|
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: 592.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIA 80
Cdd:COG3839 1 MASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 161 EPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPP 240
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 241 MNFIPVRLARQDGRLlalldsgqARCELPLGEAADALEGREIILGIRPEQIALGAADGNGLPairAEVQVTEPTGPDLLV 320
Cdd:COG3839 239 MNLLPGTVEGGGVRL--------GGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLE---ATVEVVEPLGSETLV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 504402764 321 FVTLNQTKVCCRLAPDVACRVGDTLNLQFDPARVLLFDAANGERL 365
Cdd:COG3839 308 HVRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-366 |
2.25e-177 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 497.44 E-value: 2.25e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIA 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 161 EPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPP 240
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 241 MNFIPVRLARQDGRLLAlldsgQARCELPLGEAADALEGREIILGIRPEQIALGAADGnglpAIRAEVQVTEPTGPDLLV 320
Cdd:PRK11650 240 MNLLDGRVSADGAAFEL-----AGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEG----GVPLTVDTVELLGADNLA 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 504402764 321 FVTLNQTKVCCRLAPDVACRVGDTLNLQFDPARVLLFDAANGERLH 366
Cdd:PRK11650 311 HGRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRIE 356
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-359 |
4.87e-153 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 435.30 E-value: 4.87e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIA 80
Cdd:COG3842 3 MPALELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 161 EPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSpp 240
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 241 MNFIPVRLARQDGRLLALLDSgqarcELPLGEAADALEGREIILGIRPEQIALGAADGNGlpAIRAEVQVTEPTGPDLLV 320
Cdd:COG3842 239 ANLLPGTVLGDEGGGVRTGGR-----TLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPEN--GLPGTVEDVVFLGSHVRY 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504402764 321 FVTLNQ-TKVCCRLAPDVAC--RVGDTLNLQFDPARVLLFDA 359
Cdd:COG3842 312 RVRLGDgQELVVRVPNRAALplEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-366 |
8.02e-133 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 384.77 E-value: 8.02e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGsglpDTL--KDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD 78
Cdd:PRK11000 1 MASVTLRNVTKAYG----DVVisKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGS 238
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 239 PPMNFIPVR-LARQDGRLLALLDSGQaRCELPLgEAADALEGREIILGIRPEQIaLGAADGNglPAIRAEVQVTEPTGPD 317
Cdd:PRK11000 237 PKMNFLPVKvTATAIEQVQVELPNRQ-QVWLPV-EGRGVQVGANMSLGIRPEHL-LPSDIAD--VTLEGEVQVVEQLGNE 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 318 LLVFVTL---NQTKVCCRlaPDVA-CRVGDTLNLQFDPARVLLF--DAANGERLH 366
Cdd:PRK11000 312 TQIHIQIpaiRQNLVYRQ--NDVVlVEEGATFAIGLPPERCHLFreDGTACRRLH 364
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-218 |
1.81e-127 |
|
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: 365.04 E-value: 1.81e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-356 |
4.04e-122 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 356.76 E-value: 4.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDV-SGMSPKDRDIAM 81
Cdd:COG1118 2 SIEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDE 161
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 162 PLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGspPM 241
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 242 NFIPVRlaRQDGRLLALLDSGQARCELPLGEAAdalegreiiLGIRPEQIALgAADGNGLPAIRAEVQVTEPTGPDLLVF 321
Cdd:COG1118 238 NVLRGR--VIGGQLEADGLTLPVAEPLPDGPAV---------AGVRPHDIEV-SREPEGENTFPATVARVSELGPEVRVE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504402764 322 VTLNQTK---VCCRLAPDVACR----VGDTLNLQFDPARVLL 356
Cdd:COG1118 306 LKLEDGEgqpLEAEVTKEAWAElglaPGDPVYLRPRPARVFL 347
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
5.21e-111 |
|
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: 323.32 E-value: 5.21e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-357 |
1.57e-110 |
|
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: 327.38 E-value: 1.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIA 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAF--TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEevaRVAKLLQIEHLL--ARK-PAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:TIGR03265 80 IVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAE---RVAELLDLVGLPgsERKyPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 238 SppMNFIPVRlARQDGRLLAllDSGQARCELPLGEAADALEgreiiLGIRPEQIALGAADG--NGLPAI----------- 304
Cdd:TIGR03265 237 E--VNWLPGT-RGGGSRARV--GGLTLACAPGLAQPGASVR-----LAVRPEDIRVSPAGNaaNLLLARvedmeflgafy 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 305 RAEVQVTEPTGPDLLVFVTLNQtkvccrlAPDVACRVGDTLNLQFDPARVLLF 357
Cdd:TIGR03265 307 RLRLRLEGLPGQALVADVSASE-------VERLGIRAGQPIWIELPAERLRAF 352
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-237 |
1.82e-108 |
|
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: 317.64 E-value: 1.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-237 |
1.24e-106 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 318.43 E-value: 1.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-371 |
3.31e-96 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 290.85 E-value: 3.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPpmNF 243
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 244 IPVRLARQDgrllalLDSGQARCELPLGEAADALEGrEIILGIRPEQIALGAadgNGLPAIRAEVQVTEPTGPDLLVFVT 323
Cdd:PRK11432 243 FPATLSGDY------VDIYGYRLPRPAAFAFNLPDG-ECTVGVRPEAITLSE---QGEESQRCTIKHVAYMGPQYEVTVD 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 504402764 324 LNqtkvccrlapdvacrvGDTLNLQFDPARvllFDAANGER--LHLASTG 371
Cdd:PRK11432 313 WH----------------GQELLLQVNATQ---LQPDLGEHyyLEIHPYG 343
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-238 |
7.53e-93 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 278.07 E-value: 7.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMV 82
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRK----LPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGS 238
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-325 |
1.44e-92 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 281.19 E-value: 1.44e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:NF040840 2 IRIENLSKDWKEF---KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:NF040840 79 QNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPpmNF 243
Cdd:NF040840 159 SALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 244 IPVRlARQDGRlLALLDSGQARCELPLgeaadALEGReIILGIRPEQIALGAA--DGNGLPAIRAEVQVTEPTGPdlLVF 321
Cdd:NF040840 237 IEGV-AEKGGE-GTILDTGNIKIELPE-----EKKGK-VRIGIRPEDITISTEkvKTSARNEFKGKVEEIEDLGP--LVK 306
|
....
gi 504402764 322 VTLN 325
Cdd:NF040840 307 LTLD 310
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-237 |
9.77e-92 |
|
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: 275.37 E-value: 9.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-237 |
2.91e-90 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 271.67 E-value: 2.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:TIGR00968 1 IEIANISKRFGSF--QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-324 |
2.77e-89 |
|
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: 272.06 E-value: 2.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 36 LVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEE 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 116 VARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHD 195
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 196 QIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPPMnFIPVRLARQDGRLlaLLDSGQARcELPLGEAAD 275
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV-FEATVIERKSEQV--VLAGVEGR-RCDIYTDVP 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 504402764 276 ALEGREIILGIRPEQIAL-GAADGNGLPAIRAEVQVTEPTGPDLLVFVTL 324
Cdd:TIGR01187 237 VEKDQPLHVVLRPEKIVIeEEDEANSSNAIIGHVIDITYLGMTLEVHVRL 286
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-237 |
3.71e-88 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 270.42 E-value: 3.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMV 82
Cdd:PRK10851 2 SIEIANIKKSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKI---RKLPQ-AAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVlprRERPNaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-293 |
5.06e-85 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 263.23 E-value: 5.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYgSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:PRK11607 20 LEIRNLTKSF-DGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPPMnF 243
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV-F 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 504402764 244 IPVRLARQDGRLlaLLDSGQARCELPLGEAADALEGREIILGIRPEQIAL 293
Cdd:PRK11607 257 EGVLKERQEDGL--VIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIML 304
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
1.21e-84 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 258.10 E-value: 1.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPkdrD 78
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-282 |
6.65e-81 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 250.01 E-value: 6.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:COG1125 3 EFENVTKRYPDGTV-AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEevaRVAKLLQI-----EHLLARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRA---RVDELLELvgldpEEYRDRYPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 504402764 238 SppmNFIPVRLARQDGRLLALLDSGQARCELPLGEAADALEGREI 282
Cdd:COG1125 239 A---DRGLRRLSLLRVEDLMLPEPPTVSPDASLREALSLMLERGV 280
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
4.18e-79 |
|
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: 242.38 E-value: 4.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPkdrDIAM 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDE 161
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504402764 162 PLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVM 209
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-239 |
4.34e-78 |
|
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: 240.67 E-value: 4.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKL--LQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSP 239
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
4.39e-78 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 239.95 E-value: 4.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MAT-LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR 77
Cdd:COG1136 1 MSPlLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 D------IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALA 151
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQiEAMTLGDKVAVMKDGII 214
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-236 |
2.53e-75 |
|
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: 234.46 E-value: 2.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD------RDIAMVFQSYALYPTMSV 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 95 RENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEM 174
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 175 RTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFI 236
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-214 |
1.00e-73 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 228.53 E-value: 1.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD--- 78
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 ---IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQiEAMTLGDKVAVMKDGII 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-212 |
1.49e-69 |
|
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: 216.28 E-value: 1.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMS----PKDRDI 79
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEFGlkirklpqaaideevarvakllqiehllarkpaqLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-218 |
1.14e-66 |
|
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: 210.23 E-value: 1.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIK---DGEFLILVGPSGCGKSTLMNCIAGLEQITGGAI------LIDEQDVSGMSPKDRDIAMVFQSYALYPT 91
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 92 MSVRENIEFGLKirKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLR 171
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504402764 172 VEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-236 |
6.80e-66 |
|
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: 209.07 E-value: 6.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsglpDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD--- 78
Cdd:COG1127 6 IEVRNLTKSFG----DRvvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 --IAMVFQSYALYPTMSVRENIEFGLKIR-KLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:COG1127 82 rrIGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 156 IYLFDEPLSNLD---AKLRVEMrteMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPaNQFV 232
Cdd:COG1127 162 ILLYDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWV 237
|
....
gi 504402764 233 ASFI 236
Cdd:COG1127 238 RQFL 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-237 |
1.32e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 208.31 E-value: 1.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsglpDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVsGMSPKD----- 76
Cdd:COG1126 2 IEIENLHKSFG----DLevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDinklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 RDIAMVFQSYALYPTMSVRENIEFGL-KIRKLPQAAIdEEVARvaKLLQ---IEHLLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEA-EERAM--ELLErvgLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 153 RPKIYLFDEPLSNLDAklrvEMRTE-MKLMHQ--RLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPAN 229
Cdd:COG1126 154 EPKVMLFDEPTSALDP----ELVGEvLDVMRDlaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
....*...
gi 504402764 230 QFVASFIG 237
Cdd:COG1126 230 ERTRAFLS 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-212 |
1.88e-65 |
|
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: 206.93 E-value: 1.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQsyalYP-----TMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-293 |
2.54e-65 |
|
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: 211.50 E-value: 2.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDE---QDVSG---MSPKDRDIAMVFQSYALYPTMSVRE 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 97 NIEFGLKIRKLPQAAIDeeVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRT 176
Cdd:COG4148 97 NLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 177 EMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPAnqFVASFIGSPPMNFIPVRLARQDGRL- 255
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEAGSVLEATVAAHDPDYg 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 504402764 256 LALLDSGQARCELPLGEAAdalEGREIILGIRPEQIAL 293
Cdd:COG4148 253 LTRLALGGGRLWVPRLDLP---PGTRVRVRIRARDVSL 287
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-237 |
6.95e-65 |
|
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: 210.86 E-value: 6.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 15 SGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSP------KDRDIAMVFQSYAL 88
Cdd:TIGR01186 3 TGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 YPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:TIGR01186 83 FPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 169 KLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:TIGR01186 163 LIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-227 |
1.87e-63 |
|
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: 202.56 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQsyalYP-----TMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:COG1122 80 VFQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-237 |
7.36e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.13 E-value: 7.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsglpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:COG3840 2 LRLDDLTYRYG----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFG----LKIRKLPQAAIDEEVARVakllQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGlrpgLKLTAEQRAQVEQALERV----GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.88e-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: 203.21 E-value: 1.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT---LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---- 76
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 -RDIAMVFQ--SYALYPTMSVRENIEFGLKIRK-LPQAAIDEevaRVAKLLQI----EHLLARKPAQLSGGQQQRVAMGR 148
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRE---RVAELLERvglpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAM-TLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-238 |
2.90e-60 |
|
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: 195.02 E-value: 2.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSY--ALYPTMSVRENIEFGLKIRKLPQaaIDEEVARVAKLLQI-EHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAMT-LGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASF 235
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238
|
...
gi 504402764 236 IGS 238
Cdd:COG1124 239 LAA 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-235 |
5.62e-60 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 193.87 E-value: 5.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKI-RKLPQAAIDEEVA---RVAKLLQIEHLLarkPAQLSGGQQQRVAMGRALARRP 154
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLeklEAVGLRGAEDLY---PAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPaNQFVAS 234
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQ 234
|
.
gi 504402764 235 F 235
Cdd:cd03261 235 F 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-218 |
1.25e-59 |
|
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: 192.72 E-value: 1.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTY--GSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---- 77
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 -DIAMVFQSY--ALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQI---EHLLARKPAQLSGGQQQRVAMGRALA 151
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAM-TLGDKVAVMKDGIIQQFG 218
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAGKIVEEG 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-236 |
1.81e-59 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 192.62 E-value: 1.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDI---- 79
Cdd:PRK09493 2 IEFKNVSKHFGP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEFG-LKIRKLPQAAIdEEVARvaKLLQIEHLLARK---PAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEA-EKQAR--ELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASF 235
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
.
gi 504402764 236 I 236
Cdd:PRK09493 236 L 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-258 |
5.98e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 194.53 E-value: 5.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD----- 76
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 RDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEevaRVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRK---RVAELLElvgLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 154 PKIYLFDEPLSNLDAK-----LRVemrteMKLMHQRLKTTTVYVTHDqieaM----TLGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:COG1135 159 PKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVF 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504402764 225 NDPANQFVASFIGSPPMNFIPVRLARQ------DGRLLAL 258
Cdd:COG1135 230 ANPQSELTRRFLPTVLNDELPEELLARlreaagGGRLVRL 269
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-215 |
4.74e-58 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 188.34 E-value: 4.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 159 FDEPLSNLDAKLRVEMrteMKLMHQ--RLKTTTVYVTHDQ--IEAMtlGDKVAVMKDGIIQ 215
Cdd:COG2884 161 ADEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLelVDRM--PKRVLELEDGRLV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-214 |
5.01e-58 |
|
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: 188.12 E-value: 5.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK----DRDI 79
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEFGL-KIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 159 FDEPLSNLDAklrvEMRTE-MKLMHQ--RLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03262 159 FDEPTSALDP----ELVGEvLDVMKDlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
1.30e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 195.89 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITG---GAILIDEQDVSGMSPKDR--D 78
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQS--YALYPTmSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:COG1123 85 IGMVFQDpmTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-223 |
1.74e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 187.19 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD-IAMV 82
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 163 LSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-227 |
4.72e-57 |
|
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: 186.25 E-value: 4.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD----- 76
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 RDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHdQIEAM-TLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
1.56e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 185.84 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPkDRd 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 iAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDG---IIQQF 217
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGpgrIVERL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-223 |
3.50e-56 |
|
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: 184.48 E-value: 3.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTMSVRENIEFG----LKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
7.31e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 178.33 E-value: 7.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFG-LKIRKLPQAAI----DEEVARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrLGRTSTWRSLLglfpPEDRERALEALErvgLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 151 ARRPKIYLFDEPLSNLDAKL-RVEMRTeMKLMHQRLKTTTVYVTHdQIE-AMTLGDKVAVMKDG 212
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDG 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-223 |
5.14e-53 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 176.20 E-value: 5.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR-DIAMV 82
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 163 LSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-226 |
4.88e-51 |
|
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: 170.83 E-value: 4.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGL-----KIRKLPQAAIDEEVARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 151 ARRPKIYLFDEPLSNLDAKL-RVEMRTeMKLMHQRLKTTTVYVTHdQIE-AMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:cd03256 160 MQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-223 |
4.90e-51 |
|
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: 170.44 E-value: 4.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQI-----TGGAILIDEQDVSGMSPKD-- 76
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQSYALYPtMSVRENIEFGLKIR-KLPQAAIDEevaRVAKLLQIEHLLAR-----KPAQLSGGQQQRVAMGR 148
Cdd:cd03260 79 lrRRVGMVFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDE---RVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 149 ALARRPKIYLFDEPLSNLD--AKLRVEmrtemKLMHQ-RLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDpiSTAKIE-----ELIAElKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-226 |
3.20e-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 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: 169.53 E-value: 3.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDeqdvsGMSPKDRD----- 78
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTLDEEnlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 ---IAMVFQSyalyP-----TMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:TIGR04520 76 rkkVGMVFQN----PdnqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 151 ARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-223 |
4.57e-50 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 178.87 E-value: 4.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTmSVRENIEFGlkirkLPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRAL 150
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLG-----DPDAT-DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 151 ARRPKIYLFDEPLSNLDAklrvemRTEMKLMhQRLKT-----TTVYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:COG2274 627 LRNPRILILDEATSALDA------ETEAIIL-ENLRRllkgrTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-227 |
3.26e-49 |
|
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: 167.24 E-value: 3.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---- 76
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 -RDIAMVFQsyalYPTM-----SVRENIEFGLKIRKLPQAAIDEEVARVAKLLQI-EHLLARKPAQLSGGQQQRVAMGRA 149
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 150 LARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
17-228 |
1.31e-48 |
|
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: 167.98 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 17 LPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDE---QDVSG---MSPKDRDIAMVFQSYALYP 90
Cdd:TIGR02142 9 LGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 91 TMSVRENIEFGLKIRKLPQAAIDEEvaRVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKL 170
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 171 RVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
1.39e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.45 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVnkTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:COG4619 1 LELEGL--SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPtMSVRENIEFGLKIRKLPqaaIDEEvaRVAKLLQI----EHLLARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRERK---FDRE--RALELLERlglpPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 158 LFDEPLSNLDAKL--RVEmrtemKLMHQRLK---TTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:COG4619 153 LLDEPTSALDPENtrRVE-----ELLREYLAeegRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-222 |
1.92e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 172.66 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIA 80
Cdd:COG1132 339 EIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYpTMSVRENIEFGlkirkLPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRA 149
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYG-----RPDAT-DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 150 LARRPKIYLFDEPLSNLDAklrvemRTEM-------KLMHQRlktTTVYVTH--DQIEAMtlgDKVAVMKDGIIQQFGTP 220
Cdd:COG1132 491 LLKDPPILILDEATSALDT------ETEAliqealeRLMKGR---TTIVIAHrlSTIRNA---DRILVLDDGRIVEQGTH 558
|
..
