|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-365 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 619.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAM 80
Cdd:COG3839 1 MASLELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSPAM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 241 NFFRGKLTETDFVIDNAiKIKVTEgkmkmlREQGYVNKEIVLGIRPEDIHdellfLEASQSTAFTTKIEVAELLGAESIL 320
Cdd:COG3839 240 NLLPGTVEGGGVRLGGV-RLPLPA------ALAAAAGGEVTLGIRPEHLR-----LADEGDGGLEATVEVVEPLGSETLV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 872564307 321 YMKLGDQDFAARVDARHTFSPSDQIKLAFDINKAHFFDSQTEQRI 365
Cdd:COG3839 308 HVRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-365 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 545.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSPAM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 241 NFFRGKLTETD--FVIDNAIKIKVTEGKMkmlreqGYVNKEIVLGIRPEDIHDellfleASQSTAFTTKIEVAELLGAES 318
Cdd:PRK11650 241 NLLDGRVSADGaaFELAGGIALPLGGGYR------QYAGRKLTLGIRPEHIAL------SSAEGGVPLTVDTVELLGADN 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 872564307 319 ILYMKLGDQDFAARVDARHTFSPSDQIKLAFDINKAHFFDSQTEQRI 365
Cdd:PRK11650 309 LAHGRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-359 |
4.75e-152 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 432.21 E-value: 4.75e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAM 80
Cdd:COG3842 3 MPALELENVSKRYGD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSpaM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 241 NFFRGKLTEtdfviDNAIKIKVTEGKMKMLREQGY-VNKEIVLGIRPEDIHdellFLEASQSTAFTTKIEVAELLGAESI 319
Cdd:COG3842 240 NLLPGTVLG-----DEGGGVRTGGRTLEVPADAGLaAGGPVTVAIRPEDIR----LSPEGPENGLPGTVEDVVFLGSHVR 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 872564307 320 LYMKLGD-QDFAARVDARHT--FSPSDQIKLAFDINKAHFFDS 359
Cdd:COG3842 311 YRVRLGDgQELVVRVPNRAAlpLEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-357 |
1.19e-151 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 431.76 E-value: 1.19e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNVTAvTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAM 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSPAM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 241 NFFRGKLTETDfviDNAIKIKVTEGKMKMLREQG---YVNKEIVLGIRPEdiHdellFLEASQS-TAFTTKIEVAELLGA 316
Cdd:PRK11000 240 NFLPVKVTATA---IEQVQVELPNRQQVWLPVEGrgvQVGANMSLGIRPE--H----LLPSDIAdVTLEGEVQVVEQLGN 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 872564307 317 ESILYMKL--GDQDFAARVDARHTFSPSDQIKLAFDINKAHFF 357
Cdd:PRK11000 311 ETQIHIQIpaIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLF 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.02e-147 |
|
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: 415.89 E-value: 1.02e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-309 |
3.43e-118 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 346.93 E-value: 3.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSpaMNFF 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIF 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 244 RGKLTETdfVIDNAIKIKVTEGKMKMLREQGY-VNKEIVLGIRPEDIHDELLfLEASQSTAFTTKIE 309
Cdd:PRK09452 252 DATVIER--LDEQRVRANVEGRECNIYVNFAVePGQKLHVLLRPEDLRVEEI-NDDEHAEGLIGYVR 315
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
1.87e-115 |
|
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: 334.10 E-value: 1.87e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
1.01e-114 |
|
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: 332.66 E-value: 1.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-328 |
6.17e-114 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 335.19 E-value: 6.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK-LMNDVPPKDRDIAMV 81
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 162 LSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGspAMN 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 242 FFRGKLTETDFVIDNaIKIKVTEgkmkmlreqGYVNKEIVLGIRPEDIHdelLFLEASQSTAFTTKIEVAELLGAESILY 321
Cdd:COG1118 239 VLRGRVIGGQLEADG-LTLPVAE---------PLPDGPAVAGVRPHDIE---VSREPEGENTFPATVARVSELGPEVRVE 305
|
....*..
gi 872564307 322 MKLGDQD 328
Cdd:COG1118 306 LKLEDGE 312
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-357 |
4.37e-109 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 323.10 E-value: 4.37e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND-----VPP 73
Cdd:NF040933 1 VTVRVENVTKIFkkgKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGG 233
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 234 FIGSpaMNFFRGKLTETDFVIDNAIKIKVTEGKMKmlreqgyvNKEIVLGIRPEDIH--DELLFLEASQSTAFTTKIEVA 311
Cdd:NF040933 241 LIGD--INLLEGKVEEEGLVDGNDLKIPLPNPKLE--------AGEVIIGIRPEDIDisESDMRLPPGFVEVGKGRVKVS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 872564307 312 ELLGAESILYMK-LGDQDFAARVDARHTFSPSDQIKLAFDINKAHFF 357
Cdd:NF040933 311 SYAGGVFRVVVSpIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-316 |
1.24e-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: 303.88 E-value: 1.24e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSpaM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--V 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 241 NFFRGKltetdfVIDNAiKIKVTEGKMKMLREQGYVNKEIVLGIRPEDIHdelLFLEASQSTAFTTKIEVAELLGA 316
Cdd:TIGR03265 239 NWLPGT------RGGGS-RARVGGLTLACAPGLAQPGASVRLAVRPEDIR---VSPAGNAANLLLARVEDMEFLGA 304
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-289 |
7.72e-97 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 290.93 E-value: 7.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRV 115
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 116 KDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQ 195
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 196 TEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSpaMNFFRGKLTETD---FVIDNAikikvtEGKMKMLRE 272
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERKseqVVLAGV------EGRRCDIYT 233
|
250
....*....|....*....
gi 872564307 273 QGYV--NKEIVLGIRPEDI 289
Cdd:TIGR01187 234 DVPVekDQPLHVVLRPEKI 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-237 |
1.26e-95 |
|
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: 284.62 E-value: 1.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVF 82
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKI----PKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGS 237
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-289 |
2.63e-95 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 287.77 E-value: 2.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRFGSN-TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSPamNFF 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIF 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 872564307 244 RGKLTEtDFVIDNAIKIKVTEGKmkmlrEQGYVNKEIVLGIRPEDI 289
Cdd:PRK11432 244 PATLSG-DYVDIYGYRLPRPAAF-----AFNLPDGECTVGVRPEAI 283
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
8.04e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 268.11 E-value: 8.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDRD 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 158 MDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKD--GKIQQI 216
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-327 |
1.41e-88 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 270.41 E-value: 1.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:NF040840 2 IRIENLSKDWKE--FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGspAMNFF 243
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 244 RGKLTETDF--VID-NAIKIKVTEGKmkmlreQGYVNkeivLGIRPEDIHDELLFLEASQSTAFTTKIEVAELLGAESIL 320
Cdd:NF040840 238 EGVAEKGGEgtILDtGNIKIELPEEK------KGKVR----IGIRPEDITISTEKVKTSARNEFKGKVEEIEDLGPLVKL 307
|
....*..
gi 872564307 321 YMKLGDQ 327
Cdd:NF040840 308 TLDVGII 314
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-236 |
1.76e-86 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 261.12 E-value: 1.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVtaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIG 236
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-350 |
5.10e-86 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 265.16 E-value: 5.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSpaMNFF 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 244 RGKLTETDfviDNAIKIKvTEGKMKMLREQGYV----NKEIVLGIRPEDIHdellFLEASQSTAFTTKI-EVAEL--LGA 316
Cdd:PRK11607 257 EGVLKERQ---EDGLVID-SPGLVHPLKVDADAsvvdNVPVHVALRPEKIM----LCEEPPADGCNFAVgEVIHIayLGD 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 872564307 317 ESILYMKLGD-QDFAARVDARHTF---SPS--DQIKLAFD 350
Cdd:PRK11607 329 LSIYHVRLKSgQMISAQLQNAHRYrkgLPTwgDEVRLCWE 368
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-236 |
3.11e-85 |
|
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: 3.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQNY 85
Cdd:TIGR00968 3 IANISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 86 ALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR00968 82 ALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 166 DAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIG 236
Cdd:TIGR00968 162 DAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-216 |
4.74e-85 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 257.01 E-value: 4.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN---VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPkdrDIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVM--KDGKIQQI 216
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-237 |
4.62e-82 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 252.32 E-value: 4.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVF 82
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL--EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGS 237
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
1.77e-77 |
|
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: 238.35 E-value: 1.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLE--QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-254 |
1.67e-74 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 234.59 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnvTAV-TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVF 82
Cdd:PRK10851 3 IEIANIKKSFGR--TQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKL---RKIP-KDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGSp 238
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE- 239
|
250
....*....|....*.
gi 872564307 239 aMNFFRGKLTETDFVI 254
Cdd:PRK10851 240 -VNRLQGTIRGGQFHV 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
2.29e-73 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 225.53 E-value: 2.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND----VPPKDRDIA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHMSVYDNMAFGlklrkipkdeidrrvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-235 |
1.08e-71 |
|
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: 224.44 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN-----------------------VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGA 60
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 61 FSIDGKLMNDVPPKD------RDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKA 134
Cdd:cd03294 81 VLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 135 LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQ 214
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|.
gi 872564307 215 QIGTPKEVYETPENIFVGGFI 235
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFF 261
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-236 |
1.37e-68 |
|
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: 219.72 E-value: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPP------KDRDIAMVFQNYALYPHMS 92
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVA 172
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 173 MRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIG 236
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
2.94e-68 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 213.89 E-value: 2.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD--- 77
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 ---IAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMtMASRLVVMKDGKI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-227 |
1.69e-67 |
|
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: 212.19 E-value: 1.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNyalyP-----HMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-217 |
2.50e-67 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 211.38 E-value: 2.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQ---DKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND------VPPKDRDIAMVFQNYALYPHMS 92
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLKLRKIPKDEIdrRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVA 172
Cdd:cd03297 92 VRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 173 MRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
1.00e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 207.59 E-value: 1.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD--- 77
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 ---IAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQtEAMTMASRLVVMKDGKI 213
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-235 |
1.49e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 212.66 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNN-----------------------VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDIS 57
Cdd:COG4175 1 MPKIEVRNLYKIFGKRperalklldqgkskdeilektgqTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 58 KGAFSIDGKLMNDVPPKD------RDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRK 131
Cdd:COG4175 81 AGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 132 PKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
250 260
....*....|....*....|....
gi 872564307 212 KIQQIGTPKEVYETPENIFVGGFI 235
Cdd:COG4175 241 RIVQIGTPEEILTNPANDYVADFV 264
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-231 |
3.04e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 201.45 E-value: 3.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD-IAMVF 82
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP-ENIFV 231
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLlEDVFL 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-221 |
9.81e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 200.37 E-value: 9.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnvtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFG----LKLrkipkDEIDR-RVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlrpgLKL-----TAEQRaQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-222 |
5.31e-62 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 202.25 E-value: 5.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND------VPPKDRDIAMVFQNYALYPHMSVYD 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 96 NMAFGLklRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRS 175
Cdd:COG4148 97 NLLYGR--KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 872564307 176 EISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-214 |
1.14e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.50 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDI 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 159 DEPLSNLDAklrvAMRSEISKLH---HRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQ 214
Cdd:COG2884 162 DEPTGNLDP----ETSWEIMELLeeiNRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
9.93e-60 |
|
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: 200.90 E-value: 9.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYD----NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---- 75
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 -RDIAMVFQN--YALYPHMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 151 RDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-212 |
1.79e-59 |
|
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: 191.14 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIYDNNVTAV-TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNyalyP-HM----SVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
1.42e-58 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 190.46 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNN---VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDvPPKDRd 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 iAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 872564307 158 MDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVM 208
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-226 |
1.11e-57 |
|
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: 187.49 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD-----I 78
Cdd:COG1127 6 IEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFGLK-LRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 158 MDEPLSNLD-------AKLrvamrseISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:COG1127 165 YDEPTAGLDpitsaviDEL-------IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
3.90e-57 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 186.16 E-value: 3.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDN---NVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDI 78
Cdd:COG1124 2 LEVRNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNY--ALYPHMSVYDNMAFGLKLRKIPkdEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 156 FLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
2.92e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 183.66 E-value: 2.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDvPPKD-----RDI 78
Cdd:COG1126 2 IEIENLHKSFGDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFGL-KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 158 MDEPLSNLDAK-----LRVaMRSeiskLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:COG1126 160 FDEPTSALDPElvgevLDV-MRD----LAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
3.95e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 181.02 E-value: 3.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDI 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFG-------LK--LRKIPKDEIDRrVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 150 VRDAKVFLMDEPLSNLDAKL-RVAMRSeISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-229 |
8.33e-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: 180.62 E-value: 8.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPHMSVYDNMAFG----LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 158 MDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPENI 229
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-TPELL 231
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
1.22e-53 |
|
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: 176.28 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELklENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD----- 75
Cdd:TIGR02673 1 MIEF--HNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 156 FLMDEPLSNLDAK-----LRVAMRSeisklhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:TIGR02673 159 LLADEPTGNLDPDlseriLDLLKRL------NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
9.12e-53 |
|
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: 175.70 E-value: 9.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN-VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklMNDVPPKD-----RD 77
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlweirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNyalyPH-----MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRD 152
Cdd:TIGR04520 79 VGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 153 AKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAmTMASRLVVMKDGKIQQIGTPKEVY 223
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-227 |
9.30e-53 |
|
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: 182.41 E-value: 9.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDIS---KGAFSIDGKLMNDVPPKDR--DIAMVFQN--YALYP 89
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrRIGMVFQDpmTQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 hMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:COG1123 99 -VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 170 RVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:COG1123 178 QAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-227 |
1.09e-52 |
|
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: 174.31 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN---VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD----- 75
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 156 FLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-217 |
5.33e-52 |
|
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: 172.31 E-value: 5.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN---VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---- 76
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 77 -DIAMVFQNY--ALYPHMSVYDNMAFGLKLRKIP--KDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIV 150
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 151 RDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
1.05e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.15 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENI-YKIYDNNVtaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:COG4619 1 LELEGLsFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPhMSVYDNMAFGLKLRKIPKDEidRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
1.18e-51 |
|
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: 171.53 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDIAM 80
Cdd:cd03261 3 LRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLK-LRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-217 |
1.93e-51 |
|
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: 170.43 E-value: 1.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDnnvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:TIGR01277 1 LALDKVRYEYE---HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:TIGR01277 78 ENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
5.23e-51 |
|
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: 170.42 E-value: 5.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR-DIAMVF 82
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:COG4555 161 NGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-226 |
8.24e-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: 173.37 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND------VPPKDRDIAMVFQNYALYPHMSVYD 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 96 NMAFGLKlRKIPKDeidRRVKDAA--KILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAM 173
Cdd:TIGR02142 95 NLRYGMK-RARPSE---RRISFERviELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872564307 174 RSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-213 |
1.01e-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: 168.44 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 11 KIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQNYALYPH 90
Cdd:cd03298 5 KIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGL--KLRKIPKDEidRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:cd03298 85 LTVEQNVGLGLspGLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 169 LRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-224 |
1.30e-50 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 169.29 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFGL---------KLRKIPKDEIdRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-227 |
3.57e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 169.17 E-value: 3.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYD----NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---- 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 -RDIAMVFQnyalYPHM-----SVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRA 148
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 149 IVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
4.63e-50 |
|
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: 167.36 E-value: 4.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKiYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISK-----GAFSIDGKLMNDVPPKD--- 75
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 -RDIAMVFQNYALYPhMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGLEQYLDRKPKA--LSGGQRQRVALGRAIVR 151
Cdd:cd03260 80 rRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 152 DAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlgTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-213 |
8.60e-50 |
|
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: 167.23 E-value: 8.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNV---TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlMNDVPPKDRdiAM 80
Cdd:NF040729 2 LKIQNISKTFINNKkenEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGN-EVTKPGPDR--GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVM--KDGKI 213
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrDKGKI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
3.28e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 165.65 E-value: 3.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKleNIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDI-- 78
Cdd:PRK09493 1 MIEFK--NVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 --AMVFQNYALYPHMSVYDNMAFG-LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK09493 78 eaGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 156 FLMDEPLSNLDAKLrvamRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK09493 158 MLFDEPTSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
5.57e-49 |
|
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: 164.24 E-value: 5.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK----DRDIA 79
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHMSVYDNMAFGL-KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 159 DEPLSNLDAKlrvaMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03262 160 DEPTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-228 |
1.79e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.79 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY---DNNVTAVTDFNLHIQDKEfiVF--VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--- 75
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 --RDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG1135 80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 154 KVFLMDEPLSNLDAK-----LRVamrseISKLHHRLGTTTIYVTHDqteaM----TMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:COG1135 160 KVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFA 230
|
....
