|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-368 |
5.32e-172 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 483.42 E-value: 5.32e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVP------------------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 241 TRPANLDVARFVGAPRINLLDGEVKAHGVVWAQGRL---VGHSHGKTGPCRIAFRPQAGTLESVDGLEVEGTLVNVEYTG 317
Cdd:COG3839 223 DRPANLFVAGFIGSPPMNLLPGTVEGGGVRLGGVRLplpAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLG 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 318 AELIASLQVDGIEdaCVFCFPANSPaIRVGQALRVSVPIGEIHLFDAD-GQR 368
Cdd:COG3839 303 SETLVHVRLGGQE--LVARVPGDTR-LRPGDTVRLAFDPERLHLFDAEtGRR 351
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-364 |
6.31e-151 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 429.90 E-value: 6.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVP------------------KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 241 TRPANLDVARFVGapRINLLDGEVKAH--GVVWAQGRLV----GHSHGKTGPCRIAFRPQAGTLESVDGL-EVEGTLVNV 313
Cdd:COG3842 225 ERPATRFVADFIG--EANLLPGTVLGDegGGVRTGGRTLevpaDAGLAAGGPVTVAIRPEDIRLSPEGPEnGLPGTVEDV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 314 EYTGAELIASLQVDGIEDACVFCFPANSPAIRVGQALRVSVPIGEIHLFDA 364
Cdd:COG3842 303 VFLGSHVRYRVRLGDGQELVVRVPNRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-368 |
1.97e-131 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 380.73 E-value: 1.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQR 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMP------------------KAEIEERVAEAARILELEPLLDRKPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 240 YTRPANLDVARFVGAPRINLLDGEVKAHGVVW------AQGRLVGHSHGKTGPCRIAFRPQAGTLESvDGLEVEGTLVNV 313
Cdd:PRK11650 223 YEKPASTFVASFIGSPAMNLLDGRVSADGAAFelaggiALPLGGGYRQYAGRKLTLGIRPEHIALSS-AEGGVPLTVDTV 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 314 EYTGAELIASLQVDGIEdaCVFCFPANSPAiRVGQALRVSVPIGEIHLFDADGQR 368
Cdd:PRK11650 302 ELLGADNLAHGRWGGQP--LVVRLPHQERP-AAGSTLWLHLPANQLHLFDADTGR 353
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-361 |
2.30e-111 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 329.41 E-value: 2.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA-LSPSQRDCAMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVAL 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPS------------------KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 243 PANLDVARFVGAprINLLDGEVKAhGVVWAQG-RLVGHSHGKTGPCRIAFRPQAGTLESVDGLE--VEGTLVNVEYTGAE 319
Cdd:COG1118 225 PATPFVARFLGC--VNVLRGRVIG-GQLEADGlTLPVAEPLPDGPAVAGVRPHDIEVSREPEGEntFPATVARVSELGPE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2536923639 320 LIASLQVDGIED----ACVFCFPANSPAIRVGQALRVSVPIGEIHL 361
Cdd:COG1118 302 VRVELKLEDGEGqpleAEVTKEAWAELGLAPGDPVYLRPRPARVFL 347
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-266 |
1.27e-110 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 328.44 E-value: 1.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMV 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICTPLLMRglgfwgrlpgaglfsantrriKAEAQASARKVAQSLG---IDGLWERKPAQLSGGQR 157
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQ---------------------KTPAAEITPRVMEALRmvqLEEFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
250 260
....*....|....*....|....*....
gi 2536923639 238 EIYTRPANLDVARFVGapRINLLDGEVKA 266
Cdd:PRK09452 231 EIYEEPKNLFVARFIG--EINIFDATVIE 257
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-362 |
4.92e-109 |
|
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: 323.53 E-value: 4.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMG------------------RAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:TIGR03265 144 ALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 241 TRPANLDVARFVGapRINLLDGEVKAHGVVWAQG---RLVGHSHGKTGPCRIAFRPQAGTLESVDGLE--VEGTLVNVEY 315
Cdd:TIGR03265 224 RHPATPFVADFVG--EVNWLPGTRGGGSRARVGGltlACAPGLAQPGASVRLAVRPEDIRVSPAGNAAnlLLARVEDMEF 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 316 TGAELIASLQVDGIEDACVFC-FPANS---PAIRVGQALRVSVPIGEIHLF 362
Cdd:TIGR03265 302 LGAFYRLRLRLEGLPGQALVAdVSASEverLGIRAGQPIWIELPAERLRAF 352
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-253 |
1.27e-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: 318.03 E-value: 1.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQasaRKVAQSL---GIDGLWERKPAQLSGGQRQRV 160
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLP------------------KAEIK---ERVAEALdlvQLEGYANRKPSQLSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
250
....*....|...