gi 504402764 221 QQ 222
Cdd:COG1132 559 EE 560
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-230 |
3.24e-48 |
|
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: 163.62 E-value: 3.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:TIGR02315 2 LEVENLSKVYPNG-KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENI---EFGLK--IRKLPQAAIDEEVARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRFSEEDKERALSALErvgLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 151 ARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQ 230
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-218 |
4.95e-48 |
|
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: 162.64 E-value: 4.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPkdrDIAMVFQSYALYPTMSVRENIEF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 GLK--IRKLP----QAAIDEEVArvakLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEM 174
Cdd:TIGR01184 78 AVDrvLPDLSkserRAIVEEHIA----LVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504402764 175 RTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-214 |
1.04e-47 |
|
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: 161.42 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-212 |
1.43e-47 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 161.04 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD--- 78
Cdd:NF038007 2 LNMQNAEKCYITKTIKTkvLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 ---IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:NF038007 82 relIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQiEAMTLGDKVAVMKDG 212
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDG 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
1.65e-47 |
|
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: 161.13 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDV-SGMSPKDRDIAMV 82
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 163 LSNLDAKLRVEMRteMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:cd03263 161 TSGLDPASRRAIW--DLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-195 |
1.82e-47 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 160.88 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:TIGR02673 2 IEFHNVSKAYPGG-VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 504402764 159 FDEPLSNLDAKLRVEMrteMKLMHQ--RLKTTTVYVTHD 195
Cdd:TIGR02673 161 ADEPTGNLDPDLSERI---LDLLKRlnKRGTTVIVATHD 196
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-218 |
2.82e-47 |
|
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: 160.41 E-value: 2.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 26 LSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIR 105
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 106 KLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRL 185
Cdd:TIGR01277 99 LKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178
|
170 180 190
....*....|....*....|....*....|...
gi 504402764 186 KTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:TIGR01277 179 QRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
3.89e-47 |
|
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: 158.32 E-value: 3.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIefglkirklpqaaideevarvakllqiehllarkpaqLSGGQQQRVAMGRALARRPKIYLFDE 161
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 162 PLSNLDAKLRVEMRTEM-KLMHQRlktTTVYVTHDqIEAMTLGDKVAVMKDG 212
Cdd:cd03228 123 ATSALDPETEALILEALrALAKGK---TVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-235 |
9.79e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 164.44 E-value: 9.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 15 SGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD------RDIAMVFQSYAL 88
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 YPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 169 KLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASF 235
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.57e-46 |
|
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: 167.24 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTmSVRENIEFGlkirkLPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGR 148
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLG-----RPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 149 ALARRPKIYLFDEPLSNLDAklrvemRTE---MKLMHQRLKT-TTVYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDA------ETEaeiLQALRRLAKGrTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-258 |
6.54e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.35 E-value: 6.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----R 77
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDeevARVAKLLQIEHLLARK---PAQLSGGQQQRVAMGRALARRP 154
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIK---ARVTELLELVGLSDKAdryPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHdQIEAM-TLGDKVAVMKDG-IIQQfGTPQQIYNDPANQFV 232
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH-EMDVVkRICDRVAVIDAGrLVEQ-GTVSEVFSHPKHPLT 237
|
250 260 270
....*....|....*....|....*....|....
gi 504402764 233 ASFIGS------PP--MNFIPVRLARQDGRLLAL 258
Cdd:PRK11153 238 REFIQStlhldlPEdyLARLQAEPTTGSGPLLRL 271
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-214 |
1.32e-45 |
|
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: 155.73 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFG- 101
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 102 ---LKIRKLPQAAIDEEVARVAkllqIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEM 178
Cdd:cd03298 96 spgLKLTAEDRQAIEVALARVG----LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 504402764 179 KLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-196 |
1.36e-45 |
|
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: 156.44 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGS--GLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMspkDRD--- 78
Cdd:COG4181 9 IELRGLTKTVGTgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL---DEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 ------IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAideevARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRA 149
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504402764 150 LARRPKIYLFDEPLSNLDAKLRVEMrteMKLM---HQRLKTTTVYVTHDQ 196
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQI---IDLLfelNRERGTTLVLVTHDP 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
3.19e-45 |
|
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: 152.80 E-value: 3.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMVFQSYALYPTMSVRENI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 99 EFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARK----PAQLSGGQQQRVAMGRALARRPKIYLFDEPLS 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
3.85e-45 |
|
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: 155.97 E-value: 3.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGsGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR--- 77
Cdd:COG0411 2 DPLLEVRGLTKRFG-GLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSYALYPTMSVRENIE---------------FGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQ 142
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEA-MTLGDKVAVMKDGIIQQFGTPQ 221
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVLDFGRVIAEGTPA 238
|
....*..
gi 504402764 222 QIYNDPA 228
Cdd:COG0411 239 EVRADPR 245
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
4.10e-45 |
|
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: 157.91 E-value: 4.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLK---DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ---ITGGAILIDEQDVSGMSPKD- 76
Cdd:COG0444 2 LEVRNLKVYFPTR-RGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 -----RDIAMVFQ-SY-ALYPTMSVRENIEFGLKI-RKLPQAAIDEEVARVAKLLQI---EHLLARKPAQLSGGQQQRVA 145
Cdd:COG0444 81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqieamtLG------DKVAVMKDGIIQQFGT 219
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD------LGvvaeiaDRVAVMYAGRIVEEGP 234
|
....*....
gi 504402764 220 PQQIYNDPA 228
Cdd:COG0444 235 VEELFENPR 243
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-236 |
5.70e-45 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 155.15 E-value: 5.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITG-----GAILIDEQDVSGmspKDRD 78
Cdd:TIGR00972 2 IEIENLNLFYGEK--EALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPgvrieGKVLFDGQDIYD---KKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 -------IAMVFQSYALYPtMSVRENIEFGLKIRKL-PQAAIDEevaRVAKLLQIEHL-------LARKPAQLSGGQQQR 143
Cdd:TIGR00972 77 vvelrrrVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDE---IVEESLKKAALwdevkdrLHDSALGLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 144 VAMGRALARRPKIYLFDEPLSNLD--AKLRVEmrtemKLMHQ-RLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:TIGR00972 153 LCIARALAVEPEVLLLDEPTSALDpiATGKIE-----ELIQElKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPT 227
|
250
....*....|....*.
gi 504402764 221 QQIYNDPANQFVASFI 236
Cdd:TIGR00972 228 EQIFTNPKEKRTEDYI 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-228 |
1.79e-44 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 153.75 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---DIA 80
Cdd:cd03219 1 LEVRGLTKRFG-GLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLP----------QAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 151 ARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDG-IIQQfGTPQQIYNDPA 228
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGrVIAE-GTPDEVRNNPR 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-214 |
2.45e-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: 151.01 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR-DIAMV 82
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEfglkirklpqaaideevarvakllqiehllarkpaqLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 163 LSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-212 |
4.45e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 150.09 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQsyalyptmsvreniefglkirklpqaaideevarvakllqiehllarkpaqLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504402764 163 LSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-234 |
3.19e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 151.11 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS-------GMSP 74
Cdd:COG4598 7 PALEVRDLHKSFGDL--EVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDRD--------IAMVFQSYALYPTMSVREN-IEFGLKIRKLPQAaidEEVARVAKLLQ---IEHLLARKPAQLSGGQQQ 142
Cdd:COG4598 85 ADRRqlqrirtrLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKA---EAIERAEALLAkvgLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLRVEMrteMKLMHQ-----RlktTTVYVTHDQIEAMTLGDKVAVMKDGIIQQF 217
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEV---LKVMRDlaeegR---TMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235
|
250 260
....*....|....*....|.
gi 504402764 218 GTPQQIYNDPAN----QFVAS 234
Cdd:COG4598 236 GPPAEVFGNPKSerlrQFLSS 256
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-228 |
9.22e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.81 E-value: 9.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTY--GSGL----PDTLK---DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSP 74
Cdd:COG4608 8 LEVRDLKKHFpvRGGLfgrtVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KD-----RDIAMVFQ-SYA-LYPTMSVRENIEFGLKIRKLPQAAidEEVARVAKLLQI-----EHlLARKPAQLSGGQQQ 142
Cdd:COG4608 88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLASKA--ERRERVAELLELvglrpEH-ADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLR-------VEMRTEMKLmhqrlktTTVYVTHDqieamtLG------DKVAVM 209
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQaqvlnllEDLQDELGL-------TYLFISHD------LSvvrhisDRVAVM 231
|
250
....*....|....*....
gi 504402764 210 KDGIIQQFGTPQQIYNDPA 228
Cdd:COG4608 232 YLGKIVEIAPRDELYARPL 250
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-196 |
1.26e-42 |
|
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: 147.76 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD-I 79
Cdd:TIGR03608 1 LKNISKKFGDKV--ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 504402764 160 DEPLSNLDAKLRVEMrteMKLMHQRLK--TTTVYVTHDQ 196
Cdd:TIGR03608 159 DEPTGSLDPKNRDEV---LDLLLELNDegKTIIIVTHDP 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-218 |
2.64e-42 |
|
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: 146.04 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 fqsyalyptmsvreniefglkirklPQAAideevarvaKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03214 79 -------------------------PQAL---------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 163 LSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-228 |
4.12e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGmspKDRDIA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPT--MSVRENIEFGL----KIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRP 154
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMrteMKLMHQ--RLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIqQFGTPQQIYNDPA 228
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEAL---YELLRElrREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPEN 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-236 |
7.29e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.08 E-value: 7.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS---GMSPKD--- 76
Cdd:COG4161 2 SIQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQSYALYPTMSVREN-IEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:COG4161 80 lrQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 154 PKIYLFDEPLSNLDAKLRVEMrteMKLMHQRLKT--TTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTpQQIYNDPANQF 231
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQV---VEIIRELSQTgiTQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEA 235
|
....*
gi 504402764 232 VASFI 236
Cdd:COG4161 236 FAHYL 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
1.30e-41 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 146.75 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILideqdvSGMSPKDR---DIA 80
Cdd:PRK11247 13 LLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTAPLAEareDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAidEEVARVAkllqiehlLARK----PAQLSGGQQQRVAMGRALARRPKI 156
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLKGQWRDAAL--QALAAVG--------LADRanewPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-222 |
2.98e-41 |
|
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: 145.06 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:cd03254 4 EFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTmSVRENIEFGLKIrklpqaAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRALA 151
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPN------ATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEM-KLMHQRlktTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALeKLMKGR---TSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-221 |
3.22e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 145.16 E-value: 3.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILI--DEQDVSG-MSPKD--- 76
Cdd:PRK11124 2 SIQLNGINCFYGAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKtPSDKAire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQSYALYPTMSVREN-IEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:PRK11124 80 lrRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 154 PKIYLFDEPLSNLDAKLRVEMrteMKLMHQRLKT--TTVYVTHDQIEAMTLGDKVAVMKDG-IIQQ-----FGTPQ 221
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQI---VSIIRELAETgiTQVIVTHEVEVARKTASRVVYMENGhIVEQgdascFTQPQ 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
6.23e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.52 E-value: 6.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:PRK13632 6 VMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSyalyPT-----MSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRP 154
Cdd:PRK13632 86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAmTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
7.66e-41 |
|
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: 151.46 E-value: 7.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTmSVRENIEFGlkirkLPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGR 148
Cdd:COG4987 412 AVVPQRPHLFDT-TLRENLRLA-----RPDAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKlrvemrTEMKLMhQRLKT-----TTVYVTHDQiEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAA------TEQALL-ADLLEalagrTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEEL 556
|
....*
gi 504402764 224 YNDPA 228
Cdd:COG4987 557 LAQNG 561
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-226 |
7.76e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.58 E-value: 7.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDI 79
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 ----AMVFQ--SYALYPTmSVRENIEFGLKIRKLPQAAIDEEVARVAKL--LQIEHLLARKPAQLSGGQQQRVAMGRALA 151
Cdd:PRK13637 82 rkkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-226 |
1.76e-40 |
|
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: 142.57 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---DIA 80
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRK--LPQAAIDEEVARVAKLLQIEHllaRKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRraKRKARLERVYELFPRLKERRK---QLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 159 FDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-236 |
1.79e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.64 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGA-----ILIDEQDV--SGMSPKD 76
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQSyalyPT---MSVRENIEFGLKI--------------RKLPQAAIDEEVArvAKLlqiehllaRKPAQ-L 136
Cdd:COG1117 90 lrRRVGMVFQK----PNpfpKSIYDNVAYGLRLhgikskseldeiveESLRKAALWDEVK--DRL--------KKSALgL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 137 SGGQQQRVAMGRALARRPKIYLFDEPLSNLD--AKLRVEmrtemKLMHQrLKT--TTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE-----ELILE-LKKdyTIVIVTHNMQQAARVSDYTAFFYLG 229
|
250 260
....*....|....*....|....
gi 504402764 213 IIQQFGTPQQIYNDPANQFVASFI 236
Cdd:COG1117 230 ELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-214 |
2.08e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.10 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 26 LSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIR 105
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 106 KLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRL 185
Cdd:PRK10771 100 LKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQER 179
|
170 180
....*....|....*....|....*....