gi 872564307 225 TPEN 228
Cdd:COG1135 231 NPQS 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-213 |
2.35e-48 |
|
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: 162.58 E-value: 2.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND-----VPPKDRDI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
5.60e-48 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 161.52 E-value: 5.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY-DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR-DIAMV 81
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 162 LSNLDAKLRVAMRSEISKLhhRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-213 |
1.26e-47 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 161.29 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnvtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:PRK10771 2 LKLTDITWLYHH---LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFG----LKLrkipKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlnpgLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-226 |
5.30e-47 |
|
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: 159.55 E-value: 5.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDvPPKDRdiAMVFQNYALYPHMSVYDNMAFGL 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDR--MVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 102 K--LRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISK 179
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 872564307 180 LHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGtpkEVYETP 226
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-245 |
1.06e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 163.67 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD------RDIAMVFQNYALYPHMS 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVA 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 173 MRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVggfigspaMNFFRG 245
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV--------RTFFRG 267
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
1.64e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 159.09 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDvPPKDRdiAMVFQ 83
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-224 |
4.10e-45 |
|
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: 164.62 E-value: 4.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTAV-TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:COG2274 473 DIELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYpHMSVYDNMAFGlklrkipKDEIDR-RVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGR 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG-------DPDATDeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHDqTEAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-213 |
4.65e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 155.22 E-value: 4.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFsidgkLMNDVPPKD--RDIAMV 81
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-----LAGTAPLAEarEDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPHMSVYDNMAFGLKLRKIPkdeidrRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQWRD------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872564307 162 LSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-221 |
1.10e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 161.87 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 13 YDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYpH 90
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGlklrkipKDEIDR-RVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG1132 428 GTIRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
2.72e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.94 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDRDIAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPH--MSVYDNMAFGL----KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQiGTPKEVYeTPENI 229
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVL-TPENL 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
2.87e-44 |
|
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: 150.63 E-value: 2.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR-DIAMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMafglklrkipkdeidrrvkdaakilgleqyldrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
4.25e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 153.63 E-value: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAE--LKLENIYKIYDNNVT-AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-- 75
Cdd:PRK13635 1 MKEeiIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQNyalyPH-----MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIV 150
Cdd:PRK13635 81 RQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 151 RDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-271 |
1.33e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 152.51 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNV----TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDI- 78
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 ---AMVFQ--NYALYPHmSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL--EQYLDRKPKALSGGQRQRVALGRAIVR 151
Cdd:PRK13637 83 kkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 152 DAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVY---ETPEN 228
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFkevETLES 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 872564307 229 IfvggFIGSPAMNFFRGKLTETDFVIDNAIkIKVTEGKMKMLR 271
Cdd:PRK13637 242 I----GLAVPQVTYLVRKLRKKGFNIPDDI-FTIEEAKEEILK 279
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-195 |
1.46e-43 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 149.69 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmNDVPPKDR--------D 77
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKkaskfrreK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 872564307 158 MDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQ 195
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
2.09e-43 |
|
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: 152.90 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENI---YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED---ISKGAFSIDGKLMNDVPPKD-- 75
Cdd:COG0444 2 LEVRNLkvyFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 ----RDIAMVFQN-Y-ALYPHMSVYDNMAFGLKL-RKIPKDEIDRRVKDAAKILGL---EQYLDRKPKALSGGQRQRVAL 145
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDaklrVAMRSEI----SKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*
gi 872564307 222 VYETP 226
Cdd:COG0444 238 LFENP 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
2.33e-43 |
|
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: 148.35 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVF 82
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QnyalyphmsvydnmafglklrkipkdeidrrvkdAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-194 |
7.16e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 148.01 E-value: 7.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIyKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDiskGAFSIDGKLM------NDVPPKDRD 77
Cdd:COG4136 2 LSLENL-TITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS---PAFSASGEVLlngrrlTALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGLKlRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 872564307 158 MDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHD 194
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-224 |
2.24e-42 |
|
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: 147.83 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDI 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNM---AFGLK------LRKIPKDEIdRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
2.25e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 155.30 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALyPHMSVYDNMAFGlklrkipKDEIDR-RVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGR 147
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLG-------RPDASDeELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHDqTEAMTMASRLVVMKDGKIQQIGTPKEVYET 225
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
2.93e-41 |
|
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: 143.77 E-value: 2.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK-DRDIAMVF 82
Cdd:COG4133 3 LEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKIPKDeiDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 872564307 163 SNLDAklrvAMRSEISKL---HHRLGTTTIYVTHDQTEA 198
Cdd:COG4133 160 TALDA----AGVALLAELiaaHLARGGAVLLTTHQPLEL 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
1.37e-40 |
|
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: 140.98 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN-VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYpHMSVYDNMafglklrkipkdeidrrvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHDqTEAMTMASRLVVMKDGK 212
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-275 |
7.85e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.18 E-value: 7.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVT--DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLM--NDVPPKDRDIA 79
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTlnDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNyalyPH-----MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK13650 85 MVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEaMTMASRLVVMKDGKIQQIGTPKEVyetpenifvggf 234
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL------------ 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 872564307 235 igspamnFFRGkltetDFVIDNAIKIKVTEGKMKMLREQGY 275
Cdd:PRK13650 228 -------FSRG-----NDLLQLGLDIPFTTSLVQSLRQNGY 256
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-229 |
8.03e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.05 E-value: 8.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIYDNNVT-AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:PRK13632 9 KVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNyalyPH-----MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK13632 89 FQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAmTMASRLVVMKDGKIQQIGTPKEVYETPENI 229
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-213 |
1.03e-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: 140.20 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN---VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK-DRDIA 79
Cdd:cd03266 2 ITADALTKRFRDVkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-227 |
1.48e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 140.53 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK---LMNDVPPKD---- 75
Cdd:COG4161 2 SIQLKNINCFYGSH-QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAirll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 -RDIAMVFQNYALYPHMSVYDNM-AFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLHHrLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTpKEVYETPE 227
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.72e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 137.39 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHMSVYDNM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 98 AFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRK----PKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-227 |
1.76e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 140.15 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK---LMNDVPPKD----- 75
Cdd:PRK11124 3 IQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQNYALYPHMSVYDNMAFG-LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTpKEVYETPE 227
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-226 |
4.45e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.41 E-value: 4.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDIAMVFQN-YA-LYP 89
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 HMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDa 167
Cdd:COG4608 111 RMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 168 klrVAMRSEI----SKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:COG4608 190 ---VSIQAQVlnllEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
9.58e-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: 137.95 E-value: 9.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---DIAM 80
Cdd:cd03219 1 LEVRGLTKRFGG-LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIP----------KDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIV 150
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 151 RDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
3.03e-38 |
|
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: 143.75 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIYDNN-VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDI 78
Cdd:COG4987 332 PSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYpHMSVYDNMAFGlklrkipKDEI-DRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALG 146
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 147 RAIVRDAKVFLMDEPLSNLDAKLRVAMRSEIskLHHRLGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 872564307 227 E 227
Cdd:COG4987 561 G 561
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
8.89e-38 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 134.63 E-value: 8.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVtAVTDFNLHIQDKeFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD-IAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 163 SNLDAKLRVAMRSEISklhhRLGTTTIYV--THDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03264 159 AGLDPEERIRFRNLLS----ELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-212 |
1.21e-37 |
|
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: 132.75 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVF 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QnyalyphmsvydnmafglklrkipkdeidrrvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872564307 163 SNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:cd00267 109 SGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-226 |
1.38e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.01 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----R 76
Cdd:PRK11153 3 ELKNISKVFpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 77 DIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
1.48e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 135.55 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---D 77
Cdd:COG0411 2 DPLLEVRGLTKRFGG-LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMA---------------FGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQR 142
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 143 VALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
2.83e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 132.27 E-value: 2.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAfSIDGKL--------MNDVPPKD 75
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEA-RVEGEVrlfgrniySPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 --RDIAMVFQNYALYPHMSVYDNMAFGLKLRKI--PKDEIDRRVKDAAKILGL-EQYLDR---KPKALSGGQRQRVALGR 147
Cdd:PRK14267 83 vrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAklrvAMRSEISKLHHRLGT--TTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYET 225
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDP----VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
...
gi 872564307 226 PEN 228
Cdd:PRK14267 239 PEH 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
6.34e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 131.36 E-value: 6.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYD----NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR--D 77
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYAL--YPHMSVYDNMA--------FGLKLRkIPKDEIDRrVKDAAKIL--GLEQYLDRKPKALSGGQRQRVAL 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRG-LTKKRREL-FRELLATLglGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDAKlrvamRSEI-----SKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPK-----TAALvleltEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-222 |
2.95e-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: 128.88 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHmSVYDNMAFGlklRKIPKDEidrRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVALGRA 148
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 149 IVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-213 |
3.63e-35 |
|
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: 128.09 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVT-AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:cd03245 2 RIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYpHMSVYDNMAFGLKLRKipkdeiDRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRA 148
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 149 IVRDAKVFLMDEPLSNLDaklrvaMRSEiSKLHHRL-----GTTTIYVTHdQTEAMTMASRLVVMKDGKI 213
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD------MNSE-ERLKERLrqllgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
16-237 |
6.50e-35 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 128.41 E-value: 6.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 16 NVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---------------RDIAM 80
Cdd:TIGR03005 12 ILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadekhlrqmrNKIGM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRK-IPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:TIGR03005 92 VFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGFIGS 237
Cdd:TIGR03005 172 EVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSK 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-213 |
1.35e-34 |
|
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: 126.49 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 15 NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDRDIAMVFQNYAL---YPhM 91
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 92 SVYDNMAFGL----KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03235 86 SVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872564307 168 KLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03235 166 KTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
1.35e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 126.72 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 7 ENIYKIYDNNVtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmNDV--PPKD--RDIAMVF 82
Cdd:cd03265 4 ENLVKKYGDFE-AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVvrEPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
1.80e-34 |
|
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: 126.78 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNN---VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDRD--- 77
Cdd:COG4181 9 IELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 ------IAMVFQNYALYPHMSVYDNMAFGLKLRKIPkDEIDRrvkdAAKIL---GLEQYLDRKPKALSGGQRQRVALGRA 148
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRR-DARAR----ARALLervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 149 IVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAmTMASRLVVMKDGKIQQ 215
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-213 |
2.63e-34 |
|
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: 125.93 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---- 76
Cdd:TIGR02211 2 LKCENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 77 --DIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMaSRLVVMKDGKI 213
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-213 |
4.33e-34 |
|
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: 125.06 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDR--DIAMVFQ 83
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERrkSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 N--YALYPHmSVYDNMAFGLKlrkiPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03226 79 DvdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 162 LSNLDAKlrvAMRSeISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03226 154 TSGLDYK---NMER-VGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-229 |
8.15e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 125.58 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKIYDNNVTaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVF 82
Cdd:COG4604 3 EIKNVSKRYGGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 QNYALYPHMSVYDNMAFGL----KLRKIPKDEidRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpysKGRLTAEDR--EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTP---------KEVYETPENI 229
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPeeiitpevlSDIYDTDIEV 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-226 |
1.49e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 127.30 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 37 GPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND------VPPKDRDIAMVFQNYALYPHMSVYDNMAFGLKlrKIPKDE 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 111 IDRRVKdaakILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIY 190
Cdd:PRK11144 109 FDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 872564307 191 VTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-226 |
3.44e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 124.71 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMND---VPPKDRDIAM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQN-YALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDqTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-227 |
3.64e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.75 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSI------DGKLMNDVPPKDRDIAMVFQnyalYP-HM 91
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 92 ----SVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 167 AKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
7.65e-33 |
|
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: 121.56 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRrvkdAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872564307 164 NLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
9.06e-33 |
|
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: 121.77 E-value: 9.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---DIAM 80
Cdd:cd03224 1 LEVENLNAGYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKipKDEIDRRVkdaAKILG----LEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARR--RAKRKARL---ERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-224 |
1.10e-32 |
|
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: 122.26 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 16 NVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPhMSV 93
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 94 YDNMAFGLKlrkipkDEIDRRVKDAAK-------ILGLEQYLD----RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03249 94 AENIRYGKP------DATDEEVEEAAKkanihdfIMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 163 SNLDAKLRVAMRSEISKLhhRLGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:cd03249 168 SALDAESEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-213 |
1.18e-32 |
|
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: 121.23 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPpkDRDIAMVFQ 83
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872564307 164 NLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-222 |
1.84e-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: 128.45 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENI-YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:TIGR03375 463 EIEFRNVsFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYpHMSVYDNMAFGlklRKIPKDEidrRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRA 148
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG---APYADDE---EILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 149 IVRDAKVFLMDEPLSNLDaklrvaMRSEiSKLHHRL-----GTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMD------NRSE-ERFKDRLkrwlaGKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-228 |
3.08e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 8 NIYkiYDNNVtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAfSIDGKLM--------NDVPPKD--RD 77
Cdd:COG1117 18 NVY--YGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGA-RVEGEILldgediydPDVDVVElrRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPhMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGL----EQYLDRKPKALSGGQRQRVALGRAIVRD 152
Cdd:COG1117 94 VGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 153 AKVFLMDEPLSNLD--AKLRVamrsE--ISKLHHRLgtTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:COG1117 173 PEVLLMDEPTSALDpiSTAKI----EelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
3.46e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.72 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMnDVPPKD-----RDI 78
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSllevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQN-----YAlyPhmSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK13639 81 GIVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 154 KVFLMDEPLSNLDAKlrvaMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENI 229
Cdd:PRK13639 157 EIIVLDEPTSGLDPM----GASQIMKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
4.12e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.90 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-RD--IAM 80
Cdd:COG1129 5 LEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKdeIDRR--VKDAAKIL---GLEQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGL--IDWRamRRRARELLarlGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 156 FLMDEPLSNLDAKlrvamrsEISKLH---HRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIqqIGT 218
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFriiRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-227 |
9.00e-32 |
|
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: 125.18 E-value: 9.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDiSKGAFSIDGKLMNDVPPKD-----RDIAMVFQN-YA-LYP 89
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 HMSVYDNMAFGLKLRKIP--KDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:COG4172 378 RMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 167 aklrVAMRSEI----SKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:COG4172 458 ----VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-213 |
1.24e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 120.30 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDIAMVFQNY--ALYPH 90
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGLK-LRKIPKDEIDRRVKDAAKILGLE-QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 169 LRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-208 |
1.29e-31 |
|
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: 124.71 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHmSVYDNMAFGLklRKIPKDEIDRRVKDA-------AKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEIREALERAgldefvaALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLhhRLGTTTIYVTHDqTEAMTMASRLVVM 208
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-226 |
1.64e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 119.52 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY-DNNVtaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVP-------PKD 75
Cdd:COG4598 9 LEVRDLHKSFgDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RD--------IAMVFQNYALYPHMSVYDNMAFG-LKLRKIPKDE-IDRRVKDAAKIlGLEQYLDRKPKALSGGQRQRVAL 145
Cdd:COG4598 87 RRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEaIERAEALLAKV-GLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDAK-----LRVaMRS---EisklhhrlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPElvgevLKV-MRDlaeE--------GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
....*....