gi 2536923639 241 TRPANLDVARFVG 253
Cdd:cd03300 220 EEPANRFVADFIG 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-234 |
2.66e-106 |
|
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: 311.50 E-value: 2.66e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVP------------------KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-234 |
1.95e-105 |
|
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: 309.06 E-value: 1.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVP------------------KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-367 |
2.48e-95 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 289.24 E-value: 2.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNictpllmrgLGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:PRK11000 81 FQSYALYPHLSVAEN---------MSFGLKLAGAK---------KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 241 TRPANLDVARFVGAPRINLLDGEVKAHGVVWAQGRLVGHSH------GKT----GPCRIAFRPQAgtLESVDGLEV--EG 308
Cdd:PRK11000 223 HYPANRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQvwlpveGRGvqvgANMSLGIRPEH--LLPSDIADVtlEG 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 309 TLVNVEYTGAELIASLQVDGIEDACVFCFPANSPaIRVGQALRVSVPIGEIHLFDADGQ 367
Cdd:PRK11000 301 EVQVVEQLGNETQIHIQIPAIRQNLVYRQNDVVL-VEEGATFAIGLPPERCHLFREDGT 358
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-317 |
2.37e-92 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 280.84 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 9 LTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSYALYP 88
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 89 HMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVR 168
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVP------------------KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 169 RPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDV 248
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFM 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 249 ARFVGAPriNLLDGEVKAHGVVWAQGRLVGHSHGKT----GPCRIAFRPQAGTLESVDGLEVEGTLVNVEYTG 317
Cdd:PRK11432 234 ASFMGDA--NIFPATLSGDYVDIYGYRLPRPAAFAFnlpdGECTVGVRPEAITLSEQGEESQRCTIKHVAYMG 304
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-254 |
1.11e-88 |
|
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: 267.67 E-value: 1.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRglgfwgrlpgaglfSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVK--------------PRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
250
....*....|.
gi 2536923639 244 ANLDVARFVGA 254
Cdd:cd03296 229 ASPFVYSFLGE 239
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
4-362 |
1.78e-88 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 271.10 E-value: 1.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFG----NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdLLA------LSPS 73
Cdd:NF040933 3 VRVENVTKIFKkgkkEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDK-LVAspgkiiVPPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 QRDCAMVFQSYALYPHMTVGGNICTPLLMRglgfwgRLPgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLS 153
Cdd:NF040933 82 DRNIGMVFQNWALYPNMTVFDNIAFPLKIK------KVP------------KDEIEKKVKEVAEILGISEVLDRYPRELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQL 233
Cdd:NF040933 144 GGQQQRVALARALVKNPQVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 234 GTPEEIYTRPANLDVARFVGapRINLLDGEVKAHGVVWAQGRLVGHSHGKTGPCR--IAFRPQAGTLESVDGLEVEGtLV 311
Cdd:NF040933 224 GKPEEIYDNPANIFVARLIG--DINLLEGKVEEEGLVDGNDLKIPLPNPKLEAGEviIGIRPEDIDISESDMRLPPG-FV 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 312 NV--------EYTGAELIASLQVDGIEDACVFCFpANSPaIRVGQALRVSVPIGEIHLF 362
Cdd:NF040933 301 EVgkgrvkvsSYAGGVFRVVVSPIDDDSIEIIVN-SDRP-IEEGEEVNLYVRPDKIKIF 357
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-327 |
8.60e-88 |
|
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: 268.21 E-value: 8.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 34 LLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpg 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 114 aglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGE 193
Cdd:TIGR01187 74 -----------RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 194 IRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDVARFVGAprINLLDGEVKAHGvvwaQ 273
Cdd:TIGR01187 143 LKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERK----S 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 274 GRLVGHShGKTGPCRI--------------AFRPQAGTLESVDGLE----VEGTLVNVEYTGAELIASLQVD 327
Cdd:TIGR01187 217 EQVVLAG-VEGRRCDIytdvpvekdqplhvVLRPEKIVIEEEDEANssnaIIGHVIDITYLGMTLEVHVRLE 287
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-313 |
1.27e-82 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 255.77 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKvIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVP------------------KEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:NF040840 143 RALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 244 ANLDVARFVGAPriNLLDGEVKAHG---VVWAQGRLVGHSHGKTGPCRIAFRPQAGTLES--------------VDGLEV 306
Cdd:NF040840 223 KNEFVARFVGFE--NIIEGVAEKGGegtILDTGNIKIELPEEKKGKVRIGIRPEDITISTekvktsarnefkgkVEEIED 300
|
....*..
gi 2536923639 307 EGTLVNV 313
Cdd:NF040840 301 LGPLVKL 307
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-254 |
4.18e-82 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 250.49 E-value: 4.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRglgfwgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIR------------------KHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:TIGR00968 143 RALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHP 222
|
250
....*....|.
gi 2536923639 244 ANLDVARFVGA 254
Cdd:TIGR00968 223 ANPFVMSFLGE 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-254 |
7.50e-82 |
|
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: 249.95 E-value: 7.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKViKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRglgfwgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKR------------------KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
250
....*....|.
