSYALYPHMT-VYEN-MAFALK-- 102
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVL--KR--------------FRGTELQNYFKkLYNGeIKVVHKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 103 ----LRKVPK-------EEIDK--KVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKL 169
Cdd:PRK13409 168 yvdlIPKVFKgkvrellKKVDErgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190
....*....|....*....|....*....|....*....
gi 1934240323 170 RNQMrAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIM 208
Cdd:PRK13409 248 RLNV-ARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-213 |
9.83e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR-DIAMVFQSY-----ALYPHMTV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 94 YENMAFAlKLRKVPKEEIdkKVREAAEILDITQYLD----RKPKA------LSGGQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:PRK10762 348 KENMSLT-ALRYFSRAGG--SLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 164 NLD--AK-----LRNQMRAEiiklrqriNTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:PRK10762 425 GVDvgAKkeiyqLINQFKAE--------GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-226 |
1.06e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 14 DNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGledISEGDLVIGGKRM--NDVE-----PKDR------DIAM 80
Cdd:PRK15093 17 DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMrfDDIDllrlsPRERrklvghNVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 81 VFQ--SYALYPHmtvyENMAFALkLRKVPK--------EEIDKKVREAAEILDITQYLDRK------PKALSGGQRQRVA 144
Cdd:PRK15093 94 IFQepQSCLDPS----ERVGRQL-MQNIPGwtykgrwwQRFGWRKRRAIELLHRVGIKDHKdamrsfPYELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 145 IGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFD 224
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
..
gi 1934240323 225 QP 226
Cdd:PRK15093 249 TP 250
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-211 |
2.87e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLED--ISEGDLVIGGKrmndvePKDRDIAMVFQSYALY-----PHMTVYENMAFALKLR--- 104
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGF------PKKQETFARISGYCEQndihsPQVTVRESLIYSAFLRlpk 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 105 KVPKEEIDKKVREAAEILDITQYLDR-----KPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAklrnqmRAEIIK 179
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA------RAAAIV 1058
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1934240323 180 LRQRINT-----TFIYVTH----DQTEAMtlgDRIVIMKDG 211
Cdd:PLN03140 1059 MRTVRNTvdtgrTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-222 |
5.16e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvepkdrdIAMVFQSYALYPHmTVYE 95
Cdd:TIGR01271 438 VTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 96 NMAFALKLrkvpKEEIDKKVREAAEILDITQYLDRKPK--------ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDA 167
Cdd:TIGR01271 506 NIIFGLSY----DEYRYTSVIKACQLEEDIALFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 168 KLRNQM-RAEIIKLrqRINTTFIYVThDQTEAMTLGDRIVIMKDGFIQQIGTPQEV 222
Cdd:TIGR01271 582 VTEKEIfESCLCKL--MSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-225 |
1.19e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLviggkrmndvePKDRDIAMVFQSYALYPHMTVYENMA 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 99 FALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEII 178
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1934240323 179 KLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:PRK13546 188 EFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-198 |
2.35e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGleDISEG---DLVIGGKRMNDVEP----KdR 76
Cdd:PRK10938 261 IVLNNGVVSYNDRPI-LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRRRGSGETiwdiK-K 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 77 DIAMV----------------------FQSYALYphmtvyenmafalklRKVPkEEIDKKVREAAEILDITQYLDRKP-K 133
Cdd:PRK10938 337 HIGYVssslhldyrvstsvrnvilsgfFDSIGIY---------------QAVS-DRQQKLAQQWLDILGIDKRTADAPfH 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 134 ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIYVTHDQTEA 198
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-213 |
2.92e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDR-DIAMVF-----QSYALYPHMT--- 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPlaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 -----VYENMAFALKlrkvPKEE--IDKKVREAaeiLDIT-QYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSN 164
Cdd:PRK15439 361 nvcalTHNRRGFWIK----PAREnaVLERYRRA---LNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 165 LDAKLRNqmraEIIKLRQRI---NTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:PRK15439 434 VDVSARN----DIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-282 |
5.06e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 19 AVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKrmndvepkdrdIAMVFQSYALYPHMTVYENMA 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 99 FALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEII 178
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 179 KLRQRINTTFiYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQpANLFVAGFigsPQMNFFDGELEKKDGKYQLKV 258
Cdd:PRK13545 188 EFKEQGKTIF-FISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-YDEFLKKY---NQMSVEERKDFREEQISQFQH 262
|
250 260
....*....|....*....|....