gi 872564307 218 TPKEVYETP 226
Cdd:COG4598 237 PPAEVFGNP 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.90e-31 |
|
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: 124.53 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY---DNNVT-AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSI----DGKLMNDVPPKD 75
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RD-----IAMVFQNYALYPHMSVYDNM--AFGLKLrkiPKDEIDRRVKDAAKILGL-----EQYLDRKPKALSGGQRQRV 143
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 144 ALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVY 223
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
.
gi 872564307 224 E 224
Cdd:TIGR03269 517 E 517
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-223 |
2.63e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.81 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDG---KLMNDVPPKDRDIAMVFQNyalyPH 90
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MS-----VYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK13633 96 NQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 166 DAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKEVY 223
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-215 |
2.67e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.38 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPP------KDRDIAMVFQNYALYPHMSVYD 95
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 96 NMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRS 175
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872564307 176 EISKLHHRLGTTTIYVTHDQTEAMTMaSRLVVMKDGKIQQ 215
Cdd:PRK11629 187 LLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
8.98e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.54 E-value: 8.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED-----ISKGAFSID-----GKLMND 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDtarslSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 71 VPPKDRDIAMVFQNYALYPHMSVYDNMAFG-LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIyVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-261 |
1.03e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL---EDISKGAFSIDG-----KLMNDVPPKdrdIAMVFQNY 85
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGitltaKTVWDIREK---VGIVFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 86 -ALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK13640 94 dNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 165 LDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAmTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGfIGSPAMNFFR 244
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIG-LDIPFVYKLK 251
|
250
....*....|....*..
gi 872564307 245 GKLTETDFVIDNAIKIK 261
Cdd:PRK13640 252 NKLKEKGISVPQEINTE 268
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-213 |
1.57e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.10 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-----RDIAMVFQNY--ALYPH 90
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGLK-LRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 169 LRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-226 |
3.32e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.89 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR-----DIAMVFQN--YALYPHM 91
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 92 SVYDNMAFGLKLR--KIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 169 LRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-224 |
3.96e-30 |
|
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: 115.41 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYpHMSVYDN 96
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 97 MAFGLKlrkipkDEIDRRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:cd03251 96 IAYGRP------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 166 DAKLRVAMRSEISKLHHrlGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:cd03251 170 DTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
4.44e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.75 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVP-------PKDR 76
Cdd:COG4152 2 LELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 77 diamvfqnyALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:COG4152 81 ---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 157 LMDEPLSNLDAklrVA---MRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:COG4152 152 ILDEPFSGLDP---VNvelLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-213 |
4.83e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 114.59 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDG----KLMN-DVPPKDRDI 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditRLKNrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 159 DEPLSNLDAklrvAMRSEISKL---HHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK10908 162 DEPTGNLDD----ALSEGILRLfeeFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-229 |
7.50e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.58 E-value: 7.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYD--NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN--DVPPKDRDIA 79
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNY-ALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKEVYETPENI 229
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-204 |
4.55e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.34 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIyKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGaFSIDGKLM--------NDVPPK 74
Cdd:PRK14243 10 VLRTENL-NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 75 D--RDIAMVFQNYALYPHmSVYDNMAFGLKLR--KIPKDE-IDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:PRK14243 88 EvrRRIGMVFQKPNPFPK-SIYDNIAYGARINgyKGDMDElVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 150 VRDAKVFLMDEPLSNLD--AKLRvamrseISKLHHRLGT--TTIYVTHDqteaMTMASR 204
Cdd:PRK14243 167 AVQPEVILMDEPCSALDpiSTLR------IEELMHELKEqyTIIIVTHN----MQQAAR 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
36-224 |
5.52e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQN--YALYPHMSVYDnMAFGLKLRKIPKDEI 111
Cdd:PRK13648 41 VGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpdNQFVGSIVKYD-VAFGLENHAVPYDEM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 112 DRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYV 191
Cdd:PRK13648 120 HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISI 199
|
170 180 190
....*....|....*....|....*....|...
gi 872564307 192 THDQTEAMTmASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:PRK13648 200 THDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-227 |
9.44e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:PRK11231 2 TLRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFG----LKL--RKIPKDEidRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGrspwLSLwgRLSAEDN--ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 155 VFLMDEPLSNLDAKLRVamrsEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPE 227
Cdd:PRK11231 159 VVLLDEPTTYLDINHQV----ELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-TPG 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
1.54e-28 |
|
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: 110.84 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---D 77
Cdd:COG0410 1 MPMLEVENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKiPKDEIDRRVkdaAKILG----LEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADL---ERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-215 |
1.85e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 110.64 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR------DIAMVFQNYAL 87
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 88 YPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK10584 100 IPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872564307 168 KLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLvVMKDGKIQQ 215
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL-RLVNGQLQE 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-228 |
2.22e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.29 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 12 IYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN--------DVPPKDRDIAMVFQ 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIP-KDEIDRRVKDAAKILGL--EQY--LDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLHHRLgtTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
4.53e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.60 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNyalyPH-----MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK13647 85 FQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTP 219
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
5.04e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIyKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL-----EDISKGAFSIDGK--LMNDVPP 73
Cdd:PRK14247 1 MNKIEIRDL-KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQdiFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKD--EIDRRVKDAAKILGL----EQYLDRKPKALSGGQRQRVALGR 147
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLgtTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
.
gi 872564307 228 N 228
Cdd:PRK14247 238 H 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-221 |
5.05e-28 |
|
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: 109.63 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQ 83
Cdd:cd03253 3 FENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYpHMSVYDNMAFGlKLrkipkDEIDRRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVALGRAIVRD 152
Cdd:cd03253 83 DTVLF-NDTIGYNIRYG-RP-----DATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 153 AKVFLMDEPLSNLDAKLRVAMRSEISKLhhRLGTTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKE 221
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-229 |
8.63e-28 |
|
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: 109.40 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGA-FSIDGKLMNDVPPKD--RDIAM 80
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWElrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 V---FQNYaLYPHMSVYDnM----AFG-LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRD 152
Cdd:COG1119 83 VspaLQLR-FPRDETVLD-VvlsgFFDsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 153 AKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPENI 229
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL-TSENL 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-222 |
1.38e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKD-RD----- 77
Cdd:COG3845 6 LELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSpRDaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGL---KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 155 VFLMDEPLSNL-----DAKLRV--AMRSEisklhhrlGTTTIYVTHDQTEAMTMASRLVVMKDGKIqqIGT--PKEV 222
Cdd:COG3845 162 ILILDEPTAVLtpqeaDELFEIlrRLAAE--------GKSIIFITHKLREVMAIADRVTVLRRGKV--VGTvdTAET 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-228 |
2.28e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.52 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDI---------------AMVFQNYALYPHMSVYD 95
Cdd:PRK10619 32 DVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrllrtrlTMVFQHFNLWSHMTVLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 96 N-MAFGLKLRKIPKDEI-DRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLrvam 173
Cdd:PRK10619 112 NvMEAPIQVLGLSKQEArERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL---- 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 174 RSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK10619 188 VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-228 |
2.54e-27 |
|
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: 107.45 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED----ISKGAFSIDGKLMNDVPPKDRDIAMVFQN--YALYPHMS 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL---EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 170 RVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
22-226 |
2.97e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 113.13 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN--DVPPKDRDIAMVFQNYALYPHmSVYDNMAF 99
Cdd:TIGR03797 471 DVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFENIAG 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 100 GLKLrkiPKDEidrrVKDAAKILGLEQYLDRKP-----------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR03797 550 GAPL---TLDE----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNR 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 169 LRvAMRSEISKlhhRLGTTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:TIGR03797 623 TQ-AIVSESLE---RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
3.05e-27 |
|
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: 105.20 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---RDIAM 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQnyalyphmsvydnmafglklrkipkdeidrrvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
5.08e-27 |
|
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: 104.99 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAV-TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-RD-IAM 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHmSVYDNMafglklrkipkdeidrrvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHdQTEAMTMASRLVVMKDGKI 213
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-199 |
6.32e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmndvppkDRDIAMVFQNYAL---YPhMSVY 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 95 DNMAFGL-----KLRKIPKDeiDRRVKDAA-KILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:NF040873 76 DLVAMGRwarrgLWRRLTRD--DRAAVDDAlERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|.
gi 872564307 169 LRVAMRSEISKLHHRlGTTTIYVTHDQTEAM 199
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
1.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK--------LMNdvppKD 75
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkgLMK----LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQ--NYALYPhMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK13636 82 ESVGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENI 229
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-222 |
1.72e-26 |
|
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: 110.52 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDN-NVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:TIGR01842 316 HLSVENVTIVPPGgKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHmSVYDNMA-FGlklrkipKDEIDRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGR 147
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIArFG-------ENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-229 |
2.07e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.22 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIYDNNVTAvTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYAL--------------YPHMSVYDnmafglKLRKIPKDEIDRrvkdAAKILGLEQYLDRKPKALSGGQRQRVAL 145
Cdd:PRK10253 85 LLAQNATTpgditvqelvargrYPHQPLFT------RWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeT 225
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-T 233
|
....
gi 872564307 226 PENI 229
Cdd:PRK10253 234 AELI 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-221 |
3.63e-26 |
|
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: 109.42 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY-DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHmSVYDNMAFGlKLRKIPKDEIDRRVKDA-------AKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAAAyaqdfvdKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNE 553
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-227 |
5.68e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.85 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 21 TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmNDVPPKDRD--------IAMVFQNYALYPHMS 92
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPAMSRSrlytvrkrMSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLKLR-KIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:PRK11831 101 VFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 172 AMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-226 |
7.06e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.82 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDV--PPKD------RDIAMVFQN-YA-LYPHMSVYDNMAFGLKLR- 104
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQ---DLlkADPEaqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINt 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 105 KIPKDEIDRRVKDAAKILGL--EQYlDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHH 182
Cdd:PRK11308 124 SLSAAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872564307 183 RLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK11308 203 ELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
9.06e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 9.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDI 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQN---YALYPhmSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 156 FLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
1.14e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.96 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDIsKGAFSIDGKL----------MNDVPP 73
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQNYALYPhMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGL----EQYLDRKPKALSGGQRQRVALGRA 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 149 IVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKD-----GKIQQIGTPKEVY 223
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
...
gi 872564307 224 ETP 226
Cdd:PRK14258 245 NSP 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-227 |
1.14e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.70 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEdISKGAFSIDG--------KLMNDVPPKDRDIAMVFQ--NYALY 88
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVGdyaipanlKKIKEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 89 PHmSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 168 KLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-217 |
1.23e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 103.00 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmndvppkdRDIAMVFQNYALYPHMSVYDN 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGLGGGFNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 97 MAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA----KLRVA 172
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAafqeKCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 173 MRSEISKlhhrlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIG 217
Cdd:cd03220 185 LRELLKQ-----GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-228 |
1.37e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.32 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 12 IYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDIS-----KGAFSIDGKlmNDVPPKD------RDIAM 80
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGH--NIYSPRTdtvdlrKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPhMSVYDNMAFGLKLRKIpKDE------IDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKGI-KDKqvldeaVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 155 VFLMDEPLSNLDAKlrVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK14239 169 IILLDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-222 |
1.83e-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: 107.53 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENI-YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmNDVPPKDRDiam 80
Cdd:COG4618 329 GRLSVENLtVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWDRE--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 vfqnyALYPHM------------SVYDNMA-FGlklrkipkDEIDRRVKDAAK-------ILGLEQ-Y---LDRKPKALS 136
Cdd:COG4618 403 -----ELGRHIgylpqdvelfdgTIAENIArFG--------DADPEKVVAAAKlagvhemILRLPDgYdtrIGEGGARLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 137 GGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQI 216
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAF 547
|
....*.