gi 2536923639 244 ANLDVARFVGA 254
Cdd:cd03299 222 KNEFVAEFLGF 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
3.62e-81 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 248.85 E-value: 3.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPsqrD 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVP------------------KAERRERARELLELVGLAGFEDAYPHQLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVM--REGRI 230
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRI 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-265 |
1.51e-77 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 243.07 E-value: 1.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMrglgfwgrLPgaglfsantRRIKAEAQASARKVAQSLGI---DGLWERKPAQLSGGQRQRV 160
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTV--------LP---------RRERPNAAAIKAKVTQLLEMvqlAHLADRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
250 260
....*....|....*....|....*
gi 2536923639 241 TRPANLDVARFVGapRINLLDGEVK 265
Cdd:PRK10851 226 REPATRFVLEFMG--EVNRLQGTIR 248
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-257 |
3.26e-77 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 240.38 E-value: 3.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMV 80
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICT-PLLmrgLGfWGrlpgaglfsantrriKAEAQASARKVAQSLGID--GLWERKPAQLSGGQR 157
Cdd:COG1125 82 IQQIGLFPHMTVAENIATvPRL---LG-WD---------------KERIRARVDELLELVGLDpeEYRDRYPHELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:COG1125 143 QRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPE 222
|
250 260
....*....|....*....|
gi 2536923639 238 EIYTRPANLDVARFVGAPRI 257
Cdd:COG1125 223 EILANPANDFVADFVGADRG 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-232 |
1.11e-75 |
|
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: 233.52 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN----TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdllALSPSQRDCAM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE---PVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQR 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVP------------------KAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVM--REGRILQ 232
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-239 |
2.96e-75 |
|
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: 232.95 E-value: 2.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRD----- 76
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYALYPHMTVGGNICTPLLMRglgfwGRLPgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREH-----TDLS------------EAEIRELVLEKLELVGLPGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
...
gi 2536923639 237 EEI 239
Cdd:COG1127 227 EEL 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-230 |
2.27e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 225.31 E-value: 2.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN----TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRD--- 76
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 ---CAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLS 153
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVS------------------RKERRERARELLERVGLGDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDqHEAMSMSDRVAVMREGRI 230
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-317 |
3.72e-72 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 230.11 E-value: 3.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMV 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICTPLLMrglgfwGRLPgaglfsantrriKAEAQAsarKVAQSLGIDGLWE---RKPAQLSGGQR 157
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQ------DKLP------------KAEIAS---RVNEMLGLVHMQEfakRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 238 EIYTRPANLDVARFVGAprINLLDGEVKAHGvvwaQGRLVGHSHGKTGPCR--------------IAFRPQAGTL-ESV- 301
Cdd:PRK11607 236 EIYEHPTTRYSAEFIGS--VNVFEGVLKERQ----EDGLVIDSPGLVHPLKvdadasvvdnvpvhVALRPEKIMLcEEPp 309
|
330
....*....|....*...
gi 2536923639 302 -DGLEVE-GTLVNVEYTG 317
Cdd:PRK11607 310 aDGCNFAvGEVIHIAYLG 327
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-256 |
2.18e-70 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 220.64 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMV 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNICT-PLLMRglgfWGRlpgaglfsantRRIKAEAQASARKVaqSLGIDGLWERKPAQLSGGQRQR 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALvPKLLK----WPK-----------EKIRERADELLALV--GLDPAEFADRYPHELSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:cd03295 144 VGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*..
gi 2536923639 240 YTRPANLDVARFVGAPR 256
Cdd:cd03295 224 LRSPANDFVAEFVGADR 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-245 |
7.75e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 216.78 E-value: 7.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLG-------ERDLLALspsQRD 76
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDgedltdsKKDINKL---RRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYALYPHMTVGGNIC-TPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGG 155
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTlAPIKVKKMS------------------KAEAEERAMELLERVGLADKADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDAnlrqALRGE----IRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
250
....*....|....
gi 2536923639 232 QLGTPEEIYTRPAN 245
Cdd:COG1126 216 EEGPPEEFFENPQH 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-230 |
4.96e-68 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 213.89 E-value: 4.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN----TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRD--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 ---CAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLS 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVP------------------KKERRERAEELLERVGLGDRLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDqHEAMSMSDRVAVMREGRI 230
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-239 |
8.93e-68 |
|
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: 213.90 E-value: 8.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDCA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNICTPLLMrglgfwgrlpgaglfsaNTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLRE-----------------HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLD---ANLRQALrgeIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGT 235
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
....
gi 2536923639 236 PEEI 239
Cdd:cd03261 221 PEEL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-252 |
1.30e-66 |
|
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: 212.12 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 11 KQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ------RDCAMVFQSY 84
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALAR 164
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVP------------------RAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 165 AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPA 244
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
....*...