gi 504402764 186 KTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:PRK10771 180 QLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-212 |
4.08e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.55 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-RD--IA 80
Cdd:COG1129 5 LEMRGISKSFG-GVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLP---QAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 158 LFDEPLSNLDAKlrvEMRTEMKLMHqRLK---TTTVYVTH--DQIeaMTLGDKVAVMKDG 212
Cdd:COG1129 163 ILDEPTASLTER---EVERLFRIIR-RLKaqgVAIIYISHrlDEV--FEIADRVTVLRDG 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-222 |
2.34e-38 |
|
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: 137.67 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSgLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIA 80
Cdd:cd03249 2 EFKNVSFRYPS-RPDVpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTmSVRENIEFGLKirklpqAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRA 149
Cdd:cd03249 81 LVSQEPVLFDG-TIAENIRYGKP------DATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 150 LARRPKIYLFDEPLSNLDAKlrVEMRTEMKLMHQRLKTTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:cd03249 154 LLRNPKILLLDEATSALDAE--SEKLVQEALDRAMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
4.04e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.57 E-value: 4.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 ------RDIAMVFQSYALYPTMSVREN-IEFGLKIRKLPQaaiDEEVARVAKLLQIEHLLARK---PAQLSGGQQQRVAM 146
Cdd:PRK11264 79 lirqlrQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPK---EEATARARELLAKVGLAGKEtsyPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 147 GRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|....*
gi 504402764 227 P----ANQFVASFIG 237
Cdd:PRK11264 235 PqqprTRQFLEKFLL 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-199 |
5.41e-38 |
|
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: 135.68 E-value: 5.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLPdtLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDV-SGMSPKDRDIA 80
Cdd:COG4133 1 MMLEAENLSCRRGERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAaiDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 504402764 161 EPLSNLDAKlRVEMRTEMKLMHQRLKTTTVYVTHDQIEA 199
Cdd:COG4133 157 EPFTALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-216 |
5.64e-38 |
|
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: 137.63 E-value: 5.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGL-------PDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD 76
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 -----RDIAMVFQ-SY-ALYPTMSVRENIefGLKIRKLPQAAIDEEVARVAKLLQIEHL----LARKPAQLSGGQQQRVA 145
Cdd:TIGR02769 83 rrafrRDVQLVFQdSPsAVNPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLrsedADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDG-IIQQ 216
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-212 |
9.20e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 136.75 E-value: 9.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPkdrDIAMVF 83
Cdd:PRK11248 2 LQISHLYADYG-GKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---ERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-195 |
9.36e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 135.30 E-value: 9.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAG-LEQI--TGGAILIDEQDVSGMSPKDRDI 79
Cdd:COG4136 1 MLSLENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEFGLKiRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHD 195
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-212 |
3.31e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.55 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-RD--IA 80
Cdd:COG3845 6 LELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKL-----LQIEhlLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELserygLDVD--PDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 156 IYLFDEPLSNLD----AKLRVEMRtemklmhqRLK---TTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:COG3845 162 ILILDEPTAVLTpqeaDELFEILR--------RLAaegKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
3.39e-37 |
|
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: 132.17 E-value: 3.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---RDIA 80
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFqsyalyptmsvreniefglkirklpqaaideevarvakllqiehllarkpaQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:cd03216 79 MVY---------------------------------------------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 161 EPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3-228 |
6.44e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 136.93 E-value: 6.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELrNVNKTYGsglpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ-----IT-GGAILID-EQDVSgMSPK 75
Cdd:PRK11144 1 MLEL-NFKQQLG----DLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRpqkgrIVlNGRVLFDaEKGIC-LPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 76 DRDIAMVFQSYALYPTMSVRENIEFGLKirklpqAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK11144 75 KRRIGYVFQDARLFPHYKVRGNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-214 |
7.36e-37 |
|
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: 133.10 E-value: 7.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIEFGLkirklpQAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRAL 150
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGA------PLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 151 ARRPKIYLFDEPLSNLDaklrveMRTEMKLMHqRLKT-----TTVYVTHdQIEAMTLGDKVAVMKDGII 214
Cdd:cd03245 156 LNDPPILLLDEPTSAMD------MNSEERLKE-RLRQllgdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
3.45e-36 |
|
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: 131.64 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR--- 77
Cdd:COG0410 1 MPMLEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSYALYPTMSVRENIEFGLKIRKlPQAAIDEEVARVAKLLQI-EHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFPRlKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-214 |
4.54e-36 |
|
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: 130.73 E-value: 4.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLPdtLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSpkdRDIAMVFQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 85 SYAL---YPtMSVRENIEFGL--------KIRKLPQAAIDEEVARVakllQIEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGLyghkglfrRLSKADKAKVDEALERV----GLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 154 PKIYLFDEPLSNLDAKlrvemrTEMKLMH-----QRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03235 151 PDLLLLDEPFAGVDPK------TQEDIYEllrelRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-223 |
4.91e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 131.74 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:COG4604 3 EIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGL------KIRKLPQAAIDEEVARvaklLQIEHLLARKPAQLSGGQQQR--VAMgrALARRP 154
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRfpyskgRLTAEDREIIDEAIAY----LDLEDLADRYLDELSGGQRQRafIAM--VLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMrteMKLMHQ---RLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQM---MKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
7.95e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 131.73 E-value: 7.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYG-------SGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMS 73
Cdd:PRK10419 1 MTLLNVSGLSHHYAhgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 74 PKD-----RDIAMVFQSY--ALYPTMSVRENIefGLKIRKLPQAAIDEEVARVAKLLQI----EHLLARKPAQLSGGQQQ 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREII--REPLRHLLSLDKAERLARASEMLRAvdldDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-227 |
9.70e-36 |
|
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: 136.74 E-value: 9.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQiTGGAILIDEQDVSGMSPKD-----RDIAMVFQS-YA-LYPTMS 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 94 VRENIEFGLKIRKlPQAAIDEEVARVAKLLQIEHL----LARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAK 169
Cdd:COG4172 381 VGQIIAEGLRVHG-PGLSAAERRARVAEALEEVGLdpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 170 LRVEMRTEMKLMHQRLKTTTVYVTHDQ--IEAMTlgDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:COG4172 460 VQAQILDLLRDLQREHGLAYLFISHDLavVRALA--HRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-224 |
1.40e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.39 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPD-TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS--GMSPKDR 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSyalyPT-----MSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK13650 82 KIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 153 RPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
2.15e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.59 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPD---TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR--D 78
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYAL--YPTMSVRENI--------EFGLKIRkLPQAAIDEEVARVAKL-LQIEHLLARKPAQLSGGQQQRVAMG 147
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLalayrrgkRRGLRRG-LTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 148 RALARRPKIYLFDEPLSNLDAKlrvemrTEMKLMH------QRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPK------TAALVLEltekivEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-218 |
3.05e-35 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 128.46 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGeFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD-IAMV 82
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 163 LSNLDAKLRVEMRTemklMHQRLKTTTVYV--TH--DQIEAMTlgDKVAVMKDGIIQQFG 218
Cdd:cd03264 158 TAGLDPEERIRFRN----LLSELGEDRIVIlsTHivEDVESLC--NQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-228 |
4.45e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.53 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS-GMSPKD--- 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKlkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQ--SYALYPTmSVRENIEFGlkirklPQ---AAIDEEVARVAKLLQI----EHLLARKPAQLSGGQQQRVA 145
Cdd:PRK13634 83 lrKKVGIVFQfpEHQLFEE-TVEKDICFG------PMnfgVSEEDAKQKAREMIELvglpEELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYN 225
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
...
gi 504402764 226 DPA 228
Cdd:PRK13634 236 DPD 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-224 |
7.44e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 7.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSyalyPT-----MSVRENIEFGLKIRKLPQaaiDEEVARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPR---EEMVERVDQALRqvgMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 154 PKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTlGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
8.84e-35 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 128.12 E-value: 8.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTmSVRENIEFGlkirkLPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRAL 150
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYG-----RPGAT-REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 151 ARRPKIYLFDEPLSNLDAklrvemRTEM-------KLMHQRlktTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:cd03251 154 LKDPPILILDEATSALDT------ESERlvqaaleRLMKNR---TTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEEL 223
|
.
gi 504402764 224 Y 224
Cdd:cd03251 224 L 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-222 |
1.16e-34 |
|
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: 127.73 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTmSVRENIEFGlkirKLpqAAIDEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRAL 150
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYG----RP--DATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 151 ARRPKIYLFDEPLSNLDAKlrvemrTEMKLMhQRLKT-----TTVYVTHDQIEAMTlGDKVAVMKDGIIQQFGTPQQ 222
Cdd:cd03253 153 LKNPPILLLDEATSALDTH------TEREIQ-AALRDvskgrTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-228 |
2.08e-34 |
|
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: 126.89 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---DIA 80
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 161 EPLSNLDAKLRVEMRTEMKlmHQRLKTTTVYVT-HDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIK--ILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-236 |
2.61e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.39 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDI---- 79
Cdd:PRK10619 6 LNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 -----------AMVFQSYALYPTMSVRENI-EFGLKIRKLPQAAIDEEVAR-VAKLLQIEHLLARKPAQLSGGQQQRVAM 146
Cdd:PRK10619 84 knqlrllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKyLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 147 GRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVyVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|
gi 504402764 227 PANQFVASFI 236
Cdd:PRK10619 243 PQSPRLQQFL 252
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-223 |
3.82e-34 |
|
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: 133.84 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIEFGLkirklpQAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRAL 150
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALGA------PYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 151 ARRPKIYLFDEPLSNLDaklrveMRTEMKLMHqRLK-----TTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMD------NRSEERFKD-RLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
7.19e-34 |
|
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: 125.17 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYG--SGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgMSPKD--RDI 79
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEF-----GLKIRKLpQAAIDEevarVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRP 154
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaglyGLKGDEL-TARLEE----LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMRTEMKlmHQR-LKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIR--QLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-212 |
7.42e-34 |
|
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: 123.48 E-value: 7.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTmSVRENIefglkirklpqaaideevarvakllqiehllarkpaqLSGGQQQRVAMGRALARRPKIYLFDE 161
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 162 PLSNLDAKlrvemrTEMKLMH--QRLK---TTTVYVTHdQIEAMTLGDKVAVMKDG 212
Cdd:cd03246 123 PNSHLDVE------GERALNQaiAALKaagATRIVIAH-RPETLASADRILVLEDG 171
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-162 |
1.01e-33 |
|
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: 124.94 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---DIA 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQieHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
..
gi 504402764 161 EP 162
Cdd:TIGR03410 157 EP 158
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-220 |
1.08e-33 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 124.53 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIE-FGLK-----IRKLPQAAIDEEVArvAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:cd03244 83 IPQDPVLF-SGTIRSNLDpFGEYsdeelWQALERVGLKEFVE--SLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 156 IYLFDEPLSNLDaklrveMRTEmKLMHQRLKT-----TTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:cd03244 160 ILVLDEATASVD------PETD-ALIQKTIREafkdcTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-227 |
2.30e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 126.74 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 18 PDTLK---DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR-----DIAMVFQS--YA 87
Cdd:PRK15079 31 PKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 88 LYPTMSVRENIEFGLKIR--KLPQAAIDEEV-ARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLS 164
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 165 NLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
9.00e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.10 E-value: 9.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL-----EQITGGAILIDEQDVSGMSPK 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 76 D--RDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAiDEEVARVAKLLQIEHL-------LARKPAQLSGGQQQRVAM 146
Cdd:PRK14247 79 ElrRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSK-KELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 147 GRALARRPKIYLFDEPLSNLD----AKLR---VEMRTEMklmhqrlktTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDpentAKIEslfLELKKDM---------TIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
250
....*....|....*..
gi 504402764 220 PQQIYNDPANQFVASFI 236
Cdd:PRK14247 229 TREVFTNPRHELTEKYV 245
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-209 |
1.83e-32 |
|
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: 127.79 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGsGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIA 80
Cdd:TIGR02857 321 SLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTmSVRENIEFGLK-------IRKLPQAAIDEEVArvAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPdasdaeiREALERAGLDEFVA--ALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 154 PKIYLFDEPLSNLDAKLRVEMRTEM-KLMHQRlktTTVYVTHDqIEAMTLGDKVAVM 209
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALrALAQGR---TVLLVTHR-LALAALADRIVVL 529
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-214 |
4.86e-32 |
|
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: 120.01 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGLKIRKLPQAAIDeEVARVAKLLQIEHllaRKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRID-EVLDVVGLKDSAK---KKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 164 SNLDAKLRVEMRtEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03268 155 NGLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
5.51e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.40 E-value: 5.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQS-YALYPTMSVRENIEFGLKIRKLPQaaiDEEVARVAKLLQIEHLLAR---KPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAFGLENHAVPY---DEMHRRVSEALKQVDMLERadyEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTlGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-236 |
5.67e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 121.04 E-value: 5.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 20 TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL-----EQITGGAILIDEQDVsgMSPKD------RDIAMVFQSYAL 88
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSPRTdtvdlrKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 YPtMSVRENIEFGLKIRKLPQAAI-DEEVARVAKLLQI----EHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:PRK14239 98 FP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 164 SNLDAKlrVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFI 236
Cdd:PRK14239 177 SALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-216 |
7.78e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.31 E-value: 7.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSG--LPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSP------K 75
Cdd:PRK11629 6 LQCDNLCKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 76 DRDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAvMKDGIIQQ 216
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
2.24e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.56 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGM---SPK-- 75
Cdd:PRK14267 2 KFAIETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRniySPDvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 76 ----DRDIAMVFQSYALYPTMSVRENIEFGLKIRKL--PQAAIDEEV----ARVAKLLQIEHLLARKPAQLSGGQQQRVA 145
Cdd:PRK14267 80 pievRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDA-------KLRVEMRTEMklmhqrlktTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPvgtakieELLFELKKEY---------TIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
250
....*....|....*...
gi 504402764 219 TPQQIYNDPANQFVASFI 236
Cdd:PRK14267 231 PTRKVFENPEHELTEKYV 248
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-236 |
2.50e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 119.50 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGA-----ILIDEQDV--SGMSPKD 76
Cdd:PRK14243 11 LRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQSYALYPTmSVRENIEFGLKI------------RKLPQAAIDEEVARvaKLLQiehllarKPAQLSGGQQQ 142
Cdd:PRK14243 89 vrRRIGMVFQKPNPFPK-SIYDNIAYGARIngykgdmdelveRSLRQAALWDEVKD--KLKQ-------SGLSLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLD--AKLRVEmrtemKLMHQrLKT--TTVYVTHDQIEAMTLGDKVAVM--------- 209
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDpiSTLRIE-----ELMHE-LKEqyTIIIVTHNMQQAARVSDMTAFFnvelteggg 232
|
250 260
....*....|....*....|....*..
gi 504402764 210 KDGIIQQFGTPQQIYNDPANQFVASFI 236
Cdd:PRK14243 233 RYGYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-195 |
2.79e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 118.73 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSG--LPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---- 77
Cdd:PRK10584 7 VEVHHLKKSVGQGehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 --DIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK10584 87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHD 195
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-214 |
3.38e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 117.74 E-value: 3.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgmsPKDR--DIAMV 82
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERrkSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQS--YALYpTMSVRENIEFGLKirklPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:cd03226 77 MQDvdYQLF-TDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 161 EPLSNLDAKlrvEMRTEMKLMH--QRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03226 152 EPTSGLDYK---NMERVGELIRelAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
4.33e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.21 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS---------- 70
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmhkrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 71 GMS--PKDrdiAMVFQSyalyptMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGR 148
Cdd:COG1137 79 GIGylPQE---ASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 149 ALARRPKIYLFDEPLSNLDAkLRVEmrtEMKLMHQRLKTT--TVYVT-HDQIEamTLG--DKVAVMKDGIIQQFGTPQQI 223
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDP-IAVA---DIQKIIRHLKERgiGVLITdHNVRE--TLGicDRAYIISEGKVLAEGTPEEI 223
|
....
gi 504402764 224 YNDP 227
Cdd:COG1137 224 LNNP 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-232 |
4.60e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 119.32 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAIL---IDEQDVSGMSPKDRDIA 80
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQS-YALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKtTTVYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFV 232
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-227 |
4.84e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.68 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMVFQSYALYPTMSVRENI 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 99 EFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALA-------RRPKIYLFDEPLSNLDAK-- 169
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAhq 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 170 LRVemrteMKLMHQ--RLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:COG4559 177 HAV-----LRLARQlaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-223 |
5.46e-31 |
|
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: 123.70 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTY-GSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RD 78
Cdd:COG4618 329 GRLSVENLTVVPpGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTmSVRENI-EFGlkirklpqAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAM 146
Cdd:COG4618 408 IGYLPQDVELFDG-TIAENIaRFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 147 GRALARRPKIYLFDEPLSNLDAklrvemRTEMKLMH--QRLK---TTTVYVTHDQiEAMTLGDKVAVMKDGIIQQFGTPQ 221
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDD------EGEAALAAaiRALKargATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRD 551
|
..
gi 504402764 222 QI 223
Cdd:COG4618 552 EV 553
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-223 |
6.53e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.19 E-value: 6.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTMSVRENIEFGlkiR--------KLPQAaiDEE-VARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYG---RspwlslwgRLSAE--DNArVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 153 RPKIYLFDEPLSNLDAKLRVEMrteMKLMhQRLKT---TTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVEL---MRLM-RELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-226 |
9.76e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.69 E-value: 9.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSpKDRDI- 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-KNKDIk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 ------AMVFQsyalYPTM-----SVRENIEFGlkirklPQ--AAIDEEVARVA--KLLQI---EHLLARKPAQLSGGQQ 141
Cdd:PRK13649 82 qirkkvGLVFQ----FPESqlfeeTVLKDVAFG------PQnfGVSQEEAEALAreKLALVgisESLFEKNPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 142 QRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQrLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQ 221
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
....*
gi 504402764 222 QIYND 226
Cdd:PRK13649 231 DIFQD 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-212 |
5.40e-30 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 114.19 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPDT----LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL--EQITGGAILIDEQDVSGMSP 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDRdIAMVFQSYALYPTMSVRENIEFGLKIRklpqaaideevarvakllqiehllarkpaQLSGGQQQRVAMGRALARRP 154
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 155 KIYLFDEPLSNLDA--KLRVeMRTEMKLMHQrlKTTTVYVTHD-QIEAMTLGDKVAVMKDG 212
Cdd:cd03213 131 SLLFLDEPTSGLDSssALQV-MSLLRRLADT--GRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-222 |
1.34e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALAR------R 153
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 154 PKIYLFDEPLSNLDakLRVEMRTeMKLMHQRLK---TTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:PRK13548 159 PRWLLLDEPTSALD--LAHQHHV-LRLARQLAHergLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-239 |
1.73e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.83 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSG--LPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--- 76
Cdd:PRK10535 3 ALLELKDIRRSYPSGeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 ---RDIAMVFQSYALYPTMSVRENIEfglkirkLPqaAIDEEVARVAKLLQIEHLLAR---------KPAQLSGGQQQRV 144
Cdd:PRK10535 83 lrrEHFGFIFQRYHLLSHLTAAQNVE-------VP--AVYAGLERKQRLLRAQELLQRlgledrveyQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 145 AMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVyVTHD-QIEAMtlGDKVAVMKDGiiqqfgtpqQI 223
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDpQVAAQ--AERVIEIRDG---------EI 221
|
250
....*....|....*.
gi 504402764 224 YNDPANQFVASFIGSP 239
Cdd:PRK10535 222 VRNPPAQEKVNVAGGT 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-223 |
3.56e-29 |
|
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: 118.60 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIA 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTmSVRENI-EFGlkirklpQAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGR 148
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIaRFG-------ENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-229 |
5.45e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.21 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITG-----GAILIDEQDV----SGMSPKDRDIAMVFQSYALYPt 91
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 92 MSVRENIEFGLKI----RKLPQAAIDEEVARVAKLL-QIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNL 166
Cdd:PRK14258 102 MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 167 DAKlrVEMRTEMKLMHQRLKT--TTVYVTHDQIEAMTLGDKVAVMKD-----GIIQQFGTPQQIYNDPAN 229
Cdd:PRK14258 182 DPI--ASMKVESLIQSLRLRSelTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHD 249
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-237 |
6.20e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 112.46 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL----EQITGGAILIDEQDVSGMSPKDRDIAMVFQS--YALYPTMSVR- 95
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ---ENIEFGLKIRKLPQAAIDEEVARVAkLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRV 172
Cdd:TIGR02770 84 haiETLRSLGKLSKQARALILEALEAVG-LPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 173 EMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIG 237
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-228 |
7.49e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 117.48 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKS----TLMNCIAGLEQITGGAILIDEQDVSGMSP 74
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVeaVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KD------RDIAMVFQ--SYALYPTMSVRENIEFGLKI-RKLPQAAIDEEVARVAKLLQI---EHLLARKPAQLSGGQQQ 142
Cdd:COG4172 84 RElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RV--AMgrALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqieamtLG------DKVAVMKDGII 214
Cdd:COG4172 164 RVmiAM--ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD------LGvvrrfaDRVAVMRQGEI 235
|
250
....*....|....