gi 872564307 217 GTPKEV 222
Cdd:COG4618 548 GPRDEV 553
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-197 |
3.37e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENI-YKIYDNNVtaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:PRK10247 8 LQLQNVgYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHmSVYDNMAFGLKLRKIPKDEiDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDP-AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTE 197
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-194 |
5.74e-25 |
|
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: 105.91 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNyalyPHM---SVYDNMAFGlklrkiPKDEIDRRVKDAAKILGLEQYLDRKP-----------KALSGGQRQRVALGR 147
Cdd:TIGR02868 415 AQD----AHLfdtTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMRSEIskLHHRLGTTTIYVTHD 194
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-227 |
6.55e-25 |
|
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: 101.08 E-value: 6.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---DIAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 161 PLSNLDAKlrvaMRSEISKLHHRLGTTTIYV---THDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:cd03218 160 PFAGVDPI----AVQDIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-224 |
7.55e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.13 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN------DVPPKDRDIAMVFQnyalYPHMS 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYD-----NMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK13649 98 LFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 167 AKLRVAMRSEISKLHHrLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:PRK13649 178 PKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
8.54e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.58 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD-IAM 80
Cdd:PRK13537 6 APIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMA-----FGLklrkiPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLvfgryFGL-----SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 156 FLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDG-KIQQiGTPKEVYET 225
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGrKIAE-GAPHALIES 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-229 |
9.14e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYAL-YPhMSVY 94
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-FTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 95 DNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVR------DAKVFLMDEPLSNLDAK 168
Cdd:PRK13548 95 EVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 169 -----LRVAMRseiskLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPENI 229
Cdd:PRK13548 175 hqhhvLRLARQ-----LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-TPETL 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
1.74e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNvTAVTDFNLHIQDKEfIV-FVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVP------- 72
Cdd:COG1137 1 MMTLEAENLVKSYGKR-TVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 73 -----PKDrdiAMVFQNyalyphMSVYDN-MAFgLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALG 146
Cdd:COG1137 79 gigylPQE---ASIFRK------LTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 147 RAIVRDAKVFLMDEPLSNLDAkLRVA-MRSEISKLHHR-LGtttIYVT-HDQTEAMTMASRLVVMKDGKIQQIGTPKEVY 223
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDP-IAVAdIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
....
gi 872564307 224 ETPE 227
Cdd:COG1137 225 NNPL 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-234 |
2.11e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.42 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIY---DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDRD- 77
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ---DVATLDADa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 --------IAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:PRK10535 80 laqlrrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAmTMASRLVVMKDGKI----------QQIGTP 219
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIvrnppaqekvNVAGGT 237
|
250
....*....|....*..
gi 872564307 220 KEVYETPENI--FVGGF 234
Cdd:PRK10535 238 EPVVNTASGWrqFVSGF 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-226 |
2.29e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.00 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYAL------- 87
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfefdvr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 88 -------YPHMSVYDNMafglklrkipkDEIDRR-VKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK09536 96 qvvemgrTPHRSRFDTW-----------TETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDqteaMTMASR----LVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHD----LDLAARycdeLVLLADGRVRAAGPPADVLTAD 230
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-226 |
2.57e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 104.26 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPpkdRDI-----AMVFQNYALYpHMSVY 94
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP---REVlansvAMVDQDIFLF-EGTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 95 DNMAfgLKLRKIPKDEIDRRVKDAA---KIL----GLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:TIGR03796 571 DNLT--LWDPTIPDADLVRACKDAAihdVITsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 168 KLRVAMRSEIsklhHRLGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:TIGR03796 649 ETEKIIDDNL----RRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-228 |
3.06e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.17 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVP-----PKDRDIAMVFQN-YA-LYP 89
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 HMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGLE-QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 168 KLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH 557
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-224 |
3.17e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAE-LKLENI---YKIYDNN------------------VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISK 58
Cdd:COG1134 1 MSSmIEVENVsksYRLYHEPsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 59 GAFSIDGK---LMndvppkdrDIAMVFQnyalyPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKAL 135
Cdd:COG1134 81 GRVEVNGRvsaLL--------ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 136 SGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA----KLRVAMRSEISKlhhrlGTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
250
....*....|...
gi 872564307 212 KIQQIGTPKEVYE 224
Cdd:COG1134 223 RLVMDGDPEEVIA 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-214 |
5.36e-24 |
|
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: 98.56 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndVPPKDRD-----IAMVF-QNYALYPH 90
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKkflrrIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872564307 171 VAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQ 214
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-250 |
1.91e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVT----AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN------DVPP 73
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQnyalYPHMSVYD-----NMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGR 147
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
250 260
....*....|....*....|...
gi 872564307 228 nIFVGGFIGSPAMNFFRGKLTET 250
Cdd:PRK13643 237 -FLKAHELGVPKATHFADQLQKT 258
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
3.12e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---D 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGLKLRK-IPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-218 |
3.13e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 24 NLHIQDKEFIVFVGPSGCGKSTTLRMVAGLedIS-KGAFSIDGKLMNDVPPKD--RDIAMVFQNYALyPHMSVYDNMAFG 100
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 101 LKlrKIPKDEIDRRVKDAakilGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAkl 169
Cdd:PRK11174 447 NP--DASDEQLQQALENA----WVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA-- 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 170 rvamRSE---ISKLHH-RLGTTTIYVTH--DQTEAMtmaSRLVVMKDGKIQQIGT 218
Cdd:PRK11174 519 ----HSEqlvMQALNAaSRRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGD 566
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-212 |
4.99e-23 |
|
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: 95.23 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndvppkdrdIAMVFQNyALYPHMSVYDNMAFGL 101
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 102 KLRKipkdeidRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklR 170
Cdd:cd03250 91 PFDE-------ERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA--H 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 171 VA---MRSEISKlHHRLGTTTIYVTHdQTEAMTMASRLVVMKDGK 212
Cdd:cd03250 162 VGrhiFENCILG-LLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-227 |
5.14e-23 |
|
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: 100.14 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTT----LRMVAGLEDISKGAFSIDGKLMNDVPPKD------RDIAMVFQ 83
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 N--YALYPHMSVYDNMAFGLKL-RKIPKDEIDRRVKDAAKILGL---EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG4172 100 EpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 158 MDEPLSNLDaklrVAMRSEI----SKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:COG4172 180 ADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-252 |
5.82e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVT----AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN------DVPP 73
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQnyalYPHMSVYDN-----MAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGR 147
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 148 AIVRDAKVFLMDEPLSNLDAKLRVAMrSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
250 260
....*....|....*....|....*
gi 872564307 228 NIfVGGFIGSPAMNFFRGKLTETDF 252
Cdd:PRK13641 238 WL-KKHYLDEPATSRFASKLEKGGF 261
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-222 |
6.21e-23 |
|
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: 95.69 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDRDIAMVFQNYAL---YPhMSVYDNMAFG----LKL 103
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGrtghIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 104 RKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD---AKLRVAMRSEISKl 180
Cdd:TIGR03771 83 LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFIELAG- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 872564307 181 hhrLGTTTIYVTHDQTEAMTMASRLVVMkDGKIQQIGTPKEV 222
Cdd:TIGR03771 162 ---AGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-234 |
1.06e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHiqdkEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN----DVPPKDRDIAMVFQNyalyPHMSVY--- 94
Cdd:PRK13638 23 DFSLS----PVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIFytd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 95 --DNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVA 172
Cdd:PRK13638 95 idSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 173 MRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIFVGGF 234
Cdd:PRK13638 175 MIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-213 |
1.21e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 96.69 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndVPPKDR-----DIAMVF-QNYALYPH 90
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----VPFKRRkefarRIGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNmaFGL--KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:COG4586 111 LPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 872564307 169 LRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:COG4586 189 SKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-222 |
1.64e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 99.05 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAV-TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK--DRDIAM 80
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHmSVYDNMAFGLKlrKIPkdeiDRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAI 149
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNP--GAP----FEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRS---EISKlhhrlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRnmrEICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
1.92e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL--EDISKGA--------FSIDGKLMNDVPP 73
Cdd:PRK09984 5 IRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShiellgrtVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQNYALYPHMSVYDNMAFGlKLRKIP---------KDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVA 144
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 145 LGRAIVRDAKVFLMDEPLSNLDAK-LRVAMRSeISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-229 |
2.20e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.80 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHMSVYD 95
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 96 NMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIV-------RDAKVFLMDEPLSNLD-- 166
Cdd:COG4559 95 VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDla 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 167 ---AKLRVAmrseiSKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPENI 229
Cdd:COG4559 175 hqhAVLRLA-----RQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL-TDELL 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-260 |
3.30e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.15 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNN----VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL--------------EDISKGAFSID 64
Cdd:PRK13651 2 QIKVKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 65 GKLMNDV--PPKDRDI----------AMVFQ--NYALYpHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLD 129
Cdd:PRK13651 82 KVLEKLViqKTRFKKIkkikeirrrvGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 130 RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMK 209
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 872564307 210 DGKIQQIGTPKEVYETpENIFVGGFIGSPAMNFFRGKLTETDFVIDNAIKI 260
Cdd:PRK13651 240 DGKIIKDGDTYDILSD-NKFLIENNMEPPKLLNFVNKLEKKGIDVPKVTSI 289
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-222 |
5.97e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.50 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 13 YDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVppkDRDIAMVFQNY-ALYPHM 91
Cdd:TIGR01193 483 YGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 92 ---SVYDNMAFGLKlRKIPKDEIDRRVkDAAKI--------LGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:TIGR01193 560 fsgSILENLLLGAK-ENVSQDEIWAAC-EIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRlgtTTIYVTHDQTEAmTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-167 |
6.34e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIdgklmndvpPKDRDIAMVFQNY 85
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 86 ALYPHMSVYDNMAFGLK-LRKIPKD-------------------------------EIDRRVKDAAKILGL-EQYLDRKP 132
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAeLRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRPV 150
|
170 180 190
....*....|....*....|....*....|....*
gi 872564307 133 KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-229 |
6.78e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 23 FNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDiSKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHMSVYDNMAFG 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 101 LKlRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVR-------DAKVFLMDEPLSNLDAKLRVAM 173
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 174 RSEISKLHHrLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPENI 229
Cdd:COG4138 173 DRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
7.81e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.53 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYD----NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL----------EDISKGAFSIDGKLMN 69
Cdd:PRK13631 22 LRVKNLYCVFDekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 70 DVPPKD--------RDIAMVFQ--NYALYPHmSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGG 138
Cdd:PRK13631 102 NPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 139 QRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMrSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGT 218
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*....
gi 872564307 219 PKEVYETPE 227
Cdd:PRK13631 260 PYEIFTDQH 268
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-226 |
1.01e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 10 YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL---EDISKGAFSIDGKLMNDVPPKD------RDIAM 80
Cdd:PRK09473 22 FSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQN--YALYPHMSVYDNMAFGLKLRK-IPKDE-IDRRVK--DAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK09473 102 IFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEaFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-213 |
2.64e-21 |
|
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: 90.30 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED--ISKGAFSIDGKLMNDVPPKDRdIAMVFQNYALYPHMSVYDNM 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 98 AFGLKLRKIpkdeidrrvkdaakilgleqyldrkpkalSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEI 177
Cdd:cd03213 104 MFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 872564307 178 SKLHHrLGTTTIYVTHD-QTEAMTMASRLVVMKDGKI 213
Cdd:cd03213 155 RRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-213 |
6.13e-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: 89.03 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD---IAMV---FQNYALYPHMS 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLklrkipkdeidrrvkdaakilgleqyldrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVA 172
Cdd:cd03215 95 VAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872564307 173 MRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:cd03215 139 AKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
6.78e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDG-KLMNDVPPKD-----RDIAMVFQnyalYPHMS 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYirpvrKRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDN-----MAFGLKLRKIPKDEIDRRVKDAAKILGLEQ-YLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK13646 98 LFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 167 AKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVY 223
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-219 |
7.61e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.70 E-value: 7.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYD-NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK-LMNDVPPKDRDIAMVFQ 83
Cdd:TIGR01257 931 VKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 164 NLDAKLRVAMRSEIskLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTP 219
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-218 |
1.28e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.10 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 13 YDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYpH 90
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLF-N 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGlklrkiPKDEIDRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK13657 423 RSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 160 EPLSNLDAKLRVAMRSEISKLHHrlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGT 218
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-228 |
2.32e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTT----LRMVAglediSKGAFSIDGKLMNDVPPKD-----RDIAMVFQ--NYA 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 87 LYPHMSVYDNMAFGLKL--RKIPKDEIDRRVKDAAKILGLE-QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 164 NLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-213 |
3.08e-20 |
|
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: 88.30 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHiqDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK--DRDIAMVFQNYALYPHm 91
Cdd:cd03248 26 DTLVLQDVSFTLH--PGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 92 SVYDNMAFGLKlrkipkDEIDRRVKDAAK-------ILGLEQYLD----RKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03248 103 SLQDNIAYGLQ------SCSFECVKEAAQkahahsfISELASGYDtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRlgTTTIYVTHdQTEAMTMASRLVVMKDGKI 213
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
5.07e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---DIAM 80
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFG-LKLRK------IPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 154 KVFLMDEPLSNLDAKlrvamrsEISKLH---HRL---GTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK09700 165 KVIIMDEPTSSLTNK-------EVDYLFlimNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-222 |
6.22e-20 |
|
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: 87.54 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK--DRDIAMVFQNYALYpHMSVYDN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 97 MAFGLKLRKIpkdeidRRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:cd03252 96 IALADPGMSM------ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 166 DAKLRVAMRSEISKLHHrlGTTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKEV 222
Cdd:cd03252 170 DYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-226 |
9.93e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 9.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMN--DVPPKDRDIAMVFQN--YALYPHMS 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAFGLKLR-KIPKDEIDRRVKDAAKILGL-EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklr 170
Cdd:PRK15112 106 ISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD---- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 171 VAMRSEISKLHHRL----GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK15112 182 MSMRSQLINLMLELqekqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-193 |
1.12e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 15 NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndvPPKDRDIAMVF-----QNyALYP 89
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-----DIDDPDVAEAChylghRN-AMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 HMSVYDNMAFGLKLRkipkDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKl 169
Cdd:PRK13539 87 ALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA- 161
|
170 180
....*....|....*....|....
gi 872564307 170 RVAMRSEISKLHHRLGTTTIYVTH 193
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-212 |
1.13e-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: 87.08 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 27 IQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmNDVPPKDRDIAMVFQnyalyphMSVYDnmafglKLRKI 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL---DTVSYKPQYIKADYE-------GTVRD------LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 107 PKD--EIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRL 184
Cdd:cd03237 86 TKDfyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|....*...