gi 2536923639 245 NLDVARFV 252
Cdd:cd03294 254 NDYVREFF 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-229 |
1.49e-66 |
|
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: 208.58 E-value: 1.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALS----PSQRDCAM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNIctpllmrGLGfwgrlpgaglfsantrrikaeaqasarkvaqslgidglwerkpaqLSGGQRQR 159
Cdd:cd03229 81 VFQDFALFPHLTVLENI-------ALG---------------------------------------------LSGGQQQR 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:cd03229 109 VALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-239 |
3.66e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.53 E-value: 3.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNictpllmrgLGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVAL 162
Cdd:COG1131 81 EPALYPDLTVREN---------LRFFARLYGLP---------RKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-254 |
1.92e-65 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 207.69 E-value: 1.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTkvIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQS 83
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNIctpllmrGLGFWGRLpgaglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:COG3840 80 NNLFPHLTVAQNI-------GLGLRPGL-----------KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
250
....*....|.
gi 2536923639 244 ANLDVARFVGA 254
Cdd:COG3840 222 PPPALAAYLGI 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-234 |
2.29e-64 |
|
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: 204.45 E-value: 2.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVrDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL------LALSPSQRDCAMVFQSYALYPHMTVGGN 95
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTpllmrglgfwgrlpGAGLFSANTRRIkaeaqaSARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:cd03297 96 LAF--------------GLKRKRNREDRI------SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 176 DEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-267 |
2.41e-63 |
|
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: 206.49 E-value: 2.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 23 DLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLL------ALSPSQRDCAMVFQSYALYPHMTVGGNI 96
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiFLPPHRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 CtpllmrgLGFWgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFD 176
Cdd:COG4148 99 L-------YGRK-------------RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 177 EPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDVARFVGApr 256
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEA-- 236
|
250
....*....|.
gi 2536923639 257 INLLDGEVKAH 267
Cdd:COG4148 237 GSVLEATVAAH 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-243 |
8.66e-62 |
|
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: 206.68 E-value: 8.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF-----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 -RDCAMVFQ--SYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrrIKAEAQASARKVAQSLGID-GLWERKPA 150
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLL-----------------SRAERRERVAELLERVGLPpDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 151 QLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
250
....*....|...
gi 2536923639 231 LQLGTPEEIYTRP 243
Cdd:COG1123 484 VEDGPTEEVFANP 496
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-246 |
4.52e-61 |
|
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: 197.19 E-value: 4.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTVGGNIctplLMrglgfwGRLPGAGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVA 161
Cdd:COG1120 82 QEPPAPFGLTVRELV----AL------GRYPHLGLF----GRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 162 LARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
....*
gi 2536923639 242 rPANL 246
Cdd:COG1120 228 -PELL 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-239 |
5.15e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.82 E-value: 5.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----R 75
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 DCAMVFQSYALYPHMTVGGNICTpllmrglgfwGRLPGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGG 155
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLA----------GRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLD-ANLRQALRgEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDpKTARQVMD-LLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDG 229
|
....*
gi 2536923639 235 TPEEI 239
Cdd:COG3638 230 PPAEL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-246 |
1.06e-59 |
|
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: 192.93 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQsyalYP-----HMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGG 155
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLP------------------REEIRERVEEALELVGLEHLADRPPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGT 235
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
250
....*....|.
gi 2536923639 236 PEEIYTRPANL 246
Cdd:COG1122 218 PREVFSDYELL 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-234 |
5.55e-58 |
|
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: 188.48 E-value: 5.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN----TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR---- 75
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 -DCAMVFQSY--ALYPHMTVGGNICTPLLmrglgfwgrlpgaglfSANTRRIKAEAQASARKVAQSLGIDGLW-ERKPAQ 151
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLR----------------IHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
...
gi 2536923639 232 QLG 234
Cdd:cd03257 226 EEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-245 |
8.56e-58 |
|
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: 188.47 E-value: 8.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFG----NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDC 77
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSY--ALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrrikaEAQASARKVAQSLGID-GLWERKPAQLSG 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--------------------DREERIAELLEQVGLPpSFLDRYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
250
....*....|.
gi 2536923639 235 TPEEIYTRPAN 245
Cdd:COG1124 222 TVADLLAGPKH 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-230 |
2.20e-57 |
|
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: 186.20 E-value: 2.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLL----ALSPSQRDCAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNIC-TPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITlAPIKVKGMS------------------KAEAEERALELLEKVGLADKADAYPAQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-257 |
4.47e-57 |
|
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: 190.45 E-value: 4.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 11 KQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ------RDCAMVFQSY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALAR 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWP------------------EQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 165 AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPA 244
Cdd:TIGR01186 143 ALAAEPDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPA 222
|
250
....*....|...
gi 2536923639 245 NLDVARFVGAPRI 257
Cdd:TIGR01186 223 NEYVEEFIGKVDL 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-239 |
1.63e-56 |
|
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: 185.63 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRdCAM- 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-ARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 ---VFQSYALYPHMTVGGNICTPLLMR-GLGFWGRLPGAGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGG 155
Cdd:COG0411 81 iarTFQNPRLFPELTVLENVLVAAHARlGRGLLAALLRLPRA----RREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGT 235
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....