gi 504402764 215 QQFGTPQQIYNDPA 228
Cdd:COG4172 236 VEQGPTAELFAAPQ 249
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-219 |
2.24e-28 |
|
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: 116.77 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK--DRDIAM 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIEFGLkirklPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRAL 150
Cdd:TIGR01846 536 VLQENVLF-SRSIRDNIALCN-----PGAP-FEHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 151 ARRPKIYLFDEPLSNLDAKLRVEMrteMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALI---MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGR 674
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-212 |
2.25e-28 |
|
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: 110.06 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEqdvSGMSPKDRD-IAMV 82
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNrIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 163 LSNLDAKLRVEMRTEMKLMhQRLKTTTVYVTH--DQIEAMTlgDKVAVMKDG 212
Cdd:cd03269 156 FSGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEELC--DRVLLLNKG 204
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-222 |
2.94e-28 |
|
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: 116.59 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGM--SPKDRDIAM 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLdvQAVRRQLGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTmSVRENIEFGLKIrklpqaAIDE--EVARVAKL--------LQIEHLLARKPAQLSGGQQQRVAMGRALA 151
Cdd:TIGR03797 532 VLQNGRLMSG-SIFENIAGGAPL------TLDEawEAARMAGLaedirampMGMHTVISEGGGTLSGGQRQRLLIARALV 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 152 RRPKIYLFDEPLSNLDAklrvemRTEMKLMH--QRLKTTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:TIGR03797 605 RKPRILLFDEATSALDN------RTQAIVSEslERLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDE 670
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-212 |
3.24e-28 |
|
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: 109.48 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSG---LPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILideqdVSGMspkdrdIA 80
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-----VPGS------IA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSyALYPTMSVRENIEFGLKIRKlpqaaidEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRA 149
Cdd:cd03250 70 YVSQE-PWIQNGTIRENILFGKPFDE-------ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 150 LARRPKIYLFDEPLSNLDAklrvemRTEMKLMHQ------RLKTTTVYVTHdQIEAMTLGDKVAVMKDG 212
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDA------HVGRHIFENcilgllLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-223 |
3.26e-28 |
|
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: 110.15 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK-DRDIAMV 82
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 163 LSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-223 |
5.47e-28 |
|
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: 109.88 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK--DRDIAM 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIEFGlkirklPQAAIDEEVARVAKL-----------LQIEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLagahdfiselpEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 151 ARRPKIYLFDEPLSNLDAKlrvEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:cd03252 154 IHNPRILIFDEATSALDYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
5.61e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDV----SGMSPKDRDI 79
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQS--YALYpTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:PRK13636 85 GMVFQDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-227 |
6.66e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.98 E-value: 6.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTY--------GSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK 75
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 76 D-----RDIAMVFQS-YA-LYPTMSVRENIEFGLKIR-KLPQAaidEEVARVAKL-----LQIEHLlARKPAQLSGGQQQ 142
Cdd:PRK11308 86 AqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSLSAA---ERREKALAMmakvgLRPEHY-DRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
....*
gi 504402764 223 IYNDP 227
Cdd:PRK11308 242 IFNNP 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-226 |
7.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.64 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSG------MS 73
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 74 PKDRDIAMVFQsyalYPTM-----SVRENIEFGLKIRKLPqaaIDEEVARVAKLLQ----IEHLLARKPAQLSGGQQQRV 144
Cdd:PRK13646 82 PVRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMN---LDEVKNYAHRLLMdlgfSRDVMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 145 AMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
..
gi 504402764 225 ND 226
Cdd:PRK13646 235 KD 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-227 |
1.71e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 114.43 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSgLPD--TLKDIQLSIKDGEFLILVGPSGCGKSTlmnCIAGLE---QITGGAILIDEQDVSGMSPK--D 76
Cdd:TIGR00958 479 IEFQDVSFSYPN-RPDvpVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVPLVQYDHHylH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 RDIAMVFQSYALYpTMSVRENIEFGLkirklpQAAIDEEVARVAKLLQ-----------IEHLLARKPAQLSGGQQQRVA 145
Cdd:TIGR00958 555 RQVALVGQEPVLF-SGSVRENIAYGL------TDTPDEEIMAAAKAANahdfimefpngYDTEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKlmhqrLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYN 225
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRS-----RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
..
gi 504402764 226 DP 227
Cdd:TIGR00958 703 DQ 704
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-236 |
2.40e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.60 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQ------DVSGMSPKD--RDIAMVFQSYALYPTM 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKlrKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 93 SVRENIEF-----GLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLD 167
Cdd:PRK14246 106 SIYDNIAYplkshGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 168 A-------KLRVEMRTEMklmhqrlktTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFI 236
Cdd:PRK14246 186 IvnsqaieKLITELKNEI---------AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-227 |
4.15e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILI-DEQDVSGMSPKD-- 76
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGNKNlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 ---RDIAMVFQsyalYPTM-----SVRENIEFGLKirklpQAAIDEEVARVAKLLQI------EHLLARKPAQLSGGQQQ 142
Cdd:PRK13641 82 klrKKVSLVFQ----FPEAqlfenTVLKDVEFGPK-----NFGFSEDEAKEKALKWLkkvglsEDLISKSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLRVEMrteMKLM--HQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM---MQLFkdYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
....*..
gi 504402764 221 QQIYNDP 227
Cdd:PRK13641 230 KEIFSDK 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
4.96e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQ----DVSGMSPKDRDI 79
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQS-----YAlyPTmsVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRP 154
Cdd:PRK13639 81 GIVFQNpddqlFA--PT--VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 155 KIYLFDEPLSNLDAKLRVEMrteMKLMHQRLK--TTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQI---MKLLYDLNKegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
5.41e-27 |
|
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: 112.20 E-value: 5.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGS---GLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILI----DEQDVSGMSPKD 76
Cdd:TIGR03269 280 IKVRNVSKRYISvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 RD-----IAMVFQSYALYPTMSVRENI----------EFGLK--IRKLPQAAIDEEVArvakllqiEHLLARKPAQLSGG 139
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteaiglelpdELARMkaVITLKMVGFDEEKA--------EEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 140 QQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*..
gi 504402764 220 PQQIYND 226
Cdd:TIGR03269 512 PEEIVEE 518
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
1.45e-26 |
|
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: 104.44 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVnktygsGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD---IA 80
Cdd:cd03215 5 LEVRGL------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MV---FQSYALYPTMSVRENIEFglkirklpqaaideevarvakllqiehllarkPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:cd03215 79 YVpedRKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 158 LFDEPLSNLD--AKLRVemrtemklmHQRLK------TTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03215 127 ILDEPTRGVDvgAKAEI---------YRLIReladagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-226 |
1.64e-26 |
|
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: 106.32 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsglpDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE-QITGGAILIDEQDVSGMSPKD--RD 78
Cdd:COG1119 4 LELRNVTVRRG----GKtiLDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWElrKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVfqSYAL----YPTMSVRENIEFGL--KIRkLPQAAIDEEVARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRA 149
Cdd:COG1119 80 IGLV--SPALqlrfPRDETVLDVVLSGFfdSIG-LYREPTDEQRERARELLEllgLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 150 LARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTH---DQIEAMTlgdKVAVMKDGIIQQFGTPQQIYND 226
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDGRVVAAGPKEEVLTS 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-227 |
2.43e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:PRK11831 8 VDMRGVSFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIR-KLPqaaidEEVARVAKLLQIEHLLAR-----KPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHtQLP-----APLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 153 RPKIYLFDEPLSNLDAklrVEMRTEMKL---MHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK11831 161 EPDLIMFDEPFVGQDP---ITMGVLVKLiseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-226 |
2.59e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 106.33 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSP--KDRDIA-MVFQS--YALYPTMsVR 95
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQNpdNQIVATI-VE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMR 175
Cdd:PRK13633 105 EDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 176 TEMKLMHQRLKTTTVYVTHDQIEAMTlGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13633 185 NTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-219 |
4.35e-26 |
|
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: 109.91 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:COG5265 356 GEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTmSVRENIEFGlkiRklPQAAiDEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGR 148
Cdd:COG5265 435 GIVPQDTVLFND-TIAYNIAYG---R--PDAS-EEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRlkTTTVYVTH--------DQIeamtlgdkvAVMKDGIIQQFGT 219
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivdaDEI---------LVLEAGRIVERGT 575
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-206 |
5.11e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.41 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNktYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:PRK10247 8 LQLQNVG--YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTmSVRENIEFGLKIRKlpQAAidEEVARVAKLLQI---EHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRN--QQP--DPAIFLDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 159 FDEPLSNLDAKLRvemRTEMKLMHQRLKTTTV---YVTHDQIEaMTLGDKV 206
Cdd:PRK10247 161 LDEITSALDESNK---HNVNEIIHRYVREQNIavlWVTHDKDE-INHADKV 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-277 |
9.99e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.19 E-value: 9.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGsglpDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDvsgMSPKDRD-I 79
Cdd:COG4152 1 MLELKGLTKRFG----DKtaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRrI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AmvfqsY-----ALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRP 154
Cdd:COG4152 74 G-----YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 155 KIYLFDEPLSNLDAkLRVEMrteMKLMHQRLK---TTTVYVTH--DQIEAMTlgDKVAVMKDG--IIQqfGTPQQIYND- 226
Cdd:COG4152 149 ELLILDEPFSGLDP-VNVEL---LKDVIRELAakgTTVIFSSHqmELVEELC--DRIVIINKGrkVLS--GSVDEIRRQf 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 227 PANQFVASFIGSPPMnfipvrLARQDGRLLALLDSGQARCELPLGEAADAL 277
Cdd:COG4152 221 GRNTLRLEADGDAGW------LRALPGVTVVEEDGDGAELKLEDGADAQEL 265
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-214 |
2.71e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 102.16 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSgLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK--DRDI 79
Cdd:cd03248 12 VKFQNVTFAYPT-RPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYpTMSVRENIEFGL------KIRKLPQAA-IDEEVARVAKLLQIEhlLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:cd03248 91 SLVGQEPVLF-ARSLQDNIAYGLqscsfeCVKEAAQKAhAHSFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 153 RPKIYLFDEPLSNLDAKLRVEMRtemKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-237 |
6.13e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.76 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYgsglP--DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-- 76
Cdd:PRK11288 2 SPYLSFDGIGKTF----PgvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 -RDIAMVFQSYALYPTMSVRENIEFGlkirKLPQAA--IDEEVARVAKLLQIEHL-----LARKPAQLSGGQQQRVAMGR 148
Cdd:PRK11288 78 aAGVAIIYQELHLVPEMTVAENLYLG----QLPHKGgiVNRRLLNYEAREQLEHLgvdidPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKlrvEMRTEMKLMHqRLK---TTTVYVTHDQIEAMTLGDKVAVMKDG-IIQQFGTPQQIY 224
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAR---EIEQLFRVIR-ELRaegRVILYVSHRMEEIFALCDAITVFKDGrYVATFDDMAQVD 229
|
250
....*....|...
gi 504402764 225 NDpanQFVASFIG 237
Cdd:PRK11288 230 RD---QLVQAMVG 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
8.23e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.19 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYgSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RD 78
Cdd:PRK13652 1 MHLIETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQS---YALYPTmsVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK13652 80 VGLVFQNpddQIFSPT--VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-226 |
9.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMS------P 74
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDRDIAMVFQsyalYPTM-----SVRENIEFGlkirklPQ--AAIDEEVARVA--KLLQI---EHLLARKPAQLSGGQQQ 142
Cdd:PRK13643 82 VRKKVGVVFQ----FPESqlfeeTVLKDVAFG------PQnfGIPKEKAEKIAaeKLEMVglaDEFWEKSPFELSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 143 RVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSD 230
|
....
gi 504402764 223 IYND 226
Cdd:PRK13643 231 VFQE 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-227 |
1.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.80 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYgsglPDT----LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL--------EQITGGAILIDEQDVSG 71
Cdd:PRK13640 6 VEFKHVSFTY----PDSkkpaLNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 72 MSPKdrdIAMVFQSY-ALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRAL 150
Cdd:PRK13640 82 IREK---VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 151 ARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-227 |
1.36e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 105.31 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 24 IQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGgAILIDEQDVSGMSPKD--RDIAMVFQSYALyPTMSVRENIEFG 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 102 LkirklPQAAiDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAkl 170
Cdd:PRK11174 447 N-----PDAS-DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA-- 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 171 RVEMRTEMKLMHQRLKTTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-220 |
1.86e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE--QITGGAILIDEQDVSGMSPKDR---DIAMVFQsyalYPT---- 91
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQ----YPVeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 92 MSVRENIEFGL-KIRKLPQAAID--EEVARVAKLLQIEHLLARKP--AQLSGGQQQRVAMGRALARRPKIYLFDEPLSNL 166
Cdd:COG0396 92 VSVSNFLRTALnARRGEELSAREflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 167 DA-KLRV------EMRTEmklmhqrlKTTTVYVTH-----DQIEAmtlgDKVAVMKDGIIQQFGTP 220
Cdd:COG0396 172 DIdALRIvaegvnKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGK 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
5.41e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.00 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MAT-LELRNVNKTY------GSGLPDT--------------LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITG 59
Cdd:COG1134 1 MSSmIEVENVSKSYrlyhepSRSLKELllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 60 GAILIDEQdVSGMSpkdrDIAMVFQsyalyPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGG 139
Cdd:COG1134 81 GRVEVNGR-VSALL----ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 140 QQQRVAMGRALARRPKIYLFDEPLSNLDAKLRvemRTEMKLMHQRLK--TTTVYVTHD--QIEAMTlgDKVAVMKDGIIQ 215
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAAFQ---KKCLARIRELREsgRTVIFVSHSmgAVRRLC--DRAIWLEKGRLV 225
|
250
....*....|
gi 504402764 216 QFGTPQQIYN 225
Cdd:COG1134 226 MDGDPEEVIA 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-226 |
5.78e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.20 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR--- 77
Cdd:PRK10895 1 MATLTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSYALYPTMSVRENIEFGLKIRK-LPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKlmHQRLKTTTVYVT-HDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIE--HLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
6.75e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 98.66 E-value: 6.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MAT-LELRNVNKTY------GSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQ----DV 69
Cdd:COG4778 1 MTTlLEVENLSKTFtlhlqgGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 70 SGMSPKD------RDIAMVFQSYALYPTMSVREniefgLKIRKLPQAAIDEEVA--RVAKLL---QI-EHLLARKPAQLS 137
Cdd:COG4778 80 AQASPREilalrrRTIGYVSQFLRVIPRVSALD-----VVAEPLLERGVDREEAraRARELLarlNLpERLWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 138 GGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLR---VEMRTEMKlmhqRLKTTTVYVTHDqIEAM-TLGDKVAVMKDG 212
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAK----ARGTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-224 |
7.51e-24 |
|
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: 97.72 E-value: 7.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLPDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGleqITGGAILIdEQDVS--GMSPKD 76
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSV-EGDIHynGIPYKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 ------RDIAMVFQSYALYPTMSVRENIEFGLKIRklpqaaiDEEVARVakllqiehllarkpaqLSGGQQQRVAMGRAL 150
Cdd:cd03233 77 faekypGEIIYVSEEDVHFPTLTVRETLDFALRCK-------GNEFVRG----------------ISGGERKRVSIAEAL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 151 ARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTV---YVTHDQIEAMTlgDKVAVMKDGiiqqfgtpQQIY 224
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFvslYQASDEIYDLF--DKVLVLYEG--------RQIY 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-224 |
1.04e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.40 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 19 DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMVFQSY-ALYPTMSVR 95
Cdd:PRK13642 21 NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFGLKIRKLPQaaiDEEVARVAKLLQIEHLL---ARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRV 172
Cdd:PRK13642 101 DDVAFGMENQGIPR---EEMIKRVDEALLAVNMLdfkTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 173 EMRTEMKLMHQRLKTTTVYVTHDQIEAMTlGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
1.07e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL----------EQITGGAILIDEQDVSGMSPKD--------RDIAMV 82
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQ--SYALYPTmSVRENIEFG---LKIRKlpqaaidEEVARVAK--LLQI---EHLLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK13631 122 FQfpEYQLFKD-TIEKDIMFGpvaLGVKK-------SEAKKLAKfyLNKMgldDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 153 RPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVyVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-200 |
1.45e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIdeqdvsgmsPKDRDIAMVFQSYALYPTM--SVRENI 98
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR---------AGGARVAYVPQRSEVPDSLplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 99 EFGL--------KIRKLPQAAIDEEVARVakllQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKL 170
Cdd:NF040873 79 AMGRwarrglwrRLTRDDRAAVDDALERV----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|
gi 504402764 171 RVEMRTEMKLMHQRlKTTTVYVTHDQIEAM 200
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-214 |
1.59e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNktygsgLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---RDIA 80
Cdd:COG1129 257 LEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MV---FQSYALYPTMSVRENIEFGL--KIRK---LPQAAIDEEVARVAKLLQIehllarKPA-------QLSGGQQQRVA 145
Cdd:COG1129 331 YVpedRKGEGLVLDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRI------KTPspeqpvgNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAKLRVEMrteMKLMHQRLK--TTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEI---YRLIRELAAegKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-194 |
1.84e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIdeqdvsgmsPKDRDIAMVFQ-SYalYPTMSVRENIE 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrPY--LPLGTLREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 100 FglkirklPQAAI---DEEVARVAKLLQIEHLLAR------KPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKL 170
Cdd:COG4178 448 Y-------PATAEafsDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180
....*....|....*....|....*
gi 504402764 171 RVEMrteMKLMHQRLKTTT-VYVTH 194
Cdd:COG4178 521 EAAL---YQLLREELPGTTvISVGH 542
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-169 |
2.20e-23 |
|
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: 96.27 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 31 GEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK-DRDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQ 109
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFWAAIHGGAQ 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 110 AAIDEEVARVAkLLQIEHLLArkpAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAK 169
Cdd:TIGR01189 106 RTIEDALAAVG-LTGFEDLPA---AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-231 |
2.30e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKST----LMNCIAgleqiTGGAILIDEQDVSGMSPKD-----RDIAMVFQ--SYALY 89
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 90 PTMSVRENIEFGLKIRKlPQAAIDEEVARVAKLLQIEHLLA----RKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSN 165
Cdd:PRK15134 377 PRLNVLQIIEEGLRVHQ-PTLSAAQREQQVIAVMEEVGLDPetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 166 LDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQF 231
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-240 |
2.65e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 19 DTLKDIQLSIKDGEFLILVGPSGCGKS-TLMNCIAGLEQITGGA--------------ILIDEQDVSGM-SPKDRDIAMV 82
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSEQSAAQMrHVRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQS--YALYPTMSVRENIEFGLKirkLPQAAIDEEVARVAKLL-------QIEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIR---LHQGASREEAMVEAKRMldqvripEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 154 PKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVA 233
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
....*..