gi 872564307 185 GTTTIYVTHDQTEAMTMASRLVVMkDGK 212
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-226 |
1.26e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 16 NVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK--DRDIAMVFQNYALYPHmSV 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 94 YDNMAFGLklRKIPKDEIDRRVKDAAK---ILGLEQYLD----RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:TIGR00958 572 RENIAYGL--TDTPDEEIMAAAKAANAhdfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 167 AKLRVAMRSEISklhhRLGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:TIGR00958 650 AECEQLLQESRS----RASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-219 |
2.82e-19 |
|
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: 85.24 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTT----LRMVagleDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHmS 92
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 VYDNMAfglklrkiPKDEI-DRRVKDAAKILGLEQYLDRKPKAL-----------SGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03244 94 IRSNLD--------PFGEYsDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 161 PLSNLD----AKLRVAMRSEISklhhrlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTP 219
Cdd:cd03244 166 ATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-193 |
3.17e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.72 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK-DRDIAMVFQNYALYPHMSVYDNMAFglkLRKIPKD 109
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHF---WAAIHGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 110 EiDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlRVAMRSEISKLHHRLGTTTI 189
Cdd:TIGR01189 104 A-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLARGGIVL 181
|
....
gi 872564307 190 YVTH 193
Cdd:TIGR01189 182 LTTH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-263 |
3.42e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKDR----DIA 79
Cdd:PRK13536 42 IDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPARARlaraRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHMSVYDNMA-----FGLKLRKIpkDEIDRRVKDAAKilgLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLvfgryFGMSTREI--EAVIPSLLEFAR---LESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETpenifvggF 234
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE--------H 263
|
250 260 270
....*....|....*....|....*....|
gi 872564307 235 IGSPAMNFFRGKLTETDFVID-NAIKIKVT 263
Cdd:PRK13536 264 IGCQVIEIYGGDPHELSSLVKpYARRIEVS 293
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-212 |
3.74e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLM---NDVPPKDRD 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGL---KLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 155 VFLMDEPLSNLDAKlrvamrsEISKLH---HRL---GTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:PRK11288 161 VIAFDEPTSSLSAR-------EIEQLFrviRELraeGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-236 |
4.56e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 35 FVGPSGCGKSTTLRMVAGLEDISKGaFSIDGKLM---------NDVPPKDRDIAMVFQNYALYPhMSVYDNMAFGLKLRK 105
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrsifnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 106 -IPKDEI----DRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKL 180
Cdd:PRK14271 130 lVPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 181 HHRLgtTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENI----FVGGFIG 236
Cdd:PRK14271 210 ADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-224 |
5.66e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYD-NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:PRK11176 341 DIEFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYpHMSVYDNMAFGLKlRKIPKDEIDRRVKDAAK---ILGLEQYLD----RKPKALSGGQRQRVALGRAIVRD 152
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-EQYSREQIEEAARMAYAmdfINKMDNGLDtvigENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 153 AKVFLMDEPLSNLDAKLRVAMRSEISKLH---------HRLGTttiyvthdqteaMTMASRLVVMKDGKIQQIGTPKEVY 223
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQknrtslviaHRLST------------IEKADEILVVEDGEIVERGTHAELL 566
|
.
gi 872564307 224 E 224
Cdd:PRK11176 567 A 567
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-229 |
1.03e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEfIV-FVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmnDVPPKD-RD-----IAMVFQN---YALY 88
Cdd:COG1129 267 VVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSpRDairagIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 89 PHMSVYDNMAFGL--KLRK---IPKDEIDRRVKDAAKILGLE-QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG1129 343 LDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 163 SNLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVyeTPENI 229
Cdd:COG1129 423 RGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA--TEEAI 486
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-213 |
1.18e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDN-NVTAVTDFNLHiqDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPP---KDRDIA 79
Cdd:PRK15439 12 LCARSISKQYSGvEVLKGIDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYPHMSVYDNMAFGLklrkiPKDEID-RRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGL-----PKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 159 DEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-225 |
1.22e-18 |
|
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: 83.73 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR---DIAM 80
Cdd:TIGR03410 1 LEVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILglEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 161 PLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYET 225
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-218 |
1.46e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 87.76 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVT-AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK--LMNdvppkdrdIAM 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiLTN--------ISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNMAFG-------LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 154 KVFLMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGT 218
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-166 |
1.65e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndvPPKDRDIA-------MVfQNYALYPH 90
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ-----PVDAGDIAtrrrvgyMS-QAFSLYGE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 91 MSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:NF033858 354 LTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-167 |
2.56e-18 |
|
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: 82.70 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDiSKGAFS----IDGKLMNDVPPKDRdIAMVFQNYALYP 89
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSgqilFNGQPRKPDQFQKC-VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 HMSVYDNMAFGLKLR---KIPKDEIDRRVKDAA-KILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:cd03234 95 GLTVRETLTYTAILRlprKSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
..
gi 872564307 166 DA 167
Cdd:cd03234 175 DS 176
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-213 |
2.61e-18 |
|
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: 81.59 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENI-YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD-IAMV 81
Cdd:cd03247 1 LSINNVsFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNyalyPHMsvydnmaFGLKLRkipkDEIDRRvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03247 81 NQR----PYL-------FDTTLR----NNLGRR--------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872564307 162 LSNLDAKLRVAMRSEIskLHHRLGTTTIYVTHDQTeAMTMASRLVVMKDGKI 213
Cdd:cd03247 126 TVGLDPITERQLLSLI--FEVLKDKTLIWITHHLT-GIEHMDKILFLENGKI 174
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-230 |
3.18e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHMSVYDNMAFGlklrKIP------ 107
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELVAIG----RYPwhgalg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 108 --KDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLG 185
Cdd:PRK10575 119 rfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 872564307 186 TTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVY--ETPENIF 230
Cdd:PRK10575 199 LTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMrgETLEQIY 245
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-209 |
3.61e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 82.20 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 24 NLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlMNDVPPKDRDIAMVFQNYALYPHMSVYDNMAF---- 99
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMAYLGHLPGLKADLSTLENLHFlcgl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 100 -GLKLRKIPKDeidrrvkdAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlRVAMRSEIS 178
Cdd:PRK13543 110 hGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMI 180
|
170 180 190
....*....|....*....|....*....|.
gi 872564307 179 KLHHRLGTTTIYVTHDQTEAMTMASRLVVMK 209
Cdd:PRK13543 181 SAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-218 |
4.13e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 2 AELKLENIYKIY-DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD-RD-I 78
Cdd:PRK11160 337 VSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHmSVYDNMAFGLKlrkipkDEIDRRVKDAAKILGLEQYLDRKP----------KALSGGQRQRVALGRA 148
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 149 IVRDAKVFLMDEPLSNLDAKlrvaMRSEISKL--HHRLGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGT 218
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAE----TERQILELlaEHAQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGT 556
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
3-222 |
6.00e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 85.33 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:TIGR01192 334 AVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESlrKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYpHMSVYDNMAFGlklrkiPKDEIDRRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVALGRAI 149
Cdd:TIGR01192 414 VFQDAGLF-NRSIRENIRLG------REGATDEEVYEAAKAAAAHDFILKRSNGydtlvgergnrLSGGERQRLAIARAI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRSEISKLhhRLGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNAIDAL--RKNRTTFIIAH-RLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
6.77e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGafSIDgklmndVPPKDRdiaMVF---QNY--------AL- 87
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RIA------RPAGAR---VLFlpqRPYlplgtlreALl 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 88 YPHmsvydnmafglklrkiPKDEI-DRRVKDAAKILGLEQYLDR------KPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG4178 448 YPA----------------TAEAFsDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|....
gi 872564307 161 PLSNLDAKLRVAMrseISKLHHRL-GTTTIYVTH 193
Cdd:COG4178 512 ATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-228 |
8.88e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKL------------------MNDVppKDRDI 78
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrrrsrqvielseqsaaqMRHV--RGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQN--YALYPHMSVYDNMAFGLKLRK-IPKDEI---DRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRD 152
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 153 AKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPEN 228
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-228 |
9.42e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 9.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 23 FNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDiSKGAFSIDGKLMNDVPPKD----RD---------IAM-VFQNYALY 88
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 89 PHMSVydnmafglklrkiPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVR-------DAKVFLMDEP 161
Cdd:PRK03695 94 QPDKT-------------RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 162 LSNLDAKLRVAMRSEISKLhHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPEN 228
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL-TPEN 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
36-218 |
9.60e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.49 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYpHMSVYDNMAFGlklrkipKDEIDR 113
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYG-------RPDASE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 114 R-VKDAAK-------ILGLEQYLD-----RKPKaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK--------LRva 172
Cdd:COG5265 462 EeVEAAARaaqihdfIESLPDGYDtrvgeRGLK-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRteraiqaaLR-- 538
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 872564307 173 mrsEISKLH------HRLGTttiyVTHdqteamtmASRLVVMKDGKIQQIGT 218
Cdd:COG5265 539 ---EVARGRttlviaHRLST----IVD--------ADEILVLEAGRIVERGT 575
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-211 |
2.51e-17 |
|
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: 80.17 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIY------DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSI--DGKLMNDVPPKD 75
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQNYALY--------PHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYL-DRKPKALSGGQRQRVALG 146
Cdd:COG4778 85 REILALRRRTIGYvsqflrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 147 RAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDqTEAM-TMASRLVVMKDG 211
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-227 |
4.88e-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: 79.87 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVtAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGK-----LMNDVPPKDR-- 76
Cdd:TIGR02323 4 LQVSGLSKSYGGGK-GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAERrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 77 ----DIAMVFQNYALYPHMSVYDN-------MAFGL----KLRKIPKDEIDRRVKDAAKIlgleqylDRKPKALSGGQRQ 141
Cdd:TIGR02323 83 lmrtEWGFVHQNPRDGLRMRVSAGanigerlMAIGArhygNIRATAQDWLEEVEIDPTRI-------DDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 142 RVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
....*.
gi 872564307 222 VYETPE 227
Cdd:TIGR02323 236 VLDDPQ 241
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-229 |
1.14e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPpkDRDIA---MV--FQNYALYPHMSV 93
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP--GHQIArmgVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 94 YDNMAF------------GL----KLRKIPKDEIDRrvkdAAKIL---GLEQYLDRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11300 98 IENLLVaqhqqlktglfsGLlktpAFRRAESEALDR----AATWLervGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENI 229
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
1.91e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.61 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENIYKIYdNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---RD 77
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKipKDEIDRRVKDAAKILG-LEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKI--QQIGTPKEVYETPENIFVGG 233
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDALLANEAVRSAYLGG 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-226 |
4.67e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.89 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDgklMNDVPPKD-------- 75
Cdd:PRK11701 7 LSVRGLTKLYGP-RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYR---MRDGQLRDlyalseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 ------RDIAMVFQNYA--LYPHMSVYDN-----MAFGLK----LRKIPKDEIDRRVKDAAKIlgleqylDRKPKALSGG 138
Cdd:PRK11701 83 rrrllrTEWGFVHQHPRdgLRMQVSAGGNigerlMAVGARhygdIRATAGDWLERVEIDAARI-------DDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 139 QRQRVALGRAIVRDAKVFLMDEPLSNLD----AKLRVAMRSeiskLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQ 214
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250
....*....|..
gi 872564307 215 QIGTPKEVYETP 226
Cdd:PRK11701 232 ESGLTDQVLDDP 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
5.53e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLmndvppkdrDIAMVFQ 83
Cdd:COG0488 316 LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYA-LYPHMSVYDNMafglklrkipkdeidRRVKDAAKILGLEQYLDR---------KP-KALSGGQRQRVALGRAIVRD 152
Cdd:COG0488 386 HQEeLDPDKTVLDEL---------------RDGAPGGTEQEVRGYLGRflfsgddafKPvGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 153 AKVFLMDEPLSNLDaklrVAMRSEISKLhhrLGT---TTIYVTHDQTEAMTMASRLVVMKDGKIQ 214
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETLEALEEA---LDDfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-221 |
2.52e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 10 YKIYDNNVTAvtdfnlHIQDKEFIVFVGPSGCGKSTTLRMVAGLedISKGAFSIDGKLMNDVP---PKDRDI-AMVFQNY 85
Cdd:TIGR00955 37 RKHLLKNVSG------VAKPGELLAVMGSSGAGKTTLMNALAFR--SPKGVKGSGSVLLNGMPidaKEMRAIsAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 86 ALYPHMSVYDNMAFGLKLR---KIPKDEIDRRVKDAAKILGLEQYLDRK------PKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 157 LMDEPLSNLDAklrvAMRSEISKLHHRL---GTTTIYVTHDQT-EAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:TIGR00955 189 FCDEPTSGLDS----FMAYSVVQVLKGLaqkGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
3.25e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISkgafSIDGKLMN-----------DVP 72
Cdd:TIGR03269 1 IEVKNLTKKFDG-KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYE----PTSGRIIYhvalcekcgyvERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 73 PKD------------------------------RDIAMVFQ-NYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKI 121
Cdd:TIGR03269 76 SKVgepcpvcggtlepeevdfwnlsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 122 LGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHdQTEAMT- 200
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEd 234
|
250 260
....*....|....*....|....
gi 872564307 201 MASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-194 |
3.86e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLH-----IQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGafSIDGKLmndvppkdrDIAMVFQNYALYPHMSVYDN 96
Cdd:PRK13409 352 DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPEL---------KISYKPQYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 97 mafglkLRKIPKD--------EIDRRvkdaakiLGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK13409 421 ------LRSITDDlgssyyksEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*.
gi 872564307 169 LRVAMRSEISKLHHRLGTTTIYVTHD 194
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-226 |
4.76e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 19 AVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED----ISKGAFSIDGKLMNDVPPKDR------DIAMVFQN--YA 86
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 87 LYPHMSVYDNMAFGLKLRKI-PKDEIDRRVKDAAKILGL---EQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-213 |
8.93e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 21 TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---RDIAMVFQNY---ALYPHMSVY 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 95 DNMA---------FGLKL-RKIPKDEIDRRVKD-AAKILGLEQyldrKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11288 350 DNINisarrhhlrAGCLInNRWEAENADRFIRSlNIKTPSREQ----LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 872564307 164 NLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK11288 426 GID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-229 |
9.46e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 13 YDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRdIAMVFQNYAL---YP 89
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 -------HMSVYDNMAFglkLRkIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK15056 95 vlvedvvMMGRYGHMGW---LR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDqTEAMTMASRLVVMKDGKIQQIGtPKEVYETPENI 229
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDE-GKTMLVSTHN-LGSVTEFCDYTVMVKGTVLASG-PTETTFTAENL 234
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-289 |
9.67e-15 |
|
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: 67.99 E-value: 9.67e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 236 GSPAMNFFRGKLTETDFVIDNA-IKIKVTEGKMkmLREQGYVNKEIVLGIRPEDI 289
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGgVTLPLPEGQV--LALKLYVGKEVILGIRPEHI 53
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
1.28e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.81 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTlrmVAGLEDI-------SKGAFSIDGKLMNDVPPKDRDIAMVFQN--YALYPH 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLT---CAAALGIlpagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAFGLKLRKIPKDeiDRRVKDAAKILGLE---QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK10418 96 HTMHTHARETCLALGKPAD--DATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 168 KLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-195 |
1.60e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.78 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTaVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGlediskgafsidgklmndvppkdrdiamvfq 83
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 nyalyphmsvydnmafglklrKIPKDEIDRRVKDAAKILGLEQyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03221 49 ---------------------ELEPDEGIVTWGSTVKIGYFEQ--------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|..