gi 1934240323 259 GeatvVLGGKAQELLTGKGVGERK 282
Cdd:PRK13545 263 G----LLQEDQTGRERKRKKGKKT 282
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-166 |
5.61e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 6 LKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLR-MIAGLEDISeGDLVIGGKrmndvepkdRDIAMvFQS 84
Cdd:PRK11147 322 MENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTK---------LEVAY-FDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 85 Y--ALYPHMTVYENMAFAlklrkvpKEEIDKKVREAaeilDITQYLD---------RKP-KALSGGQRQRVAIGRAIVRD 152
Cdd:PRK11147 390 HraELDPEKTVMDNLAEG-------KQEVMVNGRPR----HVLGYLQdflfhpkraMTPvKALSGGERNRLLLARLFLKP 458
|
170
....*....|....
gi 1934240323 153 PQVFLMDEPLSNLD 166
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-230 |
6.91e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 20 VHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHMTVYENM 97
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 98 AFAlklrkvpkEEIDKKVREAAEILDITQYLDRKPKAL-----------SGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PLN03232 1332 PFS--------EHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 167 AKLRNQMRAEIiklRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANLF 230
Cdd:PLN03232 1404 VRTDSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-167 |
7.35e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 5 SLKNVKKIYDNKVTAVHDFNLEiadkeF-----IVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGgkrmndvepKDRDIA 79
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLS-----FfpgakIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA---------PGIKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSYALYPHMTVYEN-------------------MAFALklrkvPKEEIDKKVREAAEILDITQYLD----------- 129
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENveegvaevkaaldrfneiyAAYAE-----PDADFDALAAEQGELQEIIDAADawdldsqleia 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1934240323 130 ----RKP------KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDA 167
Cdd:PRK11819 149 mdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-193 |
1.10e-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: 56.30 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIggkrmndvePKDRDIAMVFQ 83
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 84 SyalyPHMT--------VYENMAFALKLRKVPkeeiDKKVREAAEILDITQYLDRK---------PKALSGGQRQRVAIG 146
Cdd:TIGR00954 523 R----PYMTlgtlrdqiIYPDSSEDMKRRGLS----DKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMA 594
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1934240323 147 RAIVRDPQVFLMDEPLSNLDAklrnQMRAEIIKLRQRINTTFIYVTH 193
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-213 |
1.18e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 35 LVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRD---IAMVFQSYALYPHMTVYENM--------AFALKL 103
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLIPQLTIAENIflgrefvnRFGRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 104 RKVPKEEIDKKVREaaeiLDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQR 183
Cdd:PRK10762 115 WKKMYAEADKLLAR----LNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ 190
|
170 180 190
....*....|....*....|....*....|.
gi 1934240323 184 iNTTFIYVTHDQTEAMTLGDRIVIMKDG-FI 213
Cdd:PRK10762 191 -GRGIVYISHRLKEIFEICDDVTVFRDGqFI 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-219 |
1.49e-08 |
|
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: 53.15 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 30 KEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIggkrmndvepkdrdIAMVfqsyalyphmtvyenmafalklrkvpke 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDGE---------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 110 eidkKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEI-----IKLRQRI 184
Cdd:smart00382 40 ----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|....*
gi 1934240323 185 NTTFIYVTHDQTeamTLGDRIVIMKDGFIQQIGTP 219
Cdd:smart00382 116 NLTVILTTNDEK---DLGPALLRRRFDRRIVLLLI 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
57-214 |
3.24e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 57 SEGDLVIGGKRMNDVEPKD---RDIAMVFQS---YALYPHMTVYENMAFALKLRKVPKEEIDkkvrEAAEILDITQYLDR 130
Cdd:PRK13549 316 WEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITLAALDRFTGGSRID----DAAELKTILESIQR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 131 -KPKA---------LSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD--AKlrnqmrAEIIKLrqrIN------TTFIYVT 192
Cdd:PRK13549 392 lKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAK------YEIYKL---INqlvqqgVAIIVIS 462
|
170 180
....*....|....*....|..