gi 2536923639 236 PEEI 239
Cdd:COG0411 237 PAEV 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-256 |
9.76e-56 |
|
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: 190.88 E-value: 9.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQF--GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPD---SGSIRLGERDLLALSPSQR- 75
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 -DCAMVFQS--YALYPhMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQL 152
Cdd:COG1123 83 rRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLS------------------RAEARARVLELLEAVGLERRLDRYPHQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 153 SGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQ 232
Cdd:COG1123 144 SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
250 260
....*....|....*....|....
gi 2536923639 233 LGTPEEIYTRPANLDVARFVGAPR 256
Cdd:COG1123 224 DGPPEEILAAPQALAAVPRLGAAR 247
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-244 |
1.03e-55 |
|
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: 182.64 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRdCAM----VF 81
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI-ARLgigrTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTVGGNICTPLLMRGlgfwgrlpGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVA 161
Cdd:cd03219 82 QIPRLFPELTVLENVMVAAQART--------GSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 162 LARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
...
gi 2536923639 242 RPA 244
Cdd:cd03219 233 NPR 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-229 |
1.44e-55 |
|
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: 181.51 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVFQsyalYP-HM 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ----NPdDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 ----TVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAM 166
Cdd:cd03225 88 ffgpTVEEEVAFGLENLGLP------------------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-230 |
3.24e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 180.40 E-value: 3.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPhMTVGGNICTPLLMRGLGFwgrlpgaglfsantrrikaeAQASARKVAQSLGID-GLWERKPAQLSGGQRQRV 160
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQLRERKF--------------------DRERALELLERLGLPpDILDKPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-242 |
9.01e-55 |
|
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: 180.44 E-value: 9.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMVFQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNIctpllmrglGFWGRLpgAGLFsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVAL 162
Cdd:COG4555 82 ERGLYDRLTVRENI---------RYFAEL--YGLF-------DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-243 |
1.95e-54 |
|
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: 179.31 E-value: 1.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNT----KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ----- 74
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 RDCAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSG 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVP------------------KAEIEERVLELLELVGLEDKADAYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
....*....
gi 2536923639 235 TPEEIYTRP 243
Cdd:cd03258 224 TVEEVFANP 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-277 |
1.44e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 180.27 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ----- 74
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 RDCAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQAsarKVAQSLGIDGLWERK---PAQ 151
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVP------------------KAEIRK---RVAELLELVGLSDKAdayPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDqheamsMS------DRVAVM 225
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE------MDvvrricDRVAVL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 226 REGRILQLGTPEEIYTRPANlDVAR-FVGAPRINLLDGEVKAHGVVWA-QGRLV 277
Cdd:COG1135 215 ENGRIVEQGPVLDVFANPQS-ELTRrFLPTVLNDELPEELLARLREAAgGGRLV 267
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-239 |
3.41e-51 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 170.92 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 23 DLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSYALYPHMTVGGNIctpllm 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNI------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 103 rGLGFWgrlPGAglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNL 182
Cdd:PRK10771 93 -GLGLN---PGL--------KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 183 DANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-234 |
3.44e-51 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 170.43 E-value: 3.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 23 DLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSYALYPHMTVGGNIctpllm 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNI------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 103 rGLGFwgrLPGAglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNL 182
Cdd:TIGR01277 92 -GLGL---HPGL--------KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 183 DANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-243 |
4.76e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 171.52 E-value: 4.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GER---------DLLALS 71
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEEirlkpdrdgELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 72 PSQRD-----CAMVFQSYALYPHMTVGGNIC-TPllMRGLGfwgrlpgaglfsantrRIKAEAQASAR----KVaqslgi 141
Cdd:COG4598 87 RRQLQrirtrLGMVFQSFNLWSHMTVLENVIeAP--VHVLG----------------RPKAEAIERAEallaKV------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 142 dGLWERK---PAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSM 218
Cdd:COG4598 143 -GLADKRdayPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDV 220
|
250 260
....*....|....*....|....*
gi 2536923639 219 SDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:COG4598 221 SSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-230 |
5.52e-51 |
|
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: 169.60 E-value: 5.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSYALYPHMTVGGNIctpll 101
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNV----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 102 mrGLGfwgRLPGAglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSN 181
Cdd:cd03298 92 --GLG---LSPGL--------KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2536923639 182 LDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-246 |
7.18e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.65 E-value: 7.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLlalSPSQRDCAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMtvggnictPLLMR---GLGFWGRLpgaGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQR 157
Cdd:COG1121 81 PQRAEVDWDF--------PITVRdvvLMGRYGRR---GLF----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMReGRILQLGTPE 237
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPE 223
|
....*....
gi 2536923639 238 EIYTrPANL 246
Cdd:COG1121 224 EVLT-PENL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-239 |
1.45e-50 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 169.67 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDC 77
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNICTPLLMRgLGFWgrlpgAGLFSANTRRIKAEAQASARKVaqslGIDGLWERKPAQLSGGQR 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGR-RSTW-----RSLFGLFPKEEKQRALAALERV----GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
..