gi 872564307 164 NLDAKLRVAMRSEISKLHHrlgtTTIYVTHDQ 195
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHDR 127
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-194 |
2.11e-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: 74.44 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFsidgklmnDVPPKDRDIAMVFQNYALYPHMS-VYDNmafglKLR---------K 105
Cdd:COG1245 105 LGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG-----EIKvahkpqyvdL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 106 IPK----------DEIDRR--VKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAM 173
Cdd:COG1245 172 IPKvfkgtvrellEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
170 180
....*....|....*....|.
gi 872564307 174 RSEISKLhHRLGTTTIYVTHD 194
Cdd:COG1245 252 ARLIREL-AEEGKYVLVVEHD 271
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-226 |
3.48e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSidgklmndvppKDRDIAMVFQNyALYPHMSVYDNMAFgl 101
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF-- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 102 klrkipKDEID-RRVKDAAKIL-----------GLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PTZ00243 744 ------FDEEDaARLADAVRVSqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 170 --RVAMRSEISKLHhrlGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PTZ00243 818 geRVVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-193 |
3.80e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.60 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK-DRDIAMVFQNYALYPHMSVYDNMAFglkLRKIPKD 109
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRF---WHADHSD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 110 EidrRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD----AKLRVAMRSeisklHHRLG 185
Cdd:cd03231 104 E---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMAG-----HCARG 175
|
....*...
gi 872564307 186 TTTIYVTH 193
Cdd:cd03231 176 GMVVLTTH 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-222 |
3.90e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.83 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 24 NLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndvppkdrdIAMVFQNyALYPHMSVYDNMAFGLKL 103
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 104 rkipKDEIDRRVKDAAKIL--------GLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL-RVAMR 174
Cdd:TIGR00957 726 ----NEKYYQQVLEACALLpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFE 801
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872564307 175 SEISKLHHRLGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR00957 802 HVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-211 |
5.11e-14 |
|
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: 70.44 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD------ 77
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQNYALYpHMSVYDNMAFGLKLRKipkdeidRRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVALG 146
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 147 RAIVRDAKVFLMDEPLSNLDAKLR-VAMRSEISKLHHRLGTTTIYVTHdQTEAMTMASRLVVMKDG 211
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSdHLMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-213 |
5.87e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 25 LHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDG-----KLMNDvPPKDRDiamvfqnyalyphMSVYDNMAF 99
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivaRLQQD-PPRNVE-------------GTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 100 GLK------------LRKIPKDEIDR----------------------RVKDAAKILGLEQylDRKPKALSGGQRQRVAL 145
Cdd:PRK11147 90 GIEeqaeylkryhdiSHLVETDPSEKnlnelaklqeqldhhnlwqlenRINEVLAQLGLDP--DAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDAklrvamrSEISKLHHRLGT---TTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDI-------ETIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-213 |
1.25e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.83 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 15 NNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGledISKGAFSIDGKLM-NDVPPKD------RDIAMVFQNYAL 87
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHyNGIPYKEfaekypGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 88 YPHMSVYDNMAFGLKLRKipkDEIDRRVkdaakilgleqyldrkpkalSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03233 95 FPTLTVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 872564307 168 KLRVAMRSEISKLHHRLGTTTIyVTHDQT--EAMTMASRLVVMKDGKI 213
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEGRQ 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-219 |
1.35e-13 |
|
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: 68.98 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTAVT-DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIA 79
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLkNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 MVFQNYALYphmsvydnmAFGLKLRKIPKDEI-DRRVKDAAKIL--GLEqyldrkpkaLSGGQRQRVALGRAIVRDAKVF 156
Cdd:cd03369 86 IIPQDPTLF---------SGTIRSNLDPFDEYsDEEIYGALRVSegGLN---------LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564307 157 LMDEPLSNL----DAKLRVAMRSEISK-----LHHRLGTTTIYvthdqteamtmaSRLVVMKDGKIQQIGTP 219
Cdd:cd03369 148 VLDEATASIdyatDALIQKTIREEFTNstiltIAHRLRTIIDY------------DKILVMDAGEVKEYDHP 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-195 |
1.45e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDgklmndVPPKDrdiamvfqnyaLYPHMSVYDNMAfgl 101
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQ-----------FGREASLIDAIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 102 klrkipkdeIDRRVKDAAKILGLEQYLD-----RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSE 176
Cdd:COG2401 108 ---------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170
....*....|....*....
gi 872564307 177 ISKLHHRLGTTTIYVTHDQ 195
Cdd:COG2401 179 LQKLARRAGITLVVATHHY 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-194 |
1.86e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 69.32 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFsidgklmnDVPPKDRDIAMVFQNYALyphmSVYDNMAFGLKLRKIPK----DEI 111
Cdd:cd03236 32 VGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFRGSEL----QNYFTKLLEGDVKVIVKpqyvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 112 DRRVK-----------------DAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMR 174
Cdd:cd03236 100 PKAVKgkvgellkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180
....*....|....*....|
gi 872564307 175 SEISKLhHRLGTTTIYVTHD 194
Cdd:cd03236 180 RLIREL-AEDDNYVLVVEHD 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-194 |
1.88e-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: 71.35 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGLEDISKGafSIDGKLmndvppkdrDIAMVFQnyalYP----HMSVYDNmafglkLRKI 106
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDL---------KISYKPQ----YIspdyDGTVEEF------LRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 107 PKDEIDRRV--KDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRL 184
Cdd:COG1245 426 NTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
170
....*....|
gi 872564307 185 GTTTIYVTHD 194
Cdd:COG1245 506 GKTAMVVDHD 515
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-216 |
2.08e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---RDIAMVFQNY---ALYPHMSV 93
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 94 YDNMAFG--LKLRKI--------PKDEiDRRVKDAAKILGLE-QYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK09700 359 AQNMAISrsLKDGGYkgamglfhEVDE-QRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 163 SNLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQI 216
Cdd:PRK09700 438 RGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-229 |
2.69e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAE--LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLedISKGAFS----IDGKLMNDVPPK 74
Cdd:PRK13549 1 MMEylLEMKNITKTFGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV--YPHGTYEgeiiFEGEELQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 75 DRD---IAMVFQNYALYPHMSVYDNMAFGLKLRK---IPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRA 148
Cdd:PRK13549 78 DTEragIAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 149 IVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKiqQIGT-PKEVYETPE 227
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--HIGTrPAAGMTEDD 234
|
..
gi 872564307 228 NI 229
Cdd:PRK13549 235 II 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-212 |
3.82e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK---DRDIAMVFQNYALYPHMSV 93
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 94 YDNMAFGLKLRKIPKDEIDRRVKDAAKILGlEQYLDRKPKA----LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PRK10982 91 MDNMWLGRYPTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 872564307 170 RVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:PRK10982 170 VNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-230 |
3.85e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 57 SKGAFSIDGKLMNDVPPKD-RDIAMVFQNYALYPHMSVYDNMAFGlklrkiPKDEIDRRVKDAAKILGLEQYLDRKP--- 132
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 133 --------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHdQTEAMTMASR 204
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180 190
....*....|....*....|....*....|.
gi 872564307 205 LVVMKDGK-----IQQIGTPKEVYETPENIF 230
Cdd:PTZ00265 1428 IVVFNNPDrtgsfVQAHGTHEELLSVQDGVY 1458
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-226 |
6.58e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 14 DNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHm 91
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 92 SVYDNMAFGLKlrKIPKDEIDRRVKDAA---KILGLEQYLD----RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK10789 404 TVANNIALGRP--DATQQEIEHVARLASvhdDILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 165 LDAklrvamRSEISKLHH----RLGTTTIYVTHdQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:PRK10789 482 VDG------RTEHQILHNlrqwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-244 |
6.95e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 20 VTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMndvppkdrdIAMVFQNYALYPHMSVydNMAF 99
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR---------IGYVPQKLYLDTTLPL--TVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 100 GLKLRK-IPKDEID---RRVKDAakilgleQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRS 175
Cdd:PRK09544 89 FLRLRPgTKKEDILpalKRVQAG-------HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 176 EISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMkDGKIQQIGTPKEVYETPENIFVGGFIGSPAMNFFR 244
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYR 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
37-193 |
7.60e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 37 GPSGCGKSTTLRMVAGLEDISKGAFSIDGK-LMNDVPPKDRDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKdEIDRRV 115
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQsIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAV-GITELC 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 116 KdaakILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKlHHRLGTTTIYVTH 193
Cdd:PRK13540 113 R----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-222 |
1.25e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEfIVFV-GPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRDIAMVF 82
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 83 ------QNYALYPHMSVYDNMAFGlKLRKIPKDE---IDRRV--KDAAKILglEQY------LDRKPKALSGGQRQRVAL 145
Cdd:COG3845 337 yipedrLGRGLVPDMSVAENLILG-RYRRPPFSRggfLDRKAirAFAEELI--EEFdvrtpgPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDAKlrvAmrseISKLHHRL------GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTP 219
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVG---A----IEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPA 486
|
...
gi 872564307 220 KEV 222
Cdd:COG3845 487 AEA 489
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-281 |
1.27e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGleDISKGAFSidGK-LMNDVPPKD---RDIAMVFQNYALYPHMSVYDNMAFGLKLR-- 104
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAG--RIQGNNFT--GTiLANNRKPTKqilKRTGFVTQDDILYPHLTVRETLVFCSLLRlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 105 -KIPKDEIDRRVKDAAKILGLEQ-----YLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEIS 178
Cdd:PLN03211 171 kSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 179 KLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPENIfvgGFIGSPAMNffrgkltETDFVIDNAI 258
Cdd:PLN03211 251 SLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESV---GFSPSFPMN-------PADFLLDLAN 320
|
250 260
....*....|....*....|...
gi 872564307 259 KIKVTEGKMKmlREQGYVNKEIV 281
Cdd:PLN03211 321 GVCQTDGVSE--REKPNVKQSLV 341
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-227 |
1.63e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVT--AVTDFNLHIQDKEFIVFVGPSGCGKSttlrmvaglediskgafSIDGKLMNDVPPKDRDIAMV 81
Cdd:PLN03232 615 ISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKT-----------------SLISAMLGELSHAETSSVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPHMS------VYDNMAFGLKLRKipkdeidRRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVA 144
Cdd:PLN03232 678 RGSVAYVPQVSwifnatVRENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 145 LGRAIVRDAKVFLMDEPLSNLDAklRVAMRSEISKLHHRL-GTTTIYVThDQTEAMTMASRLVVMKDGKIQQIGTPKEVY 223
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDA--HVAHQVFDSCMKDELkGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
....
gi 872564307 224 ETPE 227
Cdd:PLN03232 828 KSGS 831
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
1.70e-12 |
|
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: 68.31 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISkgafSIDGKLMNDVPP---------K 74
Cdd:TIGR02633 2 LEMKGIVKTFGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG----TWDGEIYWSGSPlkasnirdtE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 75 DRDIAMVFQNYALYPHMSVYDNMAFG----LKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKA-LSGGQRQRVALGRAI 149
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 150 VRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGkiQQIGT 218
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-193 |
3.15e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 5 KLENIYKI--------YDN--NVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSI-DGKLMNDVPP 73
Cdd:PTZ00265 376 KLKDIKKIqfknvrfhYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 K--DRDIAMVFQN-------------YALYP-----HMSVYDN---------------------MAFGLKLRKIPKDEI- 111
Cdd:PTZ00265 456 KwwRSKIGVVSQDpllfsnsiknnikYSLYSlkdleALSNYYNedgndsqenknkrnscrakcaGDLNDMSNTTDSNELi 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 112 ----------DRRVKDAAKILGLEQYLDRKP-----------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PTZ00265 536 emrknyqtikDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260
....*....|....*....|...
gi 872564307 171 VAMRSEISKLHHRLGTTTIYVTH 193
Cdd:PTZ00265 616 YLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-168 |
3.42e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 21 TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNdvppKDRDiamVFQNYALY--------PHMS 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 93 VYDNMAFGLKLRKIPKDEidrRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-166 |
3.59e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENI-YKIYDNNVtaVTDFNLHIQDKEFIVFVGPSGCGKSTTLR-MVAGLEDISkGAFSIDGKLmndvppkdrDIAMvFQ 83
Cdd:PRK11147 322 MENVnYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTKL---------EVAY-FD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NY--ALYPHMSVYDNMAFGlklrkipKDEI-----DRRVkdaakiLG-LEQYL-----DRKP-KALSGGQRQRVALGRAI 149
Cdd:PRK11147 389 QHraELDPEKTVMDNLAEG-------KQEVmvngrPRHV------LGyLQDFLfhpkrAMTPvKALSGGERNRLLLARLF 455
|
170
....*....|....*..
gi 872564307 150 VRDAKVFLMDEPLSNLD 166
Cdd:PRK11147 456 LKPSNLLILDEPTNDLD 472
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-196 |
5.51e-12 |
|
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: 63.33 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIdgklmndvpPKDRDIAMVFQ 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NyalyPHMSVydnmafGLkLRKI---PKDEIdrrvkdaakilgleqyldrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03223 72 R----PYLPL------GT-LREQliyPWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 872564307 161 PLSNLDaklrVAMRSEISKLHHRLGTTTIYVTHDQT 196
Cdd:cd03223 118 ATSALD----EESEDRLYQLLKELGITVISVGHRPS 149
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-193 |
6.42e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 6 LENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPK--DRDIAMVFQ 83
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 84 NYALYPHmSVYDNMAFGlklRKIPKDEIDR-----RVKDAAKIL--GLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK10790 423 DPVVLAD-TFLANVTLG---RDISEEQVWQaletvQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872564307 157 LMDEPLSNLDAKLRVAMRSEISKLH---------HRLGTT----TIYVTH 193
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVRehttlvviaHRLSTIveadTILVLH 548
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-221 |
7.01e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 21 TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAG-LEDISKGAFSIDGKLMNdVPpkdrDIAMVFqnyalypHMSVYDNMAF 99
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAY-VP----QVSWIF-------NATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 100 GLklrkiPKDEidRRVKDAAKILGLEQYLDRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAk 168
Cdd:PLN03130 702 GS-----PFDP--ERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA- 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 169 lRVAMRSEISKLHHRL-GTTTIYVThDQTEAMTMASRLVVMKDGKIQQIGTPKE 221
Cdd:PLN03130 774 -HVGRQVFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-224 |
2.04e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDvpPKDRD-----IAMVFQ----NyaL 87
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRavcprIAYMPQglgkN--L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 88 YPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP------ 161
Cdd:NF033858 90 YPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPttgvdp 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 162 LS-----NLDAKLRvAMRSEISKLhhrlgTTTIYvthdqteaMTMASR---LVVMKDGKIQQIGTPKEVYE 224
Cdd:NF033858 170 LSrrqfwELIDRIR-AERPGMSVL-----VATAY--------MEEAERfdwLVAMDAGRVLATGTPAELLA 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-207 |
3.48e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.43 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 27 IQDKEFIVFVGPSGCGKSTTLRMVAGLEDiskgafsidgklmndvpPKDRDiamvfqnyalyphmsvydnmafglklrki 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLI-----------------PNGDN----------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 107 pkDEIDRrVKDAAKilglEQYLDrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGT 186
Cdd:cd03222 56 --DEWDG-ITPVYK----PQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 872564307 187 TTIYVTHDQTEAMTMASRLVV 207
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-194 |
4.67e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFsidgklmNDVPPKDRDIAMvFQNYALYPHMS-VYDNmafglKLRKIPK----DE 110
Cdd:PRK13409 105 LGPNGIGKTTAVKILSGELIPNLGDY-------EEEPSWDEVLKR-FRGTELQNYFKkLYNG-----EIKVVHKpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 111 IDRRVK-----------------DAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAM 173
Cdd:PRK13409 172 IPKVFKgkvrellkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV 251
|
170 180
....*....|....*....|.