gi 504402764 234 SFIGSPP 240
Cdd:PRK10261 267 ALLAAVP 273
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-218 |
3.83e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.90 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYgSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSP---KDRDIA 80
Cdd:PRK15439 12 LCARSISKQY-SGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGlkirkLPQAAIDEEvaRVAKLLQI--EHL-LARKPAQLSGGQQQRVAMGRALARRPKIY 157
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFG-----LPKRQASMQ--KMKQLLAAlgCQLdLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 158 LFDEPLSNLDAklrVEMRTEMKLMHQRLKTTT--VYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:PRK15439 163 ILDEPTASLTP---AETERLFSRIRELLAQGVgiVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-195 |
4.83e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.10 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-----RD 78
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIrklPQAAIDEEVARVAKLLQIEHLLARK---PAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLII---AGASGDDIRRRVSAALDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504402764 156 IYLFDEPLSNLDAKLRVEMrteMKLMHQ--RLKTTTVYVTHD 195
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGI---LRLFEEfnRVGVTVLMATHD 196
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-168 |
5.40e-23 |
|
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: 95.80 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ---ITGGAILIDEQDVSGMSPKDRdIAMVFQSYALYPTMSVREN 97
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 98 IEFGLKIR---KLPQAAIDEEVARVA-KLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:cd03234 102 LTYTAILRlprKSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-215 |
9.77e-23 |
|
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: 95.48 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGailidEQDVSGMSPKDR------DIAMVF-QSYALYPTMS 93
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG-----EVRVAGLVPWKRrkkflrRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 94 VRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVE 173
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504402764 174 MRTEMKLMHQRLKTTTVYVTHD--QIEAmtLGDKVAVMKDGIIQ 215
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYmkDIEA--LARRVLVIDKGRLL 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-223 |
1.21e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RD 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGlkirKLP------------QAAIDEEVARVakllQIEHLLARKPAQLSGGQQQRVAM 146
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMG----RTPhrsrfdtwtetdRAAVERAMERT----GVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 147 GRALARRPKIYLFDEPLSNLDAKLRVemRTeMKLMHQRLKT--TTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQV--RT-LELVRRLVDDgkTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-212 |
1.44e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.85 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL--EQITGGAILIDEQDVSGMSPKDRD--- 78
Cdd:PRK13549 6 LEMKNITKTFG-GVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTErag 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHL---LARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLdinPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 156 IYLFDEPLSNLDAKlrvEMRTEMKLMHQrLK---TTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:PRK13549 164 LLILDEPTASLTES---ETAVLLDIIRD-LKahgIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-219 |
1.83e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGsGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMV 82
Cdd:PRK13657 336 EFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYpTMSVRENIEFGlkirklPQAAIDEEVARVAKLLQIEHLLARKPA-----------QLSGGQQQRVAMGRALA 151
Cdd:PRK13657 415 FQDAGLF-NRSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 152 RRPKIYLFDEPLSNLDAKlrvemrTEMK-------LMHQRlktTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:PRK13657 488 KDPPILILDEATSALDVE------TEAKvkaaldeLMKGR---TTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-195 |
1.94e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIdeqdvsgmsPKDRDIAMVFQS 85
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 86 YALYPTMSVRENIEFGLK-IRKLPQ---------AAIDEEVARVAKLL-QIEHL----------------------LARK 132
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAeLRALEAeleeleaklAEPDEDLERLAELQeEFEALggweaearaeeilsglgfpeedLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 133 PAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAklrvEMRT--EMKLmhQRLKTTTVYVTHD 195
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEwlEEFL--KNYPGTVLVVSHD 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
2.05e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.31 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLK---DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAI---LIDEQDVSGMSPKD- 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 ----------------------RDIAMVFQ--SYALYPTmSVRENIEFGLKIRKLPQAaidEEVARVAKLLQI----EHL 128
Cdd:PRK13651 83 vleklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKE---EAKKRAAKYIELvgldESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 129 LARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKtTTVYVTHDQIEAMTLGDKVAV 208
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIF 237
|
250 260
....*....|....*....|...
gi 504402764 209 MKDGIIQQFGTPQQIYNDpaNQF 231
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD--NKF 258
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
2.18e-22 |
|
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: 98.59 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGsGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDI 79
Cdd:TIGR02868 333 PTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTmSVRENIEFGLKirklpqAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGR 148
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLARP------DATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLktTTVYVTHD 195
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-241 |
2.75e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.77 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 31 GEFLILVGPSGCGKSTLMNCIAGLEQITGGAIL-----IDEQDVSGMSPKDRDIAMVFQS-YA-LYPTMSVRENIEFGLK 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGKLQALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 104 IRKLPQAaiDEEVARVAKLL-----QIEHLLaRKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEM 178
Cdd:PRK10261 430 VHGLLPG--KAAAARVAWLLervglLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 179 KLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPPM 241
Cdd:PRK10261 507 LDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
4.40e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.57 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQI--TGGAIL------------------ 63
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 64 ----------IDEQDVSGMSPKD-------RDIAMVFQ-SYALYPTMSVRENIefglkIRKLPQAAI--DEEVARVAKLL 123
Cdd:TIGR03269 79 gepcpvcggtLEPEEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNV-----LEALEEIGYegKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 124 ---QIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKlrvemrtEMKLMHQRLKT------TTVYVTH 194
Cdd:TIGR03269 154 emvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ-------TAKLVHNALEEavkasgISMVLTS 226
|
250 260 270
....*....|....*....|....*....|..
gi 504402764 195 DQIEAMT-LGDKVAVMKDGIIQQFGTPQQIYN 225
Cdd:TIGR03269 227 HWPEVIEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-227 |
5.21e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 24 IQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSpkDRDIA---MV--FQSYALYPTMSVREN- 97
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP--GHQIArmgVVrtFQHVRLFREMTVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 98 -------IEFGL--KIRKLP--QAAIDEEVARVAKLLQIEHLLA---RKPAQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:PRK11300 102 lvaqhqqLKTGLfsGLLKTPafRRAESEALDRAATWLERVGLLEhanRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 164 SNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-222 |
7.28e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.20 E-value: 7.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-RD-I 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTmSVRENiefgLKIRKlPQaAIDEEVARV------AKLLQIEHLL-------ARkpaQLSGGQQQRVAM 146
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDN----LLLAA-PN-ASDEALIEVlqqvglEKLLEDDKGLnawlgegGR---QLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 147 GRALARRPKIYLFDEPLSNLDAklrvemRTE---MKLMHQRLKTTTV-YVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQ 222
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDA------ETErqiLELLAEHAQNKTVlMITH-RLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-234 |
7.59e-22 |
|
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: 93.24 E-value: 7.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 27 SIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgmsPKDRDIAMVFQsyalyptMSVREniefgLKIRK 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---YKPQYIKADYE-------GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 107 LPQAAIDEEV-ARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRL 185
Cdd:cd03237 86 TKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 186 KTTTVYVTHDQIEAMTLGDKVAVMkDGIIQQFGT--PQQIYNDPANQFVAS 234
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVanPPQSLRSGMNRFLKN 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-214 |
8.01e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 91.61 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD-IAMV 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTmSVRENIefglkirklpqaaideevarvakllqiehllarkPAQLSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:cd03247 81 NQRPYLFDT-TLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 163 LSNLDAKLRVEMrteMKLMHQRLKTTTV-YVTHdQIEAMTLGDKVAVMKDGII 214
Cdd:cd03247 126 TVGLDPITERQL---LSLIFEVLKDKTLiWITH-HLTGIEHMDKILFLENGKI 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-168 |
1.47e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.47 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRdIAMVFQSYALYPTMSVRENIEF 100
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 101 GLKIRKLPQAAIDEEVARVAkLLQIEHLLARkpaQLSGGQQQRVAMGRAL-ARRPkIYLFDEPLSNLDA 168
Cdd:PRK13539 97 WAAFLGGEELDIAAALEAVG-LAPLAHLPFG---YLSAGQKRRVALARLLvSNRP-IWILDEPTAALDA 160
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-267 |
1.61e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.02 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGS--GLPDTLKDIQLSIKDGEFLILVGPSGCGKS----TLMNCIAGLEQITGGAILiDEQDVSGMSP 74
Cdd:PRK09473 10 DALLDVKDLRVTFSTpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATF-NGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KD------RDIAMVFQS--YALYPTMSVRENIEFGLKIRK-LPQAAIDEEVARVAKLLQIEHllARK-----PAQLSGGQ 140
Cdd:PRK09473 89 KElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPE--ARKrmkmyPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 141 QQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 221 QQIYNDPANQFVasfIGSppMNFIPvRLARQDGRLLAL---------LDSG---QARCE 267
Cdd:PRK09473 247 RDVFYQPSHPYS---IGL--LNAVP-RLDAEGESLLTIpgnppnllrLPKGcpfQPRCP 299
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-238 |
1.76e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.93 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKT--YGSGL-----PDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS--GMSP 74
Cdd:PRK15112 5 LEVRNLSKTfrYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDRDIAMVFQ--SYALYPTMSVRENIEFGLKIRKLPQAAIDEEvaRVAKLLQIEHLLARK----PAQLSGGQQQRVAMGR 148
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREK--QIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 149 ALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
250
....*....|
gi 504402764 229 NQFVASFIGS 238
Cdd:PRK15112 243 HELTKRLIAG 252
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-218 |
2.17e-21 |
|
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: 91.44 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMspkdrDIAMVFQsyalyPTMSVRENIEF 100
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 GLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKL 180
Cdd:cd03220 108 NGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 504402764 181 MHQRLKtTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:cd03220 188 LLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-227 |
2.95e-21 |
|
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: 91.82 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAG-LEQITGGAILID----EQDVSGMSPKDR- 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTATYIMrsgaELELYQLSEAERr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 -----DIAMVFQSyalyPTMSVRENIEFGLKIRKLPQAAIDEEVARVAK-----LLQIEHLLAR---KPAQLSGGQQQRV 144
Cdd:TIGR02323 82 rlmrtEWGFVHQN----PRDGLRMRVSAGANIGERLMAIGARHYGNIRAtaqdwLEEVEIDPTRiddLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 145 AMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
...
gi 504402764 225 NDP 227
Cdd:TIGR02323 238 DDP 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-223 |
4.58e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMVF 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVRENIEFGlkirKLPQAAI-------DEE-VARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK10253 88 QNATTPGDITVQELVARG----RYPHQPLftrwrkeDEEaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-226 |
4.88e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSGLP---DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE-QITGGAILIDEQDVSGMSP----KD- 76
Cdd:PRK13645 9 LDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIVGDYAIPANLKKikevKRl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 -RDIAMVFQ--SYALYPTmSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQI-EHLLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK13645 89 rKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 153 RPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-236 |
5.13e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.81 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDeqdvsGMSPKDRDIAMVF 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-----GFSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYP------TMSVRENIEFGLKiRKLPQAAIDEEVARVAKLLQIEHL-------LARKPAQLSGGQQQRVAMGRAL 150
Cdd:TIGR01193 548 QFINYLPqepyifSGSILENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMplgyqteLSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 151 ARRPKIYLFDEPLSNLDaklrveMRTEMKLMHQRLK---TTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNdp 227
Cdd:TIGR01193 627 LTDSKVLILDESTSNLD------TITEKKIVNNLLNlqdKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLD-- 697
|
....*....
gi 504402764 228 ANQFVASFI 236
Cdd:TIGR01193 698 RNGFYASLI 706
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-216 |
5.37e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 22 KDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---RDIAMVFQSY---ALYPTMSVR 95
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFG--LKIRKLPQAA--IDE-EVARVA----KLLQIE-HLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSN 165
Cdd:PRK09700 360 QNMAISrsLKDGGYKGAMglFHEvDEQRTAenqrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 166 LDAKLRVEMRTEMKLMHQRLKTTTVyVTHDQIEAMTLGDKVAVMKDGIIQQ 216
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGKVILM-VSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-223 |
1.31e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 94.24 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNciagleqitggAILIDEQDVSGMSPKDRDIAMV 82
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS-----------ALLAEMDKVEGHVHMKGSVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSyALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLlqiEHL-------LARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:TIGR00957 705 PQQ-AWIQNDSLRENILFGKALNEKYYQQVLEACALLPDL---EILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTT-VYVTHDqIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTrILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-219 |
1.54e-20 |
|
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: 92.97 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL--EQITGGAILIDEQDVSGMSPKDRD--- 78
Cdd:TIGR02633 2 LEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTErag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQSYALYPTMSVRENIEFGLKI-RKLPQAAIDEEVARVAKLLQIEHL----LARKPAQLSGGQQQRVAMGRALARR 153
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEItLPGGRMAYNAMYLRAKNLLRELQLdadnVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 154 PKIYLFDEPLSNLDAKlrvEMRTEMKLMH--QRLKTTTVYVTHDQIEAMTLGDKVAVMKDGiiQQFGT 219
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK---ETEILLDIIRdlKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
1.61e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSyalyP-----TMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:PRK13647 84 VFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVyVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIV-ATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-212 |
1.77e-20 |
|
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: 88.93 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 12 TYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAI-----LIDEQDVSGMSPKDR-DIAMVFQS 85
Cdd:cd03290 9 SWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRySVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 86 YALYpTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEH----LLARKPAQLSGGQQQRVAMGRALARRPKIYLFDE 161
Cdd:cd03290 88 PWLL-NATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 162 PLSNLDAKLRVEMRTE--MKLMhQRLKTTTVYVTHdQIEAMTLGDKVAVMKDG 212
Cdd:cd03290 167 PFSALDIHLSDHLMQEgiLKFL-QDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-226 |
2.09e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR---DIA 80
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFG-LKIRK---LPQAAIDEEVARVAKLLQIEHL---LARKPAQLSGGQQQRVAMGRALARR 153
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGrHLTKKvcgVNIIDWREMRVRAAMMLLRVGLkvdLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 154 PKIYLFDEPLSNLDAKlrvEMRTEMKLMHQRLK--TTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK09700 164 AKVIIMDEPTSSLTNK---EVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-220 |
3.54e-20 |
|
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: 87.85 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSyalyPTM---SVRENIEfglkirklPQAAIDEEvaRVAKLLQIehllARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:cd03369 87 IPQD----PTLfsgTIRSNLD--------PFDEYSDE--EIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 159 FDEPLSNL----DAKLRVEMRTEMKlmhqrlKTTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:cd03369 149 LDEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
3.57e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.86 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD-IA 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDeevARVAKLLQIEHLLARKPAQ---LSGGQQQRVAMGRALARRPKIY 157
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAAR---ALVPPLLEFAKLENKADAKvgeLSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 158 LFDEPLSNLDAKLRvemrtemKLMHQRLKT------TTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK13537 161 VLDEPTTGLDPQAR-------HLMWERLRSllargkTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-237 |
6.80e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 9 VNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ-----------ITGGAILIDEQDVSGMSpkdR 77
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvLLGGRSIFNYRDVLEFR---R 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSYALYPtMSVRENIEFGLKIRKLPQAAIDEEVARvAKLLQI------EHLLARKPAQLSGGQQQRVAMGRALA 151
Cdd:PRK14271 102 RVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQ-ARLTEVglwdavKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLktTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQF 231
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
....*.
gi 504402764 232 VASFIG 237
Cdd:PRK14271 258 TARYVA 263
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-226 |
9.89e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.76 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLeqITGGAILIDEQDVSGMSPK-----DRDI-------AMVFQSYAL 88
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQregrlARDIrksrantGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 YPTMSVRENIEFGLK-------------IRKLPQAAIdEEVARVAkllqIEHLLARKPAQLSGGQQQRVAMGRALARRPK 155
Cdd:PRK09984 98 VNRLSVLENVLIGALgstpfwrtcfswfTREQKQRAL-QALTRVG----MVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 156 IYLFDEPLSNLDAK-LRVEMRTeMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK09984 173 VILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
4-167 |
1.31e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVnktygsGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQiTGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:COG4138 1 LQLNDV------AVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYPTMSVRENIEFGLKiRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALAR-------RP 154
Cdd:COG4138 74 LSQQQSPPFAMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEG 152
|
170
....*....|...