gi 1934240323 193 HDQTEAMTLGDRIVIMKDGFIQ 214
Cdd:PRK13549 463 SELPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-213 |
3.58e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS---EGDLVIGGKRMNDVEPKdRDIAMVFQSYALYPHMT 92
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPR-KTSAYISQNDVHVGVMT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 93 VYENMAFALKLRKV--------------------PKEEIDKKVR----EAAEILDITQYL---------------DRKPK 133
Cdd:PLN03140 256 VKETLDFSARCQGVgtrydllselarrekdagifPEAEVDLFMKatamEGVKSSLITDYTlkilgldickdtivgDEMIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 134 ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQmraeIIKLRQRI-----NTTFIYVTHDQTEAMTLGDRIVIM 208
Cdd:PLN03140 336 GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQ----IVKCLQQIvhlteATVLMSLLQPAPETFDLFDDIILL 411
|
....*
gi 1934240323 209 KDGFI 213
Cdd:PLN03140 412 SEGQI 416
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-166 |
6.84e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 7 KNVKKIYDNKVTavhdfnleIADKEF------IV-LVGPSGCGKSTTLRMIAGLEDISEGDLVIGgkrmNDVEpkdrdIA 79
Cdd:PRK11819 328 ENLSKSFGDRLL--------IDDLSFslppggIVgIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----ETVK-----LA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 MVFQSY-ALYPHMTVYENMAFALKLRKVPKEEIDKKvreaaeilditQYLDR----------KPKALSGGQRQRVAIGRA 148
Cdd:PRK11819 391 YVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSR-----------AYVGRfnfkggdqqkKVGVLSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 1934240323 149 IVRDPQVFLMDEPLSNLD 166
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-214 |
7.03e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 16 KVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGL-EDISEGDLVIGGKRMNDVEPKD---RDIAMVFQS---YALY 88
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 89 PHMTVYENMAFALKLRKVPKEEIDkkvrEAAEILDITQYLDR-KPKA---------LSGGQRQRVAIGRAIVRDPQVFLM 158
Cdd:TIGR02633 352 PILGVGKNITLSVLKSFCFKMRID----AAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 159 DEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFIQ 214
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-195 |
9.65e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVK-KIYDNKVtaVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLED--ISEGDLVIGGKRMNDVEPKDR---D 77
Cdd:PRK09580 2 LSIKDLHvSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 IAMVFQSYALYPHMTVYENMAFALK-LRKV-PKEEIDK-----KVREAAEILDITQYLDRKP--KALSGGQRQRVAIGRA 148
Cdd:PRK09580 80 IFMAFQYPVEIPGVSNQFFLQTALNaVRSYrGQEPLDRfdfqdLMEEKIALLKMPEDLLTRSvnVGFSGGEKKRNDILQM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1934240323 149 IVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQ 195
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQ 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-225 |
1.12e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 22 DFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYphmtvyenmAF 99
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF---------SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 ALKLRKVP-KEEIDKKVREAAEILDITQYLDRKP-----------KALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDA 167
Cdd:TIGR00957 1375 SLRMNLDPfSQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 168 KLRNQMRAEIiklRQRINT-TFIYVTHDQTEAMTLgDRIVIMKDGFIQQIGTPQEVFDQ 225
Cdd:TIGR00957 1455 ETDNLIQSTI---RTQFEDcTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-218 |
1.33e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKvTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDL------VIGgkrmndVEPKDrd 77
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIG------YYAQD-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 78 iamvfQSYALYPHMTVYENMAfalKLRKvPKEEiDKKVREAAEILDITQ-YLDRKPKALSGGQRQRVAIGRAIVRDPQVF 156
Cdd:PRK15064 391 -----HAYDFENDLTLFDWMS---QWRQ-EGDD-EQAVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 157 LMDEPlsnldaklRNQMRAEIIklrQRINT-------TFIYVTHDQTEAMTLGDRIV-IMKDGFIQQIGT 218
Cdd:PRK15064 461 VMDEP--------TNHMDMESI---ESLNMalekyegTLIFVSHDREFVSSLATRIIeITPDGVVDFSGT 519
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-220 |
1.95e-07 |
|