gi 872564307 174 RSEISKLHHrlGTTTIYVTHD 194
Cdd:PRK13409 252 ARLIRELAE--GKYVLVVEHD 270
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-250 |
4.67e-11 |
|
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: 64.55 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAV-TDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndvppkdrdIAMVFQNYALYPHmSVYD 95
Cdd:TIGR01271 438 VTPVlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 96 NMAFGLKLrkipkDEIdrRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:TIGR01271 506 NIIFGLSY-----DEY--RYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 165 LDaklrVAMRSEI--SKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVY-ETPEniFVGGFIGSPAMN 241
Cdd:TIGR01271 579 LD----VVTEKEIfeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEAFD 652
|
250
....*....|....
gi 872564307 242 FFRGK-----LTET 250
Cdd:TIGR01271 653 NFSAErrnsiLTET 666
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-250 |
5.65e-11 |
|
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: 62.57 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKlmndvppkdrdIAMVFQNYALYPHmSVYDNMAFGL 101
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 102 KLrkipkDEIdrRVKDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD-AKL 169
Cdd:cd03291 123 SY-----DEY--RYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 170 RVAMRSEISKLhhRLGTTTIYVThDQTEAMTMASRLVVMKDGKIQQIGTPKEVY-ETPEniFVGGFIGSPAMNFFRGK-- 246
Cdd:cd03291 196 KEIFESCVCKL--MANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQsLRPD--FSSKLMGYDTFDQFSAErr 270
|
....*..
gi 872564307 247 ---LTET 250
Cdd:cd03291 271 nsiLTET 277
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-216 |
2.18e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAM 80
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMsvydnmafgLKLRKIPKDeiDRRVKDAAKILGLEQYLDRKPK-----ALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK10522 402 VFTDFHLFDQL---------LGPEGKPAN--PALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 156 FLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQtEAMTMASRLVVMKDGKIQQI 216
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSEL 530
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-226 |
3.41e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.69 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED----ISKGAFSIDGKLMNDVPPKDR------DIAMVFQN-- 84
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 85 YALYPHMSVYDNMafglkLRKIPKDEIDR--------RVKDAAKIL---GL---EQYLDRKPKALSGGQRQRVALGRAIV 150
Cdd:COG4170 100 SCLDPSAKIGDQL-----IEAIPSWTFKGkwwqrfkwRKKRAIELLhrvGIkdhKDIMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 151 RDAKVFLMDEPLSNLDAklrvAMRSEISKLHHRL----GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETP 226
Cdd:COG4170 175 NQPRLLIADEPTNAMES----TTQAQIFRLLARLnqlqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-218 |
4.01e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIyKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLE--DISKGAFSIDGKLMNDVPPKDRD---I 78
Cdd:CHL00131 8 LEIKNL-HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPHMSVYD--NMAFGLKLRKIPKDEID-----RRVKDAAKILGLEQ-YLDRK-PKALSGGQRQRVALGRAI 149
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 150 VRDAKVFLMDEPLSNLDAKlrvAMRSeISKLHHRLGTTT---IYVTHDQteamtmasRLV---------VMKDGKIQQIG 217
Cdd:CHL00131 167 LLDSELAILDETDSGLDID---ALKI-IAEGINKLMTSEnsiILITHYQ--------RLLdyikpdyvhVMQNGKIIKTG 234
|
.
gi 872564307 218 T 218
Cdd:CHL00131 235 D 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-166 |
4.19e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 15 NNVTAVTDFNLHIQDKEFIV-------FVGPSGCGKSTTLRMVAGLEDISKGAFSIdGKLMndvppkdrDIAMVFQNY-A 86
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLppggivgVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQSRdA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 87 LYPHMSVYDNMAFGLKLRKIPKDEIDRRvkdaakilgleQYLDR----------KPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:TIGR03719 397 LDPNKTVWEEISGGLDIIKLGKREIPSR-----------AYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 872564307 157 LMDEPLSNLD 166
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-167 |
4.79e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 31 EFIVFVGPSGCGKSTTLRMVAGLEDISK----GAFSIDGKLMNDVPPKDR-DIAMVFQNYALYPHMSVYDNMAFGLKLRK 105
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAARCKT 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 106 -------IPKDEIDRRVKD-AAKILGLEQYLDRKP-----KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:TIGR00956 168 pqnrpdgVSREEYAKHIADvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-224 |
6.19e-10 |
|
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: 58.31 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIyKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLED--ISKGAFSIDGKLMNDVPPKDR---DI 78
Cdd:cd03217 1 LEIKDL-HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 79 AMVFQNYALYPhmsvydnmafGLKlrkipkdeidrrvkdaakilgLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03217 80 FLAFQYPPEIP----------GVK---------------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 159 DEPLSNLDA-KLRVAMRsEISKLhHRLGTTTIYVTHDQTEAMTMASRLV-VMKDGKIQQIGtPKEVYE 224
Cdd:cd03217 129 DEPDSGLDIdALRLVAE-VINKL-REEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSG-DKELAL 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-227 |
6.66e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 18 TAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDIS-----KGAFSIDGK-LMNDVPPKDR-----DIAMVFQN-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGEsLLHASEQTLRgvrgnKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 85 YALYPHMSVYDNMAFGLKL-----RKIPKDEI----DR-RVKDAAKILGleQYldrkPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLhrgmrREAARGEIlnclDRvGIRQAAKRLT--DY----PHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 155 VFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYETPE 227
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
1.00e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNvTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMvaglediskgafsidgkLMNDVPPKD-------- 75
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRT-----------------LVGELEPDSgtvkwsen 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 -------RDIAMVFQNyalypHMSVYDNMAfglKLRKiPKDEiDRRVKDA-AKILGLEQYLDRKPKALSGGQRQRVALGR 147
Cdd:PRK15064 382 anigyyaQDHAYDFEN-----DLTLFDWMS---QWRQ-EGDD-EQAVRGTlGRLLFSQDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 148 AIVRDAKVFLMDEPLSNLDaklrvaMRSeISKLHHRLGT---TTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMD------MES-IESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-229 |
2.11e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAG--LEDISKGAFSIDGKL-MNDVPPKDRDIAMVFQNYALYPHMSvydNMA 98
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVtLNGEPLAAIDAPRLARLRAVLPQAA---QPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 99 FGLKLRKI-------------PKDEIDRRVKDAAKIL-GLEQYLDRKPKALSGGQRQRVALGRAI---------VRDAKV 155
Cdd:PRK13547 96 FAFSAREIvllgrypharragALTHRDGEIAWQALALaGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 156 FLMDEPLSNLDAKLRVAMRSEISKLHH--RLGTTTIyvTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYeTPENI 229
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAI--VHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAHI 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-213 |
2.14e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 23 FNLHiqDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD---RDIAMVFQNY---ALYPHMSVYDN 96
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 97 MAFgLKLRKIPKDEIdrRVKDAAKILGLEQYLD----RKPKA------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK10762 351 MSL-TALRYFSRAGG--SLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872564307 167 aklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK10762 428 ----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-170 |
4.48e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 13 YDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDrdIAMVFQNYALYPHMS 92
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 93 VYDNMAFGLKLRKIPKdeidrRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK13541 87 VFENLKFWSEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-213 |
1.51e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDR-DIAMVF-----QNYALYPHMS--- 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPlaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 93 -----VYDNMAFGLklrkipkdeidRRVKDAAKilgLEQY----------LDRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:PRK15439 361 nvcalTHNRRGFWI-----------KPARENAV---LERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 158 MDEPLSNLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKI 213
Cdd:PRK15439 427 VDEPTRGVD----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-211 |
2.30e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 37 GPSGCGKSTTLRMVAglEDISKGAFSIDGKLMNDvPPKD----RDIAMVFQNYALYPHMSVYDNMAFGLKLR---KIPKD 109
Cdd:TIGR00956 796 GASGAGKTTLLNVLA--ERVTTGVITGGDRLVNG-RPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 110 EIDRRVKDAAKILGLEQYLDrkpkALSG--------GQRQRVALGRAIVRDAKVFL-MDEPLSNLDAKLRVAmrseISKL 180
Cdd:TIGR00956 873 EKMEYVEEVIKLLEMESYAD----AVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS----ICKL 944
|
170 180 190
....*....|....*....|....*....|....*
gi 872564307 181 HHRLGTT--TIYVTHDQTEAMTMAS--RLVVMKDG 211
Cdd:TIGR00956 945 MRKLADHgqAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
57-214 |
3.23e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 57 SKGAFSIDGKLMNDVPPKD---RDIAMVFQN---YALYPHMSVYDNMAFGLkLRKIPKDeidRRVKDAAKILGLEQYLDR 130
Cdd:PRK13549 316 WEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITLAA-LDRFTGG---SRIDDAAELKTILESIQR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 131 -KPKA---------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTE 197
Cdd:PRK13549 392 lKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPE 467
|
170
....*....|....*..
gi 872564307 198 AMTMASRLVVMKDGKIQ 214
Cdd:PRK13549 468 VLGLSDRVLVMHEGKLK 484
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-194 |
4.54e-08 |
|
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: 54.56 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 33 IVFVGPSGCGKSTTLRMVAGLEDiskgafSIDGKLMndvPPKDRDIAMVFQNYALYPHMSVYDNMAFGL--------KLR 104
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDK------DFNGEAR---PQPGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 105 KI------PKDEIDRRVK---------DAAKILGLEQYLDRKPKAL------------SGGQRQRVALGRAIVRDAKVFL 157
Cdd:TIGR03719 105 EIsakyaePDADFDKLAAeqaelqeiiDAADAWDLDSQLEIAMDALrcppwdadvtklSGGERRRVALCRLLLSKPDMLL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 872564307 158 MDEPLSNLDAKlrvamrsEISKLHHRLGT---TTIYVTHD 194
Cdd:TIGR03719 185 LDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-230 |
4.84e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTAV-TDFNLHIQDKEFIVFVGPSGCGKSTT----LRMVagleDISKGAFSIDGKLMNDVPPKD-- 75
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPLHTlr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 76 RDIAMVFQNYALYPhmsvyDNMAFGLKLRKIPKD-------EIdRRVKDAAKIL--GLEQYLDRKPKALSGGQRQRVALG 146
Cdd:cd03288 95 SRLSIILQDPILFS-----GSIRFNLDPECKCTDdrlwealEI-AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 147 RAIVRDAKVFLMDEPLSNLD-AKLRVAMRSEISKLHHRlgtTTIYVTHDQTEAMTmASRLVVMKDGKIQQIGTPKEVYET 225
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
....*
gi 872564307 226 PENIF 230
Cdd:cd03288 245 EDGVF 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-228 |
6.91e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNnVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKDRD---IAM 80
Cdd:PRK10762 5 LQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 81 VFQNYALYPHMSVYDNM--------AFGLKLRKIPKDEIDRRVKDaakiLGLEQYLDRKPKALSGGQRQRVALGRAIVRD 152
Cdd:PRK10762 84 IHQELNLIPQLTIAENIflgrefvnRFGRIDWKKMYAEADKLLAR----LNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 153 AKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGkiQQIGTpKEVYETPEN 228
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG--QFIAE-REVADLTED 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-222 |
1.31e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYphmsvydnmAF 99
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF---------SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 100 GLKLRKIPKDEI-DRRVKDAAKILGLEQYLDRKP-----------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:TIGR00957 1375 SLRMNLDPFSQYsDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 168 KLRVAMRSEIS---------KLHHRLGTTTIYvthdqteamtmaSRLVVMKDGKIQQIGTPKEV 222
Cdd:TIGR00957 1455 ETDNLIQSTIRtqfedctvlTIAHRLNTIMDY------------TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-183 |
2.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLEN-IYKIYDNNVTAVTDfnLHIQDKEFIVFVGPSGCGKSTTLRMVAG------------LEDISKGAFSIDGKL 67
Cdd:PRK10938 1 MSSLQISQgTFRLSDTKTLQLPS--LTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqFSHITRLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 68 MNDvPPKDRDIAMvfqnyaLYPhmsvyDNMAFGLKLRKIPKDEIDR--RVKDAAKILGLEQYLDRKPKALSGGQRQRVAL 145
Cdd:PRK10938 79 VSD-EWQRNNTDM------LSP-----GEDDTGRTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHR 183
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-205 |
4.56e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 30 KEFIVFVGPSGCGKSTTLRMVAG-LEDISKGAFSIDGklmndvppkdrdiamvfqnyalyphmsvydnmafglklrkipk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 109 deidRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEIS-----KLHHR 183
Cdd:smart00382 39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|..