gi 2536923639 238 EI 239
Cdd:cd03256 231 EL 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-232 |
2.69e-50 |
|
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: 168.77 E-value: 2.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR---- 75
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 --DCAMVFQSYALYPHMTVGGNICTPLLMRGlgfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLS 153
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLELAG--------------------RRDARARARALLERVGLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAmSMSDRVAVMREGRILQ 232
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-244 |
3.54e-50 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 171.00 E-value: 3.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQP---DSGSIRLGERDLLALSPSQ-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 ----RDCAMVFQ-SY-ALYPHMTVGGNICTPLLM-RGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWER 147
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLS------------------KAEARERAIELLERVGLPDPERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 K---PAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLR-QALRgEIRQLHDQLGVTFIYVTHDqheaMS----MS 219
Cdd:COG0444 144 LdryPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQaQILN-LLKDLQRELGLAILFITHD----LGvvaeIA 218
|
250 260
....*....|....*....|....*
gi 2536923639 220 DRVAVMREGRILQLGTPEEIYTRPA 244
Cdd:COG0444 219 DRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-230 |
8.52e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.77 E-value: 8.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDC 77
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNICTPLLMRGlgfwgrlpgaglfsANTRRIKAEAQASARKVaqslGIDGLWERKPAQLSGGQR 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTG--------------KSRKEIRRRVREVLDLV----GLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALrgeIRQLHD--QLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-230 |
1.49e-49 |
|
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: 164.49 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNIctpllmrglgfwgrlpgaglfsantrrikaeaqasarkvaqslgidglwerkpaQLSGGQRQRVAL 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-243 |
5.84e-49 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 164.95 E-value: 5.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPsqrDCAMVFQSYALYPHMTVGGNIct 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 99 pllmrglgfwgrlpGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEP 178
Cdd:TIGR01184 76 --------------ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 179 LSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI-YTRP 243
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-245 |
7.42e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 165.27 E-value: 7.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR----DCAM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNIC-TPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVaqsLGIDGLWERK---PAQLSGG 155
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMfGPLRVRGAS------------------KEEAEKQAREL---LAKVGLAERAhhyPSELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGT 235
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
250
....*....|
gi 2536923639 236 PEEIYTRPAN 245
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-264 |
7.96e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 165.62 E-value: 7.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGErdlLALSPSQRDCAMVFQSYA 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 86 LYPHMTVGGNIctpllmrGLGfwgrlpgaglfsantrrIKAEAQASARkvaQSLGIDGLWERK---PAQLSGGQRQRVAL 162
Cdd:PRK11247 92 LLPWKKVIDNV-------GLG-----------------LKGQWRDAAL---QALAAVGLADRAnewPAALSGGQKQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI---LQLGTPeei 239
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLP--- 221
|
250 260
....*....|....*....|....*
gi 2536923639 240 ytRPanldvaRFVGAPRINLLDGEV 264
Cdd:PRK11247 222 --RP------RRRGSARLAELEAEV 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-243 |
1.40e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 159.53 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA---LSPSQR-- 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQQKGli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 -----DCAMVFQSYALYPHMTVGGNICT-PLLMRGlgfwgrlpgaglfsantrRIKAEAQASARKVAQSLGIDGLWERKP 149
Cdd:PRK11264 81 rqlrqHVGFVFQNFNLFPHRTVLENIIEgPVIVKG------------------EPKEEATARARELLAKVGLAGKETSYP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
250
....*....|....
gi 2536923639 230 ILQLGTPEEIYTRP 243
Cdd:PRK11264 222 IVEQGPAKALFADP 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-238 |
2.22e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 157.64 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPD---SGSIRLGERDLLALSPSQRDCAMVFQSYALYPHMTVGGN 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICtpllmrglgfwgrlpgaglFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:COG4136 97 LA-------------------FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 176 DEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDqheamsMSDRVAVmreGRILQLGTPEE 238
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD------EEDAPAA---GRVLDLGNWQH 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-269 |
2.38e-46 |
|
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: 159.52 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF--GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGerDLLALSPSQ-----RD 76
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENlweirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSyalyP-HMTVGG-----------NICTPL-LMRglgfwgrlpgaglfsantRRIKaeaqasarKVAQSLGIDG 143
Cdd:TIGR04520 79 VGMVFQN----PdNQFVGAtveddvafgleNLGVPReEMR------------------KRVD--------EALKLVGMED 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 144 LWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMsMSDRVA 223
Cdd:TIGR04520 129 FRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVI 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 224 VMREGRILQLGTPEEIYTRP-----ANLDVarfvgaPRINLLDGEVKAHGV 269
Cdd:TIGR04520 208 VMNKGKIVAEGTPREIFSQVellkeIGLDV------PFITELAKALKKRGI 252
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-239 |
2.73e-46 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.11 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGL-----DQPDSGSIRLGERDLLALSPS----Q 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 RDCAMVFQSYALYPhMTVGGNICTPLlmrglgfwgRLpgaglfsantRRIKAEAQASARkVAQSLGIDGLWER-----KP 149
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL---------RL----------HGIKLKEELDER-VEEALRKAALWDEvkdrlHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlgVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:cd03260 140 LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
250
....*....|
gi 2536923639 230 ILQLGTPEEI 239
Cdd:cd03260 218 LVEFGPTEQI 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
6-244 |
5.68e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 160.28 E-value: 5.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQF--------GNTKVIK---GLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ 74
Cdd:COG4608 10 VRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 -----RDCAMVFQ-SYA-LYPHMTVGGNICTPLLMRGLGfwgrlpgaglfSANTRRikaeaqasaRKVAQSLGIDGL--- 144
Cdd:COG4608 90 lrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLA-----------SKAERR---------ERVAELLELVGLrpe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 145 -WERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDA-------NLrqalrgeIRQLHDQLGVTFIYVTHD----Q 212
Cdd:COG4608 150 hADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqaqvlNL-------LEDLQDELGLTYLFISHDlsvvR 222
|
250 260 270
....*....|....*....|....*....|..