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: 52.49 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 23 FNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRmndVEPKDRD-----IAMVFQSYALYPHMTVYENM 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDRLLGLDGE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 98 AFALKLRKVPKE-EIDKKVR-EAAEILDItqyldrkpkALSGGQRQRVAIGRAIVRDPQVFLMDE------Plsnldakl 169
Cdd:COG4615 428 ADPARARELLERlELDHKVSvEDGRFSTT---------DLSQGQRKRLALLVALLEDRPILVFDEwaadqdP-------- 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1934240323 170 rnQMRA----EII-KLRQRiNTTFIYVTHDQTeAMTLGDRIVIMKDGFIQQIGTPQ 220
Cdd:COG4615 491 --EFRRvfytELLpELKAR-GKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGPA 542
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-230 |
2.55e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 27 IADKEFIVLVGPSGCGKSTTL----RMIagleDISEGDLVIGGKRMNDVEPKD--RDIAMVFQSYALYPHmTVYENM-AF 99
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVdPF 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 100 ----------ALKL----RKVPKEE--IDKKVREAAeildiTQYldrkpkalSGGQRQRVAIGRAIV-RDPQVFLMDEPL 162
Cdd:PTZ00243 1408 leassaevwaALELvglrERVASESegIDSRVLEGG-----SNY--------SVGQRQLMCMARALLkKGSGFILMDEAT 1474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934240323 163 SNLDAKLRNQMRAEI---------IKLRQRINTTFIYvthdqteamtlgDRIVIMKDGFIQQIGTPQEVFDQPANLF 230
Cdd:PTZ00243 1475 ANIDPALDRQIQATVmsafsaytvITIAHRLHTVAQY------------DKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
95-218 |
4.53e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 95 ENMAFALKLRKVPKEEIDKKVREAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMR 174
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 175 AEIIKLrQRINTTFIYVTHDQTEA------MTLGDRIVIMKDGFIQQIGT 218
Cdd:NF000106 185 DEVRSM-VRDGATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKT 233
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-194 |
5.78e-07 |
|
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: 49.14 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTavhDFnleiaDKEFIVLVGPSGCGKSTTLrmiaglEDISEGdlVIGGKRMN-DVEPKDRDIA--- 79
Cdd:cd03240 4 LSIRNIRSFHERSEI---EF-----FSPLTLIVGQNGAGKTTII------EALKYA--LTGELPPNsKGGAHDPKLIreg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 80 -------MVFQS-----YALYPHMTVYENMAFalklrkVPKEEIDKkvreaaeilditqYLDRKPKALSGGQRQ------ 141
Cdd:cd03240 68 evraqvkLAFENangkkYTITRSLAILENVIF------CHQGESNW-------------PLLDMRGRCSGGEKVlaslii 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 142 RVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRI-NTTFIYVTHD 194
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQkNFQLIVITHD 182
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-230 |
2.10e-06 |
|
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: 48.37 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 13 YDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDV--EPKDRDIAMVFQSYALYp 89
Cdd:cd03288 29 YENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILF- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 90 hmtvyenmAFALKLRKVPKEE-IDKKVREAAEILDITQYLDRKPKAL-----------SGGQRQRVAIGRAIVRDPQVFL 157
Cdd:cd03288 108 --------SGSIRFNLDPECKcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 158 MDEPLSNLDAKLRNQMRAEIIK-LRQRINTTFIYVTHDQTEAmtlgDRIVIMKDGFIQQIGTPQEVFDQPANLF 230
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTaFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-166 |
3.58e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 33 IVLVGPSGCGKSTTLRMIAGLEDISEGDLVIGGKRMNDVEPKDRDIAMVFQSYALYPHMTVYENmafalklrkVPkeeiD 112
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPG---------VP----E 604
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1934240323 113 KKVREAAEILDITQYLDRKPK-ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLD 166
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
104-216 |
4.65e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 104 RKVPKEEIDKKVR--EAAEILDITQYLDRKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLR 181
Cdd:PRK10938 103 AEIIQDEVKDPARceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1934240323 182 QRINT---------------TFIYVTHDQTEAMTlGDRIVIMKDGFIQQI 216
Cdd:PRK10938 183 QSGITlvlvlnrfdeipdfvQFAGVLADCTLAET-GEREEILQQALVAQL 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-216 |
5.93e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 134 ALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDGFI 213
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
...