gi 504402764 155 KIYLFDEPLSNLD 167
Cdd:COG4138 153 QLLLLDEPMNSLD 165
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-235 |
2.07e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.84 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTY-----GSGLPDTLK--------------DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILid 65
Cdd:COG4586 3 EVENLSKTYrvyekEPGLKGALKglfrreyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 66 eqdVSGMSP-KDR-----DIAMVF-QSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLaRKPA-QLS 137
Cdd:COG4586 81 ---VLGYVPfKRRkefarRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVrQLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 138 GGQQQR--VAMgrALARRPKIYLFDEPLSNLD--AKLRVemRTEMKLMHQRLKTTTVYVTHD--QIEAmtLGDKVAVMKD 211
Cdd:COG4586 157 LGQRMRceLAA--ALLHRPKILFLDEPTIGLDvvSKEAI--REFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDH 230
|
250 260
....*....|....*....|....
gi 504402764 212 GiiqqfgtpQQIYNDPANQFVASF 235
Cdd:COG4586 231 G--------RIIYDGSLEELKERF 246
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-214 |
5.33e-19 |
|
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: 84.12 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE--QITGGAILIDEQDVSGMSPKDR---DIAMVFQSYALYPtmsvr 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 eniefGLKirklpqaaideevarvakllqIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLD-------A 168
Cdd:cd03217 91 -----GVK---------------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalrlvA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 169 KLRVEMRTEmklmhqrlKTTTVYVTH-----DQIEAmtlgDKVAVMKDGII 214
Cdd:cd03217 145 EVINKLREE--------GKSVLIITHyqrllDYIKP----DRVHVLYDGRI 183
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-214 |
6.35e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---R 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMVFQSYALYPTMSVRENIEFGLKIRKLPQaaIDEEVARVAKLL-QIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQ--FQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-227 |
1.13e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.59 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQ-----DVSGMSPKDR- 77
Cdd:PRK11701 7 LSVRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 -----DIAMVFQSYA--LYPTMSVRENI----------EFGlKIRklpQAAIDEevarvakLLQIEHLLAR---KPAQLS 137
Cdd:PRK11701 85 rllrtEWGFVHQHPRdgLRMQVSAGGNIgerlmavgarHYG-DIR---ATAGDW-------LERVEIDAARiddLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 138 GGQQQRVAMGRALARRPKIYLFDEPLSNLD----AKLRVEMRT---EMKLmhqrlktTTVYVTHDQIEAMTLGDKVAVMK 210
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGlvrELGL-------AVVIVTHDLAVARLLAHRLLVMK 226
|
250
....*....|....*..
gi 504402764 211 DGIIQQFGTPQQIYNDP 227
Cdd:PRK11701 227 QGRVVESGLTDQVLDDP 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-214 |
1.96e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVF 83
Cdd:COG3845 258 LEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 ------QSYALYPTMSVRENIEFGlKIRKLP--------QAAIDEEVARVAKLLQI----EHLLARkpaQLSGGQQQRVA 145
Cdd:COG3845 337 yipedrLGRGLVPDMSVAENLILG-RYRRPPfsrggfldRKAIRAFAEELIEEFDVrtpgPDTPAR---SLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAKlrvemRTEMklMHQRLK------TTTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVG-----AIEF--IHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-196 |
4.08e-18 |
|
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: 80.19 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEqdvsgmspkdrdiamvf 83
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 qsyalyptmsvreniefGLKIRKLPqaaideevarvakllqiehllarkpaQLSGGQQQRVAMGRALARRPKIYLFDEPL 163
Cdd:cd03221 62 -----------------TVKIGYFE--------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|...
gi 504402764 164 SNLDaklrVEMRTEMKLMHQRLKTTTVYVTHDQ 196
Cdd:cd03221 99 NHLD----LESIEALEEALKEYPGTVILVSHDR 127
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-245 |
7.00e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIA-----GLEqiTGGAILIDeqdvsGM---SPKDRDI-AMVFQSYALYPT 91
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVK--GSGSVLLN-----GMpidAKEMRAIsAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 92 MSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLlaRKPAQ-----------LSGGQQQRVAMGRALARRPKIYLFD 160
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGL--RKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 161 EPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQiyndpANQFVaSFIGSP- 239
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ-----AVPFF-SDLGHPc 265
|
....*.
gi 504402764 240 PMNFIP 245
Cdd:TIGR00955 266 PENYNP 271
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
7.82e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAI-LIDEQDVSGMSPKDRDI 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYALYPTMSVRENI-----EFGLKIRKLpQAAIDE--EVARvakllqIEHLLARKPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLlvfgrYFGMSTREI-EAVIPSllEFAR------LESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 153 RPKIYLFDEPLSNLDAKLRvemrtemKLMHQRLKT------TTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHAR-------HLIWERLRSllargkTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
1.06e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsglpDT--LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDiam 81
Cdd:COG0488 316 LELEGLSKSYG----DKtlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 vfqsyALYPTMSVRENIEfglkirklpQAAIDEEVARVAKLLqiEHLL-----ARKP-AQLSGGQQQRVAMGRALARRPK 155
Cdd:COG0488 389 -----ELDPDKTVLDELR---------DGAPGGTEQEVRGYL--GRFLfsgddAFKPvGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 156 IYLFDEPLSNLDaklrVEMRTEMKLMHQRLKTTTVYVTHDQ--IEAMTlgDKVAVMKDGIIQQF 217
Cdd:COG0488 453 VLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRyfLDRVA--TRILEFEDGGVREY 510
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-223 |
1.43e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK--DRDIA 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTmSVRENIEFGlkiRKLPQAAIDE--EVARVAKLLQ-----IEHLLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:PRK10790 419 MVQQDPVVLAD-TFLANVTLG---RDISEEQVWQalETVQLAELARslpdgLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 154 PKIYLFDEPLSNLDAKlrVEMRTEMKLMHQRLKTTTVYVTHdQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK10790 495 PQILILDEATANIDSG--TEQAIQQALAAVREHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-219 |
3.74e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTY-GSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSG--MSPKDRDIA 80
Cdd:PRK11176 342 IEFRNVTFTYpGKEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYpTMSVRENIEFGLKiRKLPQAAIdEEVARVAKLLQ-IEHL-------LARKPAQLSGGQQQRVAMGRALAR 152
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-EQYSREQI-EEAARMAYAMDfINKMdngldtvIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 153 RPKIYLFDEPLSNLDAKlrvEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:PRK11176 498 DSPILILDEATSALDTE---SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGT 561
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-228 |
4.03e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 22 KDIQLSIKDGEFLILVGPSGCGKStlMNCIAGLEQI------TGGAILIDEQDVSGMSPKDRDIAMVFQS--YALYPTMS 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILpagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 94 VREN-IEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLD--AKL 170
Cdd:PRK10418 98 MHTHaRETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDvvAQA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 171 RVeMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPA 228
Cdd:PRK10418 178 RI-LDLLESIVQKR-ALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-227 |
4.05e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 12 TYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMVFQSYALY 89
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 90 pTMSVRENIEFGLKirklpqAAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:PRK10789 402 -SDTVANNIALGRP------DATQQEIEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 159 FDEPLSNLDAklrvemRTEMKLMH---QRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDP 227
Cdd:PRK10789 475 LDDALSAVDG------RTEHQILHnlrQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-240 |
5.63e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.11 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYGS--GLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE----QITGGAILIDEQDVSGMSP 74
Cdd:COG4170 1 MPLLDIRNLTIEIDTpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDR------DIAMVFQ--SYALYPTMSVRENIEFGL-------------KIRKlpQAAIdEEVARVAkLLQIEHLLARKP 133
Cdd:COG4170 81 RERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIpswtfkgkwwqrfKWRK--KRAI-ELLHRVG-IKDHKDIMNSYP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 134 AQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDqIEAMT-LGDKVAVMKDG 212
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD-LESISqWADTITVLYCG 235
|
250 260
....*....|....*....|....*...
gi 504402764 213 IIQQFGTPQQIYNDPANQFVASFIGSPP 240
Cdd:COG4170 236 QTVESGPTEQILKSPHHPYTKALLRSMP 263
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-194 |
7.62e-17 |
|
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: 77.19 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIdeqdvsgmsPKDRDIAMVFQ-SYalYPTMSVREnie 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY--LPLGTLRE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 100 fglkirklpqaaideevarvakllQIEHLLARKpaqLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKlrvemrTEMK 179
Cdd:cd03223 83 ------------------------QLIYPWDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE------SEDR 129
|
170
....*....|....*..
gi 504402764 180 LMH--QRLKTTTVYVTH 194
Cdd:cd03223 130 LYQllKELGITVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-168 |
9.14e-17 |
|
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: 77.92 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 26 LSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK-DRDIAMVFQSYALYPTMSVRENIEFGLKI 104
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFWHAD 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 105 RKlpQAAIDEEVARVAkLLQIEHLLArkpAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:cd03231 101 HS--DEQVEEALARVG-LNGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-256 |
1.54e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL-----EQITGGAILI--------DEQDVSGMspKDRDIAMVFQSyaly 89
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFhgesllhaSEQTLRGV--RGNKIAMIFQE---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 90 PTMSVR--ENIEFGLK--------IRKlpQAAIDEEVA---RVAkLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:PRK15134 101 PMVSLNplHTLEKQLYevlslhrgMRR--EAARGEILNcldRVG-IRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 157 YLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFI 236
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
250 260
....*....|....*....|
gi 504402764 237 GSPPMNFiPVRLARQDGRLL 256
Cdd:PRK15134 258 NSEPSGD-PVPLPEPASPLL 276
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-242 |
2.02e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.18 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS--GMSPKDRDIA 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYpTMSVRENI-------EFGLkIRKLPQAAIDEEVARVAKLLQIEhlLARKPAQLSGGQQQRVAMGRALARR 153
Cdd:PLN03232 1314 IIPQSPVLF-SGTVRFNIdpfsehnDADL-WEALERAHIKDVIDRNPFGLDAE--VSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 154 PKIYLFDEPLSNLDAKLRVEMRtemKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVA 233
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQ---RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
....*....
gi 504402764 234 SFIGSPPMN 242
Cdd:PLN03232 1467 MVHSTGPAN 1475
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-235 |
2.11e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATL-ELRNVNKTYGSglPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPkdrdi 79
Cdd:PRK09544 1 MTSLvSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 amvfQSYALYPTMSVRENiefglKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:PRK09544 74 ----QKLYLDTTLPLTVN-----RFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQfGTPQQIYNDPanQFVASF 235
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEVVSLHP--EFISMF 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-240 |
2.85e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.02 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTYG-SGLPDTLKD-IQLSIKDGEFLILVGPSGCGKSTLMNCIAGL----EQITGGAILIDEQDVSGMSP 74
Cdd:PRK11022 1 MALLNVDKLSVHFGdESAPFRAVDrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDR------DIAMVFQS--YALYPTMSVRENIEFGLKI------RKLPQAAIDeevarVAKLLQI---EHLLARKPAQLS 137
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhqggnkKTRRQRAID-----LLNQVGIpdpASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 138 GGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQF 217
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260
....*....|....*....|...
gi 504402764 218 GTPQQIYNDPANQFVASFIGSPP 240
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRALP 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-226 |
3.36e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 22 KDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR-DIAMVF-----QSYALYPTMSVR 95
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENI------EFGLKIRKLPQAAIDEevaRVAKLLQIEHLLARKPAQ-LSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:PRK15439 360 WNVcalthnRRGFWIKPARENAVLE---RYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 169 KLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK15439 437 SARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD 493
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-224 |
4.36e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS----GMSPKDRDIAMVFQ--SYALYPTmSV 94
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQdpEQQIFYT-DI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 95 RENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLlARKPAQ-LSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVE 173
Cdd:PRK13638 96 DSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 174 MRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIY 224
Cdd:PRK13638 175 MIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-219 |
5.16e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 20 TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGleqitggailideqdvsGMSPKDRDIAMVFQSYALYPTMS------ 93
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVSwifnat 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 94 VRENIEFGLKIRKlpqaaidEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRALARRPKIYLFDEP 162
Cdd:PLN03232 695 VRENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 163 LSNLDAklRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:PLN03232 768 LSALDA--HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-215 |
7.55e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILideqdvsgmspKDRDIAMVFQSyALYPTMSVRENIEF 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 glkirklpqaaIDEE-VARVAKLLQIEHLLA--------------RKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSN 165
Cdd:PTZ00243 744 -----------FDEEdAARLADAVRVSQLEAdlaqlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504402764 166 LDAKLRVEMRTEMKLMHQRLKtTTVYVTHdQIEAMTLGDKVAVMKDGIIQ 215
Cdd:PTZ00243 813 LDAHVGERVVEECFLGALAGK-TRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-195 |
8.67e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.82 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ-ITGGAILideqdvsgmSPkDRDIAMVFQ 84
Cdd:TIGR03719 7 MNRVSKVVPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKdFNGEARP---------QP-GIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 85 SYALYPTMSVRENIEFGL-KIRKL-------------PQAAIDEEVARVAKLLQI-----EHLLARK----------P-- 133
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVaEIKDAldrfneisakyaePDADFDKLAAEQAELQEIidaadAWDLDSQleiamdalrcPpw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 134 ----AQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKlrvemrTEMKLMH--QRLKTTTVYVTHD 195
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE------SVAWLERhlQEYPGTVVAVTHD 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-217 |
9.00e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 9.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYgsglP--DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRD- 78
Cdd:PRK10762 3 ALLQLKGIDKAF----PgvKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 --IAMVFQSYALYPTMSVRENIEFGLKIRKlPQAAID-----EEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALA 151
Cdd:PRK10762 79 agIGIIHQELNLIPQLTIAENIFLGREFVN-RFGRIDwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 152 RRPKIYLFDEPlsnLDAKLRVEMRTEMKLMHQrLKTT---TVYVTHDQIEAMTLGDKVAVMKDGiiqQF 217
Cdd:PRK10762 158 FESKVIIMDEP---TDALTDTETESLFRVIRE-LKSQgrgIVYISHRLKEIFEICDDVTVFRDG---QF 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-223 |
1.50e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.53 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGS--GLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCI------------------------------ 51
Cdd:PTZ00265 1166 IEIMDVNFRYISrpNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 52 -----AGLEQIT-------------------GGAILIDEQDVSGMSPKD-RDIAMVFQSYALYPTMSVRENIEFGlkirk 106
Cdd:PTZ00265 1245 deeqnVGMKNVNefsltkeggsgedstvfknSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG----- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 107 lPQAAIDEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMR 175
Cdd:PTZ00265 1320 -KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 176 TEMKLMHQRLKTTTVYVTHdQIEAMTLGDKVAVMKD-----GIIQQFGTPQQI 223
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNNpdrtgSFVQAHGTHEEL 1450
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-169 |
1.73e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgmspKDRDiamVFQSYALY--------PTMSV 94
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 95 RENIEFGLKIRKLP-QAAIDEEVARVAkLLQIEHLLARkpaQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAK 169
Cdd:PRK13538 92 LENLRFYQRLHGPGdDEALWEALAQVG-LAGFEDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-196 |
1.89e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSGLPDT---------------------LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILI 64
Cdd:COG2401 10 LMRVTKVYSSVLDLServaivleafgvelrvveryvLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 65 DEQDVsgmsPKDRDIAMVfqsYALYPTMSVRENIEFgLKIRKLPQAAideevarvakllqiehLLARKPAQLSGGQQQRV 144
Cdd:COG2401 90 DVPDN----QFGREASLI---DAIGRKGDFKDAVEL-LNAVGLSDAV----------------LWLRRFKELSTGQKFRF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 145 AMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQ 196
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-212 |
2.94e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 16 GLPDTLKDIQLSIKD-------------GEFLILVGPSGCGKSTLMNCIAGLEQITG--GAILIDEQDVSgmSPKDRDIA 80
Cdd:PLN03211 66 GHKPKISDETRQIQErtilngvtgmaspGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENIEFGLKIRkLPQAAIDEEVARVAKLLQIEHLLARKPAQ---------LSGGQQQRVAMGRALA 151
Cdd:PLN03211 144 FVTQDDILYPHLTVRETLVFCSLLR-LPKSLTKQEKILVAESVISELGLTKCENTiignsfirgISGGERKRVSIAHEML 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-195 |
5.84e-15 |
|
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: 76.36 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 27 SIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAIlideqdvsgmsPKDRDIamvfqSY------ALYPtMSVRENIEF 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKI-----SYkpqyisPDYD-GTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 GLKiRKLPQAAIDEEVARVaklLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEM-RTEMK 179
Cdd:COG1245 425 ANT-DDFGSSYYKTEIIKP---LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVaKAIRR 500
|
170
....*....|....*.
gi 504402764 180 LMHQRLKTTTVyVTHD 195
Cdd:COG1245 501 FAENRGKTAMV-VDHD 515
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
3-214 |
6.90e-15 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 76.15 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYG---SGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD-RD 78
Cdd:TIGR01194 337 SIELKDVHMNPKapeGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyRD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 I-AMVFQSYALYPTMSVRENIEfglkirklpQAAIDEEVARVAKL-----LQIEHLLARKPAQLSGGQQQRVAMGRA-LA 151
Cdd:TIGR01194 417 LfSAIFADFHLFDDLIGPDEGE---------HASLDNAQQYLQRLeiadkVKIEDGGFSTTTALSTGQQKRLALICAwLE 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504402764 152 RRPkIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQiEAMTLGDKVAVMKDGII 214
Cdd:TIGR01194 488 DRP-ILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-169 |
1.02e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAglEQITGGAILIDEQDVSGmSPKD----RDIAMVFQSYALYPTMSVRE 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNG-RPLDssfqRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 97 NIEFGLKIR---KLPQAAIDEEVARVAKLLQIEHL---LARKPAQ-LSGGQQQRVAMGRALARRPKIYLF-DEPLSNLDA 168
Cdd:TIGR00956 856 SLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYadaVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS 935
|
.