gi 2536923639 213 HeamsMSDRVAVMREGRILQLGTPEEIYTRPA 244
Cdd:COG4608 223 H----ISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-277 |
1.04e-45 |
|
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: 160.28 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL------LALSPSQRDCAMVFQSYALYPHMTVGGN 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ictplLMRGLgfwgrlpgaglfsanTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:TIGR02142 96 -----LRYGM---------------KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 176 DEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDVARfvgAP 255
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR---ED 232
|
250 260
....*....|....*....|....*....
gi 2536923639 256 RINLLDGEVKAH-------GVVWAQGRLV 277
Cdd:TIGR02142 233 QGSLIEGVVAEHdqhygltALRLGGGHLW 261
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
1.17e-45 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 157.33 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTK----VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPsqrD 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVP------------------KAERRARAEELLALVGLADFARRRIWQLSGGM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVM--REGRI 230
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-235 |
1.21e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSG-----------SIRLGERDLLALsp 72
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlniagnhfdfSKTPSDKAIREL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 73 sQRDCAMVFQSYALYPHMTVGGN-ICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQ 151
Cdd:PRK11124 81 -RRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLS------------------KDQALARAEKLLERLRLKPYADRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
....
gi 2536923639 232 QLGT 235
Cdd:PRK11124 221 EQGD 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-246 |
1.81e-45 |
|
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: 157.23 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA-----LSPSQRDCAMVFQsyalYPHM 90
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkkLKDLRKKVGLVFQ----FPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 -----TVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGID-GLWERKPAQLSGGQRQRVALAR 164
Cdd:TIGR04521 94 qlfeeTVYKDIAFGPKNLGLS------------------EEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 165 AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPA 244
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
..
gi 2536923639 245 NL 246
Cdd:TIGR04521 236 EL 237
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-234 |
2.71e-45 |
|
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: 153.75 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFqsya 85
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 86 lyphmtvggnictpllmrglgfwgrLPgaglfsantrrikaeaQASARkvaqsLGIDGLWERKPAQLSGGQRQRVALARA 165
Cdd:cd03214 78 -------------------------VP----------------QALEL-----LGLAHLADRPFNELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 166 MVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-215 |
5.19e-45 |
|
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: 153.79 E-value: 5.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNictpllmrgLGFWGRLPGAglfsantrrikAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:COG4133 81 GHADGLKPELTVREN---------LRFWAALYGL-----------RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQlHDQLGVTFIYVTHDQHEA 215
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-243 |
8.78e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 8.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSI-----------RLGERDLLALsp 72
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdfsqKPSEKAIRLL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 73 sQRDCAMVFQSYALYPHMTVGGN-ICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQ 151
Cdd:COG4161 81 -RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLS------------------KEQAREKAMKLLARLRLTDKADRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLhDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
250
....*....|..
gi 2536923639 232 QLGTpEEIYTRP 243
Cdd:COG4161 221 EQGD-ASHFTQP 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-229 |
1.30e-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: 151.24 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 5 HISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 syalyphmtvggnictpllmrglgfwgrlpgaglfsantrrikaeaqasarkvaqslgidglwerkpaqLSGGQRQRVAL 162
Cdd:cd00267 81 ---------------------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-230 |
2.90e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.80 E-value: 2.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RDC--AMVFQ 82
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAgiAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNIctpllmrglgFWGRLPGAGLFsANTRRIKAEaqasARKVAQSLGIDGLWERKPAQLSGGQRQRVAL 162
Cdd:COG1129 87 ELNLVPNLSVAENI----------FLGREPRRGGL-IDWRAMRRR----ARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-241 |
2.34e-43 |
|
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: 150.91 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALS-----PSQRDC 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNICTPLLMRgLGFWgrlpgAGLFSANTRRIKAEAQASARKVaqslGIDGLWERKPAQLSGGQR 157
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGY-KPTW-----RSLLGRFSEEDKERALSALERV----GLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
....