gi 1934240323 214 QQI 216
Cdd:PRK10982 470 AGI 472
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-211 |
1.36e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 17 VTAVHDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIS--EGDLVIGG-----KRMNDVEpkDRDIAMVFQSYALYP 89
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGevcrfKDIRDSE--ALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 90 HMTVYENMaFaLKLRKVPKEEID--KKVREAAEILDITQyLDRKPKALSG----GQRQRVAIGRAIVRDPQVFLMDEPLS 163
Cdd:NF040905 92 YLSIAENI-F-LGNERAKRGVIDwnETNRRARELLAKVG-LDESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1934240323 164 NLD----AKLRNQMRaeiiKLRQRiNTTFIYVTHDQTEAMTLGDRIVIMKDG 211
Cdd:NF040905 169 ALNeedsAALLDLLL----ELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-209 |
1.86e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.27 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 25 LEIADKEFIVLVGPSGCGKSTTLRMIAgledisegdLVIGGKRMNDVEPKDRDIAMVfqsyalyphmtvyenmafalklr 104
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKAGCI----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 105 kvpkeeidkkvrEAAEILDITQYLDRkpkaLSGGQRQRVAI-----GRAIVRDPqVFLMDEPLSNLDakLRNQMR-AEII 178
Cdd:cd03227 64 ------------VAAVSAELIFTRLQ----LSGGEKELSALalilaLASLKPRP-LYILDEIDRGLD--PRDGQAlAEAI 124
|
170 180 190
....*....|....*....|....*....|.
gi 1934240323 179 KLRQRINTTFIYVTHDQtEAMTLGDRIVIMK 209
Cdd:cd03227 125 LEHLVKGAQVIVITHLP-ELAELADKLIHIK 154
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-208 |
4.31e-05 |
|
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: 43.47 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 11 KIYDNKVTAVHDFNLEIADKEFIVLVGPSGCGKSTTLrmiaglediSEGDLVIGGKRMNDVEPKdrdiamvfqsyaLYPH 90
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---------NEGLYASGKARLISFLPK------------FSRN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 91 MTVyenmaFALKLRKVPKEEIDkkvreaaeilditqY--LDRKPKALSGGQRQRVAIGRAIVRDPQ--VFLMDEPLSNLD 166
Cdd:cd03238 61 KLI-----FIDQLQFLIDVGLG--------------YltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1934240323 167 AKLRNQMRAEIIKLRQRINTTfIYVTHDQTeAMTLGDRIVIM 208
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTV-ILIEHNLD-VLSSADWIIDF 161
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
64-229 |
7.43e-05 |
|
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: 44.62 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 64 GGKRMND----VEPKDRDIAMVFQsyalyphMTVYENMAFALKLRKVPKEE--IDKKVREAAEILDITQ-------YLDR 130
Cdd:TIGR00630 412 GGTRLKPealaVTVGGKSIADVSE-------LSIREAHEFFNQLTLTPEEKkiAEEVLKEIRERLGFLIdvgldylSLSR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 131 KPKALSGGQRQRVA----IGRAIVrdPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQRINtTFIYVTHDQtEAMTLGDRIV 206
Cdd:TIGR00630 485 AAGTLSGGEAQRIRlatqIGSGLT--GVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDE-DTIRAADYVI 560
|
170 180
....*....|....*....|....*....