gi 504402764 169 K 169
Cdd:TIGR00956 936 Q 936
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-226 |
1.52e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 20 TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAG-LEQITGGAILIDEQdvsgmspkdrdIAMVFQSYALYpTMSVRENI 98
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 99 EFGLKIrklpQAAIDEEVARVAKLLQIEHLLA--------RKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKL 170
Cdd:PLN03130 700 LFGSPF----DPERYERAIDVTALQHDLDLLPggdlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 171 RVE-----MRTEMKlmhqrlKTTTVYVThDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PLN03130 776 GRQvfdkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-167 |
2.63e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 27 SIKDGEFLILVGPSGCGKSTLMNCIAGLeqITG-GAILIDEQDVSGMSPKDRD-------------IAM-VFQSYALYPT 91
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQPLEAWSAAELArhraylsqqqtppFAMpVFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 92 MSVREniefglkirklpqAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMG-------RALARRPKIYLFDEPLS 164
Cdd:PRK03695 96 DKTRT-------------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
...
gi 504402764 165 NLD 167
Cdd:PRK03695 163 SLD 165
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-196 |
3.10e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgmspKDR-----DIAMVFQSYALYPTMSVR 95
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLctyqkQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFGLKIrklpqAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMR 175
Cdd:PRK13540 93 ENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170 180
....*....|....*....|.
gi 504402764 176 TemKLMHQRLKTTTVYVTHDQ 196
Cdd:PRK13540 168 T--KIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-195 |
4.94e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.47 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPDtLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIA 80
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTMSVRENiefglkirklpQAAIDEEVARVAKLLQIEHLLARKPA-----QLSGGQQQRVAMGRALARRPK 155
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEG-----------KPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504402764 156 IYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHD 195
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-195 |
5.64e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYGSGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ-ITGGAILIDeqdvsGMSpkdrdIAMVFQ 84
Cdd:PRK11819 9 MNRVSKVVPPKKQ-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKeFEGEARPAP-----GIK-----VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 85 SYALYPTMSVRENIEFGLK-IRKL-------------PQAAIDEEVARVAKLL-QIEHLLA--------------RKP-- 133
Cdd:PRK11819 78 EPQLDPEKTVRENVEEGVAeVKAAldrfneiyaayaePDADFDALAAEQGELQeIIDAADAwdldsqleiamdalRCPpw 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 134 ----AQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAK----LrvemrtEMKLmhQRLKTTTVYVTHD 195
Cdd:PRK11819 158 dakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawL------EQFL--HDYPGTVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-223 |
5.85e-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: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS--GMSPKDRDIAM 81
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkiGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIE-FGlkirklpqAAIDEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRA 149
Cdd:TIGR00957 1365 IPQDPVLF-SGSLRMNLDpFS--------QYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504402764 150 LARRPKIYLFDEPLSNLDAK----LRVEMRTEmklmhqrLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLEtdnlIQSTIRTQ-------FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-161 |
7.17e-14 |
|
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: 72.91 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPD---TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVsgmSPKDRD- 78
Cdd:COG4615 327 TLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREa 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 ----IAMVFQSYALYPTMsvrenieFGlkirkLPQAAIDEEVARVAKLLQIEHLLARK-----PAQLSGGQQQRVAMGRA 149
Cdd:COG4615 404 yrqlFSAVFSDFHLFDRL-------LG-----LDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVA 471
|
170
....*....|...
gi 504402764 150 LA-RRPkIYLFDE 161
Cdd:COG4615 472 LLeDRP-ILVFDE 483
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-168 |
7.57e-14 |
|
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: 69.58 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ--ITGGAILIDEQdvsgmsPKD----RDIAMVFQSYALYPTMSV 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR------PLDknfqRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 95 RENIEFGLKIRklpqaaideevarvakllqiehllarkpaQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:cd03232 97 REALRFSALLR-----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-214 |
8.95e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNktyGSGLPDtlkDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIA-MV 82
Cdd:PRK11288 258 LRLDGLK---GPGLRE---PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 F-----QSYALYPTMSVRENI-----EFGLKIRKLPQAAIDEEVARvaklLQIEHLLARKPA------QLSGGQQQRVAM 146
Cdd:PRK11288 332 LcpedrKAEGIIPVHSVADNInisarRHHLRAGCLINNRWEAENAD----RFIRSLNIKTPSreqlimNLSGGNQQKAIL 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504402764 147 GRALARRPKIYLFDEPLSNLDaklrVEMRTEM-KLMHQRLKT--TTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGID----VGAKHEIyNVIYELAAQgvAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-219 |
9.90e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 71.04 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAIlideqDVSGMspkdrdIAMVFQSYALYPTmSVRENIEF 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHSGR------ISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 GLkirklpqaAIDE-EVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:cd03291 121 GV--------SYDEyRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 169 KLRVEM--RTEMKLMHQRlktTTVYVThDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:cd03291 193 FTEKEIfeSCVCKLMANK---TRILVT-SKMEHLKKADKILILHEGSSYFYGT 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-212 |
1.20e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.07 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 6 LRNVNKTYgSGLpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPK---DRDIAMV 82
Cdd:PRK10982 1 MSNISKSF-PGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRK---LPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-169 |
1.52e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYgsglpDTLKDIQL------SIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILI-DEQDVSGMSPK- 75
Cdd:PTZ00265 383 IQFKNVRFHY-----DTRKDVEIykdlnfTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKw 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 76 -DRDIAMVFQSYALYpTMSVRENIEFGL---------------------------------------------------K 103
Cdd:PTZ00265 458 wRSKIGVVSQDPLLF-SNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliE 536
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 104 IRKLPQAAIDEEVARVAKLLQI-----------EHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAK 169
Cdd:PTZ00265 537 MRKNYQTIKDSEVVDVSKKVLIhdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-245 |
2.67e-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: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 29 KDGEFLILVGPSGCGKSTLMNCIAGlEQITGGAILIDEQD----------------VSGMSPKDRDIAMVFQSYALYPTm 92
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAG-KLKPNLGKFDDPPDwdeildefrgselqnyFTKLLEGDVKVIVKPQYVDLIPK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 93 SVRENIEFGLKiRKLPQAAIDEevarVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRV 172
Cdd:cd03236 102 AVKGKVGELLK-KKDERGKLDE----LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 173 EMrteMKLMHQRLKTT--TVYVTHDQIEAMTLGDKVAVMKD-----GIIQQ-FGTPQQIyndpaNQFVASFIGSPPMNFI 244
Cdd:cd03236 177 NA---ARLIRELAEDDnyVLVVEHDLAVLDYLSDYIHCLYGepgayGVVTLpKSVREGI-----NEFLDGYLPTENMRFR 248
|
.
gi 504402764 245 P 245
Cdd:cd03236 249 E 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-231 |
2.76e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAM 81
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYALYpTMSVRENIE-FG---------------LK--IRKLPQaAIDEEVARVAKllqiehllarkpaQLSGGQQQR 143
Cdd:PLN03130 1318 IPQAPVLF-SGTVRFNLDpFNehndadlweslerahLKdvIRRNSL-GLDAEVSEAGE-------------NFSVGQRQL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 144 VAMGRALARRPKIYLFDEplsnldAKLRVEMRTE---MKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:PLN03130 1383 LSLARALLRRSKILVLDE------ATAAVDVRTDaliQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTP 1456
|
250
....*....|.
gi 504402764 221 QQIYNDPANQF 231
Cdd:PLN03130 1457 ENLLSNEGSAF 1467
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-220 |
3.41e-13 |
|
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: 71.58 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 24 IQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDV-SGMSPKDRDIAMVFQSYALYPTMSVRENIEFGL 102
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 103 KIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTemKLMH 182
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD--LLLK 1106
|
170 180 190
....*....|....*....|....*....|....*...
gi 504402764 183 QRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTP 220
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-214 |
6.31e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 9 VNKTYGSGLpdtlKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDR-DIAMVFQSY- 86
Cdd:PRK10762 260 VDNLSGPGV----NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEd 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 87 ----ALYPTMSVRENI------EFGLKIRKLPQAAIDEEVARVAKLLQIehllaRKPAQ------LSGGQQQRVAMGRAL 150
Cdd:PRK10762 336 rkrdGLVLGMSVKENMsltalrYFSRAGGSLKHADEQQAVSDFIRLFNI-----KTPSMeqaiglLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 151 ARRPKIYLFDEPLSNLDaklrVEMRTEMKLMHQRLKT---TTVYVTHDQIEAMTLGDKVAVMKDGII 214
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-219 |
7.60e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 70.32 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAIlideqDVSGMspkdrdIAMVFQSYALYPTmSVRENIEF 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHSGR------ISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 GLkirklpqaAIDE-EVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVAMGRALARRPKIYLFDEPLSNLDA 168
Cdd:TIGR01271 510 GL--------SYDEyRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 169 KLRVEM--RTEMKLMHQRlktTTVYVThDQIEAMTLGDKVAVMKDGIIQQFGT 219
Cdd:TIGR01271 582 VTEKEIfeSCLCKLMSNK---TRILVT-SKLEHLKKADKILLLHEGVCYFYGT 630
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
237-291 |
8.77e-13 |
|
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: 62.60 E-value: 8.77e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 237 GSPPMNFIPVRLARQDgrllALLDSGQARCELPLGE--AADALEGREIILGIRPEQI 291
Cdd:pfam17912 1 GSPPMNFLPATVVEDG----LLVLGGGVTLPLPEGQvlALKLYVGKEVILGIRPEHI 53
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-181 |
9.21e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 2 ATLELRNVNKTYGSGlPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgMSPKDRDIAM 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 82 VFQSYAL---YPTMsVRENIEFG-------LKIRKL-PQAAIDEEVARVaKLLQIEHllaRKPAQLSGGQQQRVAMGRAL 150
Cdd:PRK15056 83 VPQSEEVdwsFPVL-VEDVVMMGryghmgwLRRAKKrDRQIVTAALARV-DMVEFRH---RQIGELSGGQKKRVFLARAI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 504402764 151 ARRPKIYLFDEPLSNLDAK-------LRVEMRTEMKLM 181
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKteariisLLRELRDEGKTM 195
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-194 |
1.00e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 28 IKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgMSPKDRDIAMVFQSYALYPTMSVRENIEF-----GL 102
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLPGLKADLSTLENLHFlcglhGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 103 KIRKLPQAAIdeevaRVAKLLQIEHLLARkpaQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKlRVEMRTEMKLMH 182
Cdd:PRK13543 113 RAKQMPGSAL-----AIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAH 183
|
170
....*....|..
gi 504402764 183 QRLKTTTVYVTH 194
Cdd:PRK13543 184 LRGGGAALVTTH 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-215 |
1.52e-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: 68.70 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL-EQITGGAILIDEQDVSGMSPKD---RDIAMVFQS---YALYPTMSVR 95
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKP------AQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAK 169
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTAspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504402764 170 LRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQ 215
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-195 |
2.22e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 28 IKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEqdvsgmspkdrDIAMVFQSYALYPTMSVRENIEfglKI-RK 106
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-----------KISYKPQYIKPDYDGTVEDLLR---SItDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 107 LPQAAIDEEVArvaKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEM-RTEMKLMHQRL 185
Cdd:PRK13409 428 LGSSYYKSEII---KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVaKAIRRIAEERE 504
|
170
....*....|
gi 504402764 186 KTTTVyVTHD 195
Cdd:PRK13409 505 ATALV-VDHD 513
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-245 |
2.80e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD--RDIAMVFQSYALYPTMSVRENI 98
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 99 EFGlkirKLP--------QAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKL 170
Cdd:PRK10575 107 AIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 171 RVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPanqfVASFIGSPPMNFIP 245
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE----TLEQIYGIPMGILP 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-215 |
3.43e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQitG---GAILIDEQDVSGMSPKD---RDIAMVFQS---YALYPTMS 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 94 VRENI--------EFGLKIRK-LPQAAIDEEVARVAklLQIEHLLARKpAQLSGGQQQRVAMGRALARRPKIYLFDEPLS 164
Cdd:PRK13549 358 VGKNItlaaldrfTGGSRIDDaAELKTILESIQRLK--VKTASPELAI-ARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 165 NLDAKLRVEMrteMKLMHQRLK--TTTVYVTHDQIEAMTLGDKVAVMKDGIIQ 215
Cdd:PRK13549 435 GIDVGAKYEI---YKLINQLVQqgVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-236 |
5.88e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 19 DTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGleQITGGAILIDEQ-DVSGMSPKD------RDIAMVFQSYALYPT 91
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGViTYDGITPEEikkhyrGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 92 MSVRENIEFGLKIRKlPQ---AAIDEEVAR------VAKLLQIEHLLARKPAQ-----LSGGQQQRVAMGRALARRPKIY 157
Cdd:TIGR00956 153 LTVGETLDFAARCKT-PQnrpDGVSREEYAkhiadvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 158 LFDEPLSNLDAKLRVEMRTEMKLMHQRLKtTTVYVTHDQI--EAMTLGDKVAVMKDGiiqqfgtpQQIYNDPANQFVASF 235
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILD-TTPLVAIYQCsqDAYELFDKVIVLYEG--------YQIYFGPADKAKQYF 302
|
.
gi 504402764 236 I 236
Cdd:TIGR00956 303 E 303
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-162 |
9.27e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgmSPKDRD-----I 79
Cdd:NF033858 3 RLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRavcprI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 80 AMVFQSYA--LYPTMSVRENIEFGLKIRKLPQAaidEEVARVAKLLQIEHLL--ARKPA-QLSGGQQQRVAMGRALARRP 154
Cdd:NF033858 79 AYMPQGLGknLYPTLSVFENLDFFGRLFGQDAA---ERRRRIDELLRATGLApfADRPAgKLSGGMKQKLGLCCALIHDP 155
|
....*...
gi 504402764 155 KIYLFDEP 162
Cdd:NF033858 156 DLLILDEP 163
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-235 |
1.51e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.59 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 28 IKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDeqdvsgmspkdrdiamvfqsyalyptmsvreniefGLKIRKL 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-----------------------------------GITPVYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 108 PQAAideevarvakllqiehllarkpaQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKT 187
Cdd:cd03222 67 PQYI-----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504402764 188 TTVYVTHDQIEAMTLGDKVAVM--KDGIIQQFGTPQQIYNDpANQFVASF 235
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFegEPGVYGIASQPKGTREG-INRFLRGY 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-245 |
1.82e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.19 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGG-AILIDEQDVSGMSPKDRDIAMV 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 83 FQSYALYPTMSVRENIEFGLKIRKLPQaaidEEVARVA----KLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYL 158
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPA----EEIEKVAnwsiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 159 FDEPLSNLDAKLRVEM-RTEMKLMhqRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASF-I 236
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLwNTIVSII--REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkI 2171
|
....*....
gi 504402764 237 GSPPMNFIP 245
Cdd:TIGR01257 2172 KSPKDDLLP 2180
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-240 |
3.57e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 1 MATLELRNVNKTY--GSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQ----ITGGAILIDEQDVSGMSP 74
Cdd:PRK15093 1 MPLLDIRNLTIEFktSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 75 KDR------DIAMVFQ--SYALYPTMSVRENI---------------EFGLKIRKlpqaAIdEEVARVAkLLQIEHLLAR 131
Cdd:PRK15093 81 RERrklvghNVSMIFQepQSCLDPSERVGRQLmqnipgwtykgrwwqRFGWRKRR----AI-ELLHRVG-IKDHKDAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 132 KPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKD 211
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250 260
....*....|....*....|....*....
gi 504402764 212 GIIQQFGTPQQIYNDPANQFVASFIGSPP 240
Cdd:PRK15093 235 GQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-212 |
8.05e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGsGLPdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGL------EqitgGAILIDEQDVSGMSPKD- 76
Cdd:NF040905 2 LEMRGITKTFP-GVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRFKDIRDs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 --RDIAMVFQSYALYPTMSVRENIEFGLKIRKlpQAAID-EEVARVAKllqieHLLAR-----KPAQLSG----GQQQRV 144
Cdd:NF040905 76 eaLGIVIIHQELALIPYLSIAENIFLGNERAK--RGVIDwNETNRRAR-----ELLAKvgldeSPDTLVTdigvGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 145 AMGRALARRPKIYLFDEPLSNLD----AKLrvemrteMKLMHQrLKT---TTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNeedsAAL-------LDLLLE-LKAqgiTSIIISHKLNEIRRVADSITVLRDG 215
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-194 |
8.26e-11 |
|
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: 63.61 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAM-VFQSYALYPtMSVRENIEFG 101
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSSEDMKRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 102 LKirklpqaaiDEEVARVAKLLQIEHLLARKPA---------QLSGGQQQRVAMGRALARRPKIYLFDEPLSnldaKLRV 172
Cdd:TIGR00954 549 LS---------DKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS----AVSV 615
|
170 180
....*....|....*....|..