gi 872564307 184 LGTTTIYVTHDQTEAMTMASRL 205
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-166 |
5.85e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 33 IVFV-GPSGCGKSTTLRMVAGLEDISKGAFSIdGKLMndvppkdrDIAMVFQNY-ALYPHMSVYDNMAFGLKLRKIPKDE 110
Cdd:PRK11819 352 IVGIiGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNRE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564307 111 IDRRvkdaakilgleQYLDR----------KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK11819 423 IPSR-----------AYVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-214 |
6.19e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENI--YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL-EDISKGAFSIDGKLMNDVPPKD---RD 77
Cdd:TIGR02633 258 LEARNLtcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 78 IAMVFQN---YALYPHMSVYDNMAFGLKLRKIPKDEIDrrvkDAAKILGLEQYLDR-KPKA---------LSGGQRQRVA 144
Cdd:TIGR02633 338 IAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRID----AAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQKAV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564307 145 LGRAIVRDAKVFLMDEPLSNLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKDGKIQ 214
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVD----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
36-215 |
7.59e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDIsKGAFSIDGKLMNDVPPKDRDIAmvfqnYALYPHMSVYDNMAFGLKLRKIPKDEiDRRV 115
Cdd:cd03289 36 LGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKA-----FGVIPQKVFIFSGTFRKNLDPYGKWS-DEEI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 116 KDAAKILGLEQYLDRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRseiSKLHHRL 184
Cdd:cd03289 109 WKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAF 185
|
170 180 190
....*....|....*....|....*....|.
gi 872564307 185 GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQ 215
Cdd:cd03289 186 ADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-222 |
9.33e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALY---------PHMSVYDNMAFGLKLR 104
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFsgtvrfnidPFSEHNDADLWEALER 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 105 KIPKDEIDRRVkdaakiLGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKlhhRL 184
Cdd:PLN03232 1348 AHIKDVIDRNP------FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE---EF 1418
|
170 180 190
....*....|....*....|....*....|....*...
gi 872564307 185 GTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-167 |
9.69e-07 |
|
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: 48.78 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDIS--KGAFSIDGKlmndvpPKD----RDIAMVFQNYALYPHMSVYDNMAFGLKLRkipkd 109
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTAGviTGEILINGR------PLDknfqRSTGYVEQQDVHSPNLTVREALRFSALLR----- 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 872564307 110 eidrrvkdaakilgleqyldrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03232 108 ------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-230 |
1.35e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 27 IQDKEFIVFVGPSGCGKSTTL----RMVagleDISKGAFSIDGKLMNDVPPKD--RDIAMVFQNYALYPHmSVYDNM--- 97
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVdpf 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 98 -------------AFGLKLRKIPKDE-IDRRVKDaakilGLEQYldrkpkalSGGQRQRVALGRAIV-RDAKVFLMDEPL 162
Cdd:PTZ00243 1408 leassaevwaaleLVGLRERVASESEgIDSRVLE-----GGSNY--------SVGQRQLMCMARALLkKGSGFILMDEAT 1474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872564307 163 SN----LDAKLRVAMRSEISK-----LHHRLGTTTIYvthdqteamtmaSRLVVMKDGKIQQIGTPKEVYETPENIF 230
Cdd:PTZ00243 1475 ANidpaLDRQIQATVMSAFSAytvitIAHRLHTVAQY------------DKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-193 |
2.94e-06 |
|
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: 48.98 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENIYKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSI--DGKLMNdVPPKDRDIAMV 81
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFY-VPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 82 FQNYALYPhMSVYDNMAFGLklrkipkdeidrRVKDAAKIL---GLEQYLDRK---------PKALSGGQRQRVALGRAI 149
Cdd:TIGR00954 531 LRDQIIYP-DSSEDMKRRGL------------SDKDLEQILdnvQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 872564307 150 VRDAKVFLMDEPLSnldaKLRVAMRSEISKLHHRLGTTTIYVTH 193
Cdd:TIGR00954 598 YHKPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-194 |
4.48e-06 |
|
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: 46.83 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 3 ELKLENIYKIYDNNVTavtDFnlhiqDKEFIVFVGPSGCGKSTTLrmvagleDISKGAFSIDGKLMNDVPPKDRDIA--- 79
Cdd:cd03240 3 KLSIRNIRSFHERSEI---EF-----FSPLTLIVGQNGAGKTTII-------EALKYALTGELPPNSKGGAHDPKLIreg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 80 -------MVFQN-----YALYPHMSVYDNMAFglklrkIPKDEIDrrvkdaaKILGLEqyldrkPKALSGGQRQ------ 141
Cdd:cd03240 68 evraqvkLAFENangkkYTITRSLAILENVIF------CHQGESN-------WPLLDM------RGRCSGGEKVlaslii 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 872564307 142 RVALGRAIVRDAKVFLMDEPLSNLDA-KLRVAMRSEISKLHHRLGTTTIYVTHD 194
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
282-357 |
9.27e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 42.99 E-value: 9.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564307 282 LGIRPEDIHdellflEASQSTAFTTKIEVAELLGAESILYMKLGD-QDFAARVDARHT--FSPSDQIKLAFDINKAHFF 357
Cdd:pfam08402 1 LAIRPEKIR------LAAAANGLSGTVTDVEYLGDHTRYHVELAGgEELVVRVPNAHArpPAPGDRVGLGWDPEDAHVL 73
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-167 |
1.06e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDIS---KGAFSIDGKLMNDVPPKdRDIAMVFQNYALYPHMSV 93
Cdd:PLN03140 178 LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPR-KTSAYISQNDVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 94 YDNMAF-----GLKLRKIPKDEIDRRVKDAA-----------------------------KILGLE-----QYLDRKPKA 134
Cdd:PLN03140 257 KETLDFsarcqGVGTRYDLLSELARREKDAGifpeaevdlfmkatamegvksslitdytlKILGLDickdtIVGDEMIRG 336
|
170 180 190
....*....|....*....|....*....|...
gi 872564307 135 LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDS 369
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-219 |
2.13e-05 |
|
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: 46.33 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 23 FNLHIQDKEfIVF-VGPSGCGKSTTLRMVAGLEDISKGAFSIDGKLmndVPPKDRD-----IAMVFQNYALYPHMSVYDN 96
Cdd:COG4615 351 IDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 97 MAfglklrkipkdeidrrvkDAAKILGLEQYL--DRKPK---------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:COG4615 427 EA------------------DPARARELLERLelDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 872564307 166 DAKLR-VAMRSEISKLhHRLGTTTIYVTHDQTeAMTMASRLVVMKDGKIQQIGTP 219
Cdd:COG4615 489 DPEFRrVFYTELLPEL-KARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGP 541
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-235 |
2.25e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 1 MAELKLENI---YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGledISKGAFSIDGKLM--NDV---- 71
Cdd:PRK15093 1 MPLLDIRNLtieFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMrfDDIdllr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 72 -PPKDR------DIAMVFQ--NYALYPHMSVYDNMA---------------FGLKLRKipKDEIDRRV--KDAAKILGle 125
Cdd:PRK15093 78 lSPRERrklvghNVSMIFQepQSCLDPSERVGRQLMqnipgwtykgrwwqrFGWRKRR--AIELLHRVgiKDHKDAMR-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 126 qyldRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEAMTMASRL 205
Cdd:PRK15093 154 ----SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
250 260 270
....*....|....*....|....*....|
gi 872564307 206 VVMKDGKIQQIGTPKEVYETPENIFVGGFI 235
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-222 |
2.87e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 114 RVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLhHRLGTTTIYVTH 193
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQ 202
|
90 100
....*....|....*....|....*....
gi 872564307 194 DQTEAMTMASRLVVMKDGKIQQIGTPKEV 222
Cdd:NF000106 203 YMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
91-229 |
3.05e-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: 46.16 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 91 MSVYDNMAF--GLKL---RKIPKDEIDRRVKDAAKIL---GLEQ-YLDRKPKALSGGQRQRVALGRAI------VrdakV 155
Cdd:TIGR00630 436 LSIREAHEFfnQLTLtpeEKKIAEEVLKEIRERLGFLidvGLDYlSLSRAAGTLSGGEAQRIRLATQIgsgltgV----L 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 156 FLMDEPLSNLDAK--LRVamrseISKLHH--RLGTTTIYVTHDQtEAMTMASRLVVM------KDGKIQQIGTPKEVYET 225
Cdd:TIGR00630 512 YVLDEPSIGLHQRdnRRL-----INTLKRlrDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEILAN 585
|
....
gi 872564307 226 PENI 229
Cdd:TIGR00630 586 PDSL 589
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-215 |
1.24e-04 |
|
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: 44.13 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 15 NNVTA--VTDFNLHIQDKEFIV-------FVGPSGCGKSTTLRMVAGLEDiSKGAFSIDG------------KLMNDVPP 73
Cdd:TIGR01271 1221 QGLTAkyTEAGRAVLQDLSFSVeggqrvgLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswnsvtlqtwrKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 74 KDRDIAMVFQNyALYPHMSVYDNMAF------GLK--LRKIPkDEIDRRVKDAAKILgleqyldrkpkalSGGQRQRVAL 145
Cdd:TIGR01271 1300 KVFIFSGTFRK-NLDPYEQWSDEEIWkvaeevGLKsvIEQFP-DKLDFVLVDGGYVL-------------SNGHKQLMCL 1364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564307 146 GRAIVRDAKVFLMDEPLSNLD-AKLRVAMRSeiskLHHRLGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQ 215
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDpVTLQIIRKT----LKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-194 |
1.71e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGLEDISKG------AFSIdGKLMNDvPPKDRDiAMVFQNY--ALYPHMSVYD-----NMAFGL- 101
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEGearpapGIKV-GYLPQE-PQLDPE-KTVRENVeeGVAEVKAALDrfneiYAAYAEp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 102 ------------KLRKI--PKD--EIDRRVKDAAKILGLEQYlDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK11819 116 dadfdalaaeqgELQEIidAADawDLDSQLEIAMDALRCPPW-DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL 194
|
170 180 190
....*....|....*....|....*....|..
gi 872564307 166 DAKlrvamrsEISKLHHRLGT---TTIYVTHD 194
Cdd:PRK11819 195 DAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-213 |
2.78e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 121 ILGLEQYLDRKP-KALSGGQrQRVAL-GRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRLGTTTIYVTHDQTEA 198
Cdd:PRK10938 387 ILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
90
....*....|....*.
gi 872564307 199 -MTMASRLVVMKDGKI 213
Cdd:PRK10938 466 pACITHRLEFVPDGDI 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-212 |
3.02e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 17 VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGL------EdiskGAFSIDGKLM-----NDvpPKDRDIAMVFQNY 85
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCrfkdiRD--SEALGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 86 ALYPHMSVYDNMAFGLKLRK---IPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:NF040905 88 ALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 872564307 163 SNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGK 212
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
36-175 |
4.51e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 36 VGPSGCGKSTTLRMVAGlediSKGAFSIDGKL-MNDVPPKDRDIAMVF----QNYALYPHMSVYDNMAFGLKLR---KIP 107
Cdd:PLN03140 912 MGVSGAGKTTLMDVLAG----RKTGGYIEGDIrISGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSAFLRlpkEVS 987
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564307 108 KDEIDRRVKDAAKILGLEQYLDR-----KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK-LRVAMRS 175
Cdd:PLN03140 988 KEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRT 1061
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
10-196 |
5.19e-04 |
|
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: 40.38 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 10 YKIYDNNVTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLrmvagLEDISKGAfsidGKLMNDVPPKDRDIAMVFQNyalyp 89
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLYASG----KARLISFLPKFSRNKLIFID----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 90 hmsvydnmafglKLRKIpkdeIDrrvkdaakiLGLEqY--LDRKPKALSGGQRQRVALGRAIVRDAK--VFLMDEPLSNL 165
Cdd:cd03238 67 ------------QLQFL----ID---------VGLG-YltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|.
gi 872564307 166 DAKLRVAMRSEISKLHHrLGTTTIYVTHDQT 196
Cdd:cd03238 121 HQQDINQLLEVIKGLID-LGNTVILIEHNLD 150
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-232 |
6.20e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 23 FNLHIQDKEFIVfvGPSGCGKSTTLRMVAGLEDISKGAFSIDGklmndvppkdrdiamvfqnyalyphmsvYDNMAFGLK 102
Cdd:PLN03130 1260 FEISPSEKVGIV--GRTGAGKSSMLNALFRIVELERGRILIDG----------------------------CDISKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 103 -LRK----IPK-------------------------DEIDR-RVKDAAK--ILGLEQYLDRKPKALSGGQRQRVALGRAI 149
Cdd:PLN03130 1310 dLRKvlgiIPQapvlfsgtvrfnldpfnehndadlwESLERaHLKDVIRrnSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 150 VRDAKVFLMDEPLSNL----DAKLRVAMRSEISK-----LHHRLGTttiyvthdqteaMTMASRLVVMKDGKIQQIGTPK 220
Cdd:PLN03130 1390 LRRSKILVLDEATAAVdvrtDALIQKTIREEFKSctmliIAHRLNT------------IIDCDRILVLDAGRVVEFDTPE 1457
|
250
....*....|..
gi 872564307 221 EVYETPENIFVG 232
Cdd:PLN03130 1458 NLLSNEGSAFSK 1469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-254 |
6.41e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 4 LKLENI---YKIYDNN----------------VTAVTDFNLHIQDKEFIVFVGPSGCGKSTTLRMVAGLEDISKGAFSID 64
Cdd:PRK13546 5 VNIKNVtkeYRIYRTNkermkdalipkhknktFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 65 GklmndvppkdrDIAMVFQNYALYPHMSVYDNMAFGLKLRKIPKDEIDRRVKDAAKILGLEQYLDRKPKALSGGQRQRVA 144
Cdd:PRK13546 85 G-----------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 145 LGRAIVRDAKVFLMDEPLSNLDAKLRVAMRSEISKLHHRlGTTTIYVTHDQTEAMTMASRLVVMKDGKIQQIGTPKEVYE 224
Cdd:PRK13546 154 FSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLP 232
|
250 260 270
....*....|....*....|....*....|..
gi 872564307 225 TPENiFVGGF--IGSPAMNFFRGKLTETDFVI 254
Cdd:PRK13546 233 KYEA-FLNDFkkKSKAEQKEFRNKLDESRFVI 263
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-221 |
1.72e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 134 ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVAMRSEISKLHHRL---GTTTIYVTHDQTEAMTMASRLVVMKD 210
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID----VGAKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILVMSN 466
|
90
....*....|.
gi 872564307 211 GKIQQIGTPKE 221
Cdd:PRK10982 467 GLVAGIVDTKT 477
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-166 |
2.40e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|....*..
gi 872564307 130 RKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
32-118 |
9.83e-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: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564307 32 FIVFVGPSGCGKSTTLRmvaglediskgafsidgKLMNDVPPkDRDIAMVFqnyalYPHMSVYD-----NMAFGLKLRKI 106
Cdd:COG3267 45 FVVLTGEVGTGKTTLLR-----------------RLLERLPD-DVKVAYIP-----NPQLSPAEllraiADELGLEPKGA 101
|
90
....*....|..
gi 872564307 107 PKDEIDRRVKDA 118
Cdd:COG3267 102 SKADLLRQLQEF 113
|
|
| |