gi 1934240323 207 IM------KDGFIQQIGTPQEVFDQPANL 229
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANPDSL 589
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-193 |
1.81e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934240323 130 RKPKALSGGQRQRVAIGRAIVRDPQVFLMDEPLSNLDAKLRNQMRAEIIKLRQrintTFIYVTH 193
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
285-321 |
5.12e-04 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 37.98 E-value: 5.12e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1934240323 285 VGIRPEHIAFAAAPgsDTVSSKVDVSEMMGSEVYLHV 321
Cdd:pfam08402 1 LAIRPEKIRLAAAA--NGLSGTVTDVEYLGDHTRYHV 35
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-229 |
7.59e-04 |
|
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: 40.61 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 4 VSLKNVKKIYDNKVTAV-HDFNLEIADKEFIVLVGPSGCGKSTTLRMIAGLEDIsEGDLVIGGKRMNDVEPKDRDIAmvf 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 83 qsYALYPHMTVYENMAFALKLRKVPK---EEIDKKVREAAEILDITQY-------LDRKPKALSGGQRQRVAIGRAIVRD 152
Cdd:cd03289 79 --FGVIPQKVFIFSGTFRKNLDPYGKwsdEEIWKVAEEVGLKSVIEQFpgqldfvLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 153 PQVFLMDEPLSNLDAklrnqMRAEIIK--LRQRINTTFIYVTHDQTEAMTLGDRIVIMKDGFIQQIGTPQEVFDQPANL 229
Cdd:cd03289 157 AKILLLDEPSAHLDP-----ITYQVIRktLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
128-208 |
1.32e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 128 LDRKPKALSGGQRQRVAIGRAIVRDPQ--VFLMDEPLSNLDAKLRNQMRAEIIKLRQRINTTFIyVTHDQtEAMTLGDRI 205
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLV-VEHDE-DTIRAADHV 208
|
...
gi 1934240323 206 VIM 208
Cdd:cd03270 209 IDI 211
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
10-51 |
6.51e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 37.25 E-value: 6.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1934240323 10 KKIYDNKVTAVHDFnLEIADKEFIVLVGPSGCGKSTTLRMIA 51
Cdd:pfam03215 26 RKIKDVQEWLDAMF-LENAKHRILLISGPSGCGKSTVIKELS 66
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
32-188 |
8.15e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 32 FIVLVGPSGCGKSTTLRMIagLEDIsegdlviggkrmndvePKDRDIAMVFqsyalYPHMTV---YENMAFALklrKVPK 108
Cdd:COG3267 45 FVVLTGEVGTGKTTLLRRL--LERL----------------PDDVKVAYIP-----NPQLSPaelLRAIADEL---GLEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934240323 109 EEIDKKVREAAeildITQYLdrkpkALSGGQRQRVAIgraIVRDPQvfLMDEP-------LSN----------------- 164
Cdd:COG3267 99 KGASKADLLRQ----LQEFL-----LELAAAGRRVVL---IIDEAQ--NLPPEtleelrlLSNletdsrkllqivlvgqp 164
|
170 180
....*....|....*....|....*.
gi 1934240323 165 -LDAKL-RNQMRAeiikLRQRINTTF 188
Cdd:COG3267 165 eLRERLaRPELRQ----LRQRITARY 186
|
|
| PRK06851 |
PRK06851 |
hypothetical protein; Provisional |
7-60 |
8.18e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235878 Cd Length: 367 Bit Score: 37.64 E-value: 8.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1934240323 7 KNVKKIYDNKVTA-----VHDFNLEIADKEFIvLVGPSGCGKSTTLRMIaGLEDISEGD 60
Cdd:PRK06851 3 GNVKHYFAGGNTArgfysLYDSIIDGANRIFI-LKGGPGTGKSTLMKKI-GEEFLEKGY 59
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
32-51 |
9.48e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.78 E-value: 9.48e-03
|
| |