gi 504402764 173 EMRTEMKLMHQRLKTTTVYVTH 194
Cdd:TIGR00954 616 DVEGYMYRLCREFGITLFSVSH 637
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-230 |
2.17e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.56 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 16 GLPDT----LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEqiTGGAIlidEQDV--SGMSPKDRDIAMVF----QS 85
Cdd:PLN03140 887 GVTEDrlqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGGYI---EGDIriSGFPKKQETFARISgyceQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 86 YALYPTMSVRENIEFGLKIRkLPQAAIDEE----VARVAKLLQIEHLlarKPA--------QLSGGQQQRVAMGRALARR 153
Cdd:PLN03140 962 DIHSPQVTVRESLIYSAFLR-LPKEVSKEEkmmfVDEVMELVELDNL---KDAivglpgvtGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 154 PKIYLFDEPLSNLDAK-LRVEMRTemklMHQRLKT--TTVYVTH----DQIEAMtlgDKVAVMKDGiiqqfgtPQQIYND 226
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARaAAIVMRT----VRNTVDTgrTVVCTIHqpsiDIFEAF---DELLLMKRG-------GQVIYSG 1103
|
....
gi 504402764 227 PANQ 230
Cdd:PLN03140 1104 PLGR 1107
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-226 |
2.98e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQiTGGAILIDeqdvsGMSPKDRDIAMVF 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID-----GVSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYP------TMSVRENIEfglkirklPQAAI-DEEVARVAKLLQIEHLLARKPAQ-----------LSGGQQQRVA 145
Cdd:TIGR01271 1292 KAFGVIPqkvfifSGTFRKNLD--------PYEQWsDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMC 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAklrVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYN 225
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
.
gi 504402764 226 D 226
Cdd:TIGR01271 1441 E 1441
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-231 |
5.02e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 3 TLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVS--GMSPKDRDIA 80
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGayGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYPTmSVRENIEFGLKirklpqaAIDEEVARVAKLLQIEHLLARKP-----------AQLSGGQQQRVAMGRA 149
Cdd:PTZ00243 1388 MIPQDPVLFDG-TVRQNVDPFLE-------ASSAEVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 150 LARRPKIY-LFDEPLSNLDAKLRVEMR----------TEMKLMHqRLKTTTVYvthdqieamtlgDKVAVMKDGIIQQFG 218
Cdd:PTZ00243 1460 LLKKGSGFiLMDEATANIDPALDRQIQatvmsafsayTVITIAH-RLHTVAQY------------DKIIVMDHGAVAEMG 1526
|
250
....*....|...
gi 504402764 219 TPQQIYNDPANQF 231
Cdd:PTZ00243 1527 SPRELVMNRQSIF 1539
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-171 |
5.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.34 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSgmspkdrDIAMVFQSY-----ALYPTMSVR 95
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-------NIAKPYCTYighnlGLKLEMTVF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504402764 96 ENIEFGLKI---RKLPQAAIdeevarvaKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLR 171
Cdd:PRK13541 89 ENLKFWSEIynsAETLYAAI--------HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
119-174 |
5.71e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 5.71e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 119 VAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEM 174
Cdd:COG1245 196 LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
119-174 |
6.07e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 6.07e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 119 VAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEM 174
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV 251
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-219 |
8.49e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE--QITGGAILIDEQDVSGMSPKDRD--- 78
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 79 IAMVFQsyalYP-TMSVRENIEF-------GLKIRKLPQAAIDEEVARVAKLLQI----EHLLARKPAQ-LSGGQQQRVA 145
Cdd:CHL00131 86 IFLAFQ----YPiEIPGVSNADFlrlaynsKRKFQGLPELDPLEFLEIINEKLKLvgmdPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 146 MGRALARRPKIYLFDEPLSNLDAK-LRVEMRTEMKLMHQrlKTTTVYVTH-----DQIEAmtlgDKVAVMKDGIIQQFGT 219
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDaLKIIAEGINKLMTS--ENSIILITHyqrllDYIKP----DYVHVMQNGKIIKTGD 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-167 |
1.10e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIdEQD--VSGMsPKD--RDIA-MVFQsyalYPTMSVR 95
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDliVARL-QQDppRNVEgTVYD----FVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFgLKI-----RKLPQAAIDEEVARVAKLL-QIEH------------------LLARKP-AQLSGGQQQRVAMGRAL 150
Cdd:PRK11147 93 EQAEY-LKRyhdisHLVETDPSEKNLNELAKLQeQLDHhnlwqlenrinevlaqlgLDPDAAlSSLSGGWLRKAALGRAL 171
|
170
....*....|....*..
gi 504402764 151 ARRPKIYLFDEPLSNLD 167
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD 188
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-167 |
1.56e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLE--QITGGAILIDEQDVSGMSPKDR---DIAMVFQSYALYPTMSVR 95
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 96 ENIEFGLK-IRKL-PQAAID-----EEVARVAKLLQI-EHLLARK-PAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNL 166
Cdd:PRK09580 97 FFLQTALNaVRSYrGQEPLDrfdfqDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
.
gi 504402764 167 D 167
Cdd:PRK09580 177 D 177
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-167 |
1.72e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSIKDGE---FLilvGPSGCGKSTLMNCIAGLEQITGG-AIL----IDEQD------VSGMSpkdrdiamvfQSYAL 88
Cdd:NF033858 284 HVSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGeAWLfgqpVDAGDiatrrrVGYMS----------QAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 YPTMSVRENIEFGLKIRKLPQAAIDeevARVAKLLQ---IEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSN 165
Cdd:NF033858 351 YGELTVRQNLELHARLFHLPAAEIA---ARVAEMLErfdLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
..
gi 504402764 166 LD 167
Cdd:NF033858 428 VD 429
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-167 |
1.83e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLpdTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQdvsgmspkdRDIAMVF 83
Cdd:TIGR03719 323 IEAENLTKAFGDKL--LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET---------VKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSY-ALYPTMSVRENIEFGLKIRKLPQAAIDEEvARVAKL------LQiehllaRKPAQLSGGQQQRVAMGRALARRPKI 156
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGLDIIKLGKREIPSR-AYVGRFnfkgsdQQ------KKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 504402764 157 YLFDEPLSNLD 167
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-223 |
4.69e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGleQITGGA----------ILIDEQDVSGMSPKD--RDIAMVFQSYAL 88
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGaprgarvtgdVTLNGEPLAAIDAPRlaRLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 YPTMSVRENIEFGlkirKLPQAAI-------DEEVARVA-KLLQIEHLLARKPAQLSGGQQQRVAMGRALA--------- 151
Cdd:PRK13547 95 AFAFSAREIVLLG----RYPHARRagalthrDGEIAWQAlALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 152 RRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQI 223
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-223 |
5.91e-09 |
|
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: 56.46 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGM---SPKDRdIA 80
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhTLRSR-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 81 MVFQSYALYpTMSVRENIEFGLKirklpqaAIDEEVARVAKLLQIEHLLARKPAQL-----------SGGQQQRVAMGRA 149
Cdd:cd03288 99 IILQDPILF-SGSIRFNLDPECK-------CTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 150 LARRPKIYLFDEPLSNLD-AKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAmtlgDKVAVMKDGIIQQFGTPQQI 223
Cdd:cd03288 171 FVRKSSILIMDEATASIDmATENILQKVVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENL 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-195 |
1.13e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.53 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 31 GEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIdeqdVSGmspkdrdiamvfqsyalyptmsvreniefglkirklpqa 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDG--------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 111 aidEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMR-----TEMKLMHQRL 185
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEK 115
|
170
....*....|
gi 504402764 186 KTTTVYVTHD 195
Cdd:smart00382 116 NLTVILTTND 125
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
284-357 |
2.32e-08 |
|
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: 50.70 E-value: 2.32e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504402764 284 LGIRPEQIALGAADGnglpAIRAEVQVTEPTGPDLLVFVTL-NQTKVCCRLAPDVAC--RVGDTLNLQFDPARVLLF 357
Cdd:pfam08402 1 LAIRPEKIRLAAAAN----GLSGTVTDVEYLGDHTRYHVELaGGEELVVRVPNAHARppAPGDRVGLGWDPEDAHVL 73
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-195 |
1.20e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSGlpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDrdiamvf 83
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 84 QSYALYPTMSVREniefglKIRKLPQAAIDEEVAR--VAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDE 161
Cdd:PRK15064 391 HAYDFENDLTLFD------WMSQWRQEGDDEQAVRgtLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190
....*....|....*....|....*....|....
gi 504402764 162 PLSNLDaklrVEMRTEMKLMHQRLKTTTVYVTHD 195
Cdd:PRK15064 465 PTNHMD----MESIESLNMALEKYEGTLIFVSHD 494
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-196 |
2.28e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 23 DIQLSikDGEFLILVGPSGCGKSTLMNCIagleqitgGAILIDEQdvsgmspkdrdiamvfqsyalyptmsvreniefgL 102
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAI--------GLALGGAQ----------------------------------S 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 103 KIRKLPQAAIDEEVARVAkllqIEHLLARKpaQLSGGQQQRVAMGRALA-----RRPkIYLFDEPLSNLDakLRVEMRTE 177
Cdd:cd03227 51 ATRRRSGVKAGCIVAAVS----AELIFTRL--QLSGGEKELSALALILAlaslkPRP-LYILDEIDRGLD--PRDGQALA 121
|
170 180
....*....|....*....|
gi 504402764 178 MKLMHQRLKTTTV-YVTHDQ 196
Cdd:cd03227 122 EAILEHLVKGAQViVITHLP 141
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-218 |
2.45e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 7 RNVNKTYGSglpdtLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAIlideqdvsgmsPKDRDIAMVFQSY 86
Cdd:PRK13546 31 KHKNKTFFA-----LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 87 ALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNL 166
Cdd:PRK13546 95 GLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504402764 167 DAKLRVEMRTEMKLMHQRLKtTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFG 218
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-226 |
3.22e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 20 TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAG-LEQITG--------GAILIDEQDVSGMSP--KDRDIAMVfqsyal 88
Cdd:PRK10938 18 TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGerqsqfshITRLSFEQLQKLVSDewQRNNTDML------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 89 yptmSVRENiEFGLKIRKLPQAAIDEEV--ARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNL 166
Cdd:PRK10938 92 ----SPGED-DTGRTTAEIIQDEVKDPArcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 167 DAKLRVEMRTEMKLMHQRlKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYND 226
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-199 |
3.25e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNKTYGsglpD--TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGlEQITGGA---ILIDEQDVSGMSPKD--R 77
Cdd:PRK10938 262 VLNNGVVSYN----DrpILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSndlTLFGRRRGSGETIWDikK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 78 DIAMV----------------------FQSYALYPTMSVREniefglkiRKLPQAAIDeevarvakLLQIEHLLARKPAQ 135
Cdd:PRK10938 337 HIGYVssslhldyrvstsvrnvilsgfFDSIGIYQAVSDRQ--------QKLAQQWLD--------ILGIDKRTADAPFH 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504402764 136 -LSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEA 199
Cdd:PRK10938 401 sLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-167 |
5.74e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 16 GLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAI---------LIDEQDVSGMSPKDRDIAMVFQSY 86
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 87 ALYPTMSVRENI-EFGLKIRklpqaaideevarvakllqiehlLARKPA-QLSGGQQQRVAMGRALARRPKIYLFDEPLS 164
Cdd:PLN03073 600 PGVPEQKLRAHLgSFGVTGN-----------------------LALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
...
gi 504402764 165 NLD 167
Cdd:PLN03073 657 HLD 659
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-167 |
1.19e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKTYGSglpdtlkdiQLSIKDGEFLI-------LVGPSGCGKSTLMNCIAGLEQITGGAILIdeqdvsGMSPKd 76
Cdd:PRK11819 325 IEAENLSKSFGD---------RLLIDDLSFSLppggivgIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVK- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 77 rdIAMVFQSY-ALYPTMSVRENIEFGLKIRKLPQAaideEVARVAkllqiehLLAR---------KPA-QLSGGQQQRVA 145
Cdd:PRK11819 389 --LAYVDQSRdALDPNKTVWEEISGGLDIIKVGNR----EIPSRA-------YVGRfnfkggdqqKKVgVLSGGERNRLH 455
|
170 180
....*....|....*....|..
gi 504402764 146 MGRALARRPKIYLFDEPLSNLD 167
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD 477
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
105-219 |
1.32e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 105 RKLPQAAIDEEVARvaklLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQR 184
Cdd:NF000106 118 RKDARARADELLER----FSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 504402764 185 LKT---TTVYVTHDQIEA--MTLGDKVAVMKDGIIQQFGT 219
Cdd:NF000106 194 GATvllTTQYMEEAEQLAheLTVIDRGRVIADGKVDELKT 233
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-164 |
2.21e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAIlideqDVSGMSpkdrdiAMVFQSYALYPTMSVRENIEF 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA------ALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504402764 101 GLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLS 164
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-212 |
2.25e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 20 TLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKD---RDIAMVFQ---SYALYPTMS 93
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 94 VR-----ENIE-----FGL----KIRKLPQAAIDEevARVAKLLQIEHLlarkpAQLSGGQQQRVAMGRALARRPKIYLF 159
Cdd:PRK10982 343 IGfnsliSNIRnyknkVGLldnsRMKSDTQWVIDS--MRVKTPGHRTQI-----GSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 160 DEPLSNLDAKLRVEMRTEMKLMHQRLKtTTVYVTHDQIEAMTLGDKVAVMKDG 212
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-195 |
2.39e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTLMNciagleqiTGGAILIDEQDVSGMSPKDRDIAMVfqsyalyptmsvrenief 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLPKFSRNKLIF------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 101 glkIRKLpQAAIDeevarvaklLQIEHL-LARKPAQLSGGQQQRVAMGRALARRPK--IYLFDEPLSNLDaklrveMRTE 177
Cdd:cd03238 65 ---IDQL-QFLID---------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH------QQDI 125
|
170 180
....*....|....*....|...
gi 504402764 178 MKLMHQ-----RLKTTTVYVTHD 195
Cdd:cd03238 126 NQLLEVikgliDLGNTVILIEHN 148
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-206 |
9.10e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 21 LKDIQLSIKDGEFLILVGPSGCGKSTL-MNCIAG------LEQITGGA----ILIDEQDV---SGMSPKdrdIAMVFQSY 86
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAegqrryVESLSAYArqflGQMDKPDVdsiEGLSPA---IAIDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 87 ALYPTMSVRENIEFGLKIRKL-PQAAIdeeVARVAKLLQI--EHL-LARKPAQLSGGQQQRVAMGRALARRPK--IYLFD 160
Cdd:cd03270 88 SRNPRSTVGTVTEIYDYLRLLfARVGI---RERLGFLVDVglGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504402764 161 EPLSNLdaklrvEMRTEMKLMH--QRLKT---TTVYVTHDQiEAMTLGDKV 206
Cdd:cd03270 165 EPSIGL------HPRDNDRLIEtlKRLRDlgnTVLVVEHDE-DTIRAADHV 208
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
9-62 |
4.18e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.23 E-value: 4.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 504402764 9 VNKTYGSGLpDTLKDIqlsIKdGEFLILVGPSGCGKSTLMNCIAGLEQITGGAI 62
Cdd:cd01854 68 VSAKTGEGL-DELREL---LK-GKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
4-137 |
1.20e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 4 LELRNVNKtygsglpdtLKDIQLSIKDGEFLIlVGPSGCGKSTLMNCIA--------GLEQITGGAILIDEQDVSGMSPK 75
Cdd:pfam13476 1 LTIENFRS---------FRDQTIDFSKGLTLI-TGPNGSGKTTILDAIKlalygktsRLKRKSGGGFVKGDIRIGLEGKG 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504402764 76 DRDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLS 137
Cdd:pfam13476 71 KAYVEITFENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILP 132
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-167 |
1.25e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 5 ELRNVNktYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQdvsgmspkdRDIAMvFQ 84
Cdd:PRK11147 321 EMENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK---------LEVAY-FD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 85 SY--ALYPTMSVRENIEFGLKirklpqaaiDEEVARVAKllqieHLL------------ARKPAQ-LSGGQQQRVAMGRA 149
Cdd:PRK11147 389 QHraELDPEKTVMDNLAEGKQ---------EVMVNGRPR-----HVLgylqdflfhpkrAMTPVKaLSGGERNRLLLARL 454
|
170
....*....|....*...
gi 504402764 150 LARRPKIYLFDEPLSNLD 167
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLD 472
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
9-60 |
2.05e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 2.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 504402764 9 VNKTYGSGLPDTLKDIQlsikdGEFLILVGPSGCGKSTLMNCIAG-LEQITGG 60
Cdd:pfam03193 89 VSAKTGEGIEALKELLK-----GKTTVLAGQSGVGKSTLLNALLPeLDLRTGE 136
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
3-49 |
2.54e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 504402764 3 TLELRNVNKtygsglpDTLKDIQLSIKDGEFLILVGPSGCGKSTLMN 49
Cdd:TIGR00630 613 FLTLKGARE-------NNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
91-227 |
5.21e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402764 91 TMSVRENIEFGLKIRKLP-QAAIDEEV-----ARVAKLLQI--EHL-LARKPAQLSGGQQQRVAMGRALARRPK--IYLF 159
Cdd:TIGR00630 435 ELSIREAHEFFNQLTLTPeEKKIAEEVlkeirERLGFLIDVglDYLsLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVL 514
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504402764 160 DEPLSNLDAklRVEMRTEMKLMHQR-LKTTTVYVTHDQiEAMTLGDKVAVMKDG-------IIQQfGTPQQIYNDP 227
Cdd:TIGR00630 515 DEPSIGLHQ--RDNRRLINTLKRLRdLGNTLIVVEHDE-DTIRAADYVIDIGPGagehggeVVAS-GTPEEILANP 586
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
18-60 |
6.67e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 38.60 E-value: 6.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 504402764 18 PDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAglEQITGG 60
Cdd:COG1401 208 EETLEAFLAALKTKKNVILAGPPGTGKTYLARRLA--EALGGE 248
|
|
| |