gi 2536923639 238 EIYT 241
Cdd:TIGR02315 232 ELDD 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-229 |
1.13e-42 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 146.76 E-value: 1.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNT--KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAM 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYpHMTVGGNIctpllmrglgfwgrlpgaglfsantrrikaeaqasarkvaqslgidglwerkpaqLSGGQRQR 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------------------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDqHEAMSMSDRVAVMREGR 229
Cdd:cd03228 105 IAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-230 |
1.14e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 148.27 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR------DCAMVFQSYALYPH 89
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:TIGR02211 98 FTALENVAMPLLIGKKS------------------VKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMsDRVAVMREGRI 230
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-229 |
1.36e-42 |
|
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: 147.78 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDC 77
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsanTRRIKAEAQASARKVaqslgidGLWERK---PAQLSG 154
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKK--------------EREIQRRVGAALRQV-------GLEHKAdafPEQLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:TIGR02673 141 GEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-222 |
1.49e-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: 147.38 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RD-CAM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNICTPLlmrglgfwgrlpgaglfsANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQR 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGL------------------KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQhEAMSMSDRV 222
Cdd:TIGR03608 143 VALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-239 |
5.57e-42 |
|
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: 156.15 E-value: 5.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFG--NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDC 77
Cdd:COG2274 472 GDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYpHMTVGGNICtpllmrglgfwgrlpgAGLFSANTRRIkaeaqasaRKVAQSLGIDGLWERKP-------- 149
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENIT----------------LGDPDATDEEI--------IEAARLAGLHDFIEALPmgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 ---AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDqHEAMSMSDRVAVMR 226
Cdd:COG2274 607 eggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLD 683
|
250
....*....|...
gi 2536923639 227 EGRILQLGTPEEI 239
Cdd:COG2274 684 KGRIVEDGTHEEL 696
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-243 |
8.20e-42 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 147.28 E-value: 8.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GER--------------DLL 68
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQlyhmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 69 ALSPSQRDCAMVFQSYALYPHMTVGGNIC-TPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWER 147
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTeAPVLVLGMA------------------RAEAEKRAMELLDMVGLADKADH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 KPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMRE 227
Cdd:TIGR03005 143 MPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDK 222
|
250
....*....|....*.
gi 2536923639 228 GRILQLGTPEEIYTRP 243
Cdd:TIGR03005 223 GRIVEQGKPDEIFRQP 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-234 |
1.47e-41 |
|
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: 145.20 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTK----VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GERDLLALSPSQRDCA 78
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNictpllmrgLGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:cd03266 82 FVSDSTGLYDRLTAREN---------LEYFAGLYGLK---------GDELTARLEELADRLGMEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
2.48e-41 |
|
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: 142.95 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQrdcamvfqsya 85
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 86 lyphmtvggnictpllmrglgfwgrlpgaglfsantrrikaeaqasarkvAQSLGIdglweRKPAQLSGGQRQRVALARA 165
Cdd:cd03216 72 --------------------------------------------------ARRAGI-----AMVYQLSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 166 MVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-243 |
7.59e-41 |
|
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: 150.99 E-value: 7.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 9 LTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPDSGSIRLGERDLLALSPSQ-----RDCAMVFQS 83
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 -YA-LYPHMTVGGNICTPLlmrglgfwgRLPGAGLfSANTRRikaeaqasaRKVAQSL---GID-GLWERKPAQLSGGQR 157
Cdd:COG4172 371 pFGsLSPRMTVGQIIAEGL---------RVHGPGL-SAAERR---------ARVAEALeevGLDpAARHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE 511
|
....*.
gi 2536923639 238 EIYTRP 243
Cdd:COG4172 512 QVFDAP 517
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
1.88e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 144.06 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQF---------GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALS 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 72 PSQ-----RDCAMVFQSY--ALYPHMTVGGNICTPllMRGLgfwgrlpgaglfsanTRRIKAEAQASARKVAQSLGID-G 143
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREP--LRHL---------------LSLDKAERLARASEMLRAVDLDdS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 144 LWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVA 223
Cdd:PRK10419 144 VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVM 223
|
....*....
gi 2536923639 224 VMREGRILQ 232
Cdd:PRK10419 224 VMDNGQIVE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-254 |
2.13e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 145.71 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF-GNTKVIKGLD---LTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ----- 74
Cdd:PRK11153 2 IELKNISKVFpQGGRTIHALNnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 RDCAMVFQSYALYPHMTVGGNICTPLlmrglgfwgRLpgaglfsANTRriKAEAQAsarKVAQSLGIDGLWERK---PAQ 151
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPL---------EL-------AGTP--KAEIKA---RVTELLELVGLSDKAdryPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250 260
....*....|....*....|....
gi 2536923639 232 QLGTPEEIYTRPANlDVAR-FVGA 254
Cdd:PRK11153 221 EQGTVSEVFSHPKH-PLTReFIQS 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
7-232 |
2.34e-40 |
|
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: 143.79 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 7 SGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDCAMVF 81
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 Q-SY-ALYPHMTVGGNICTPllMRGLgfwgrlpgaglfsanTRRIKAEAQASARKVAQSLGIDG-LWERKPAQLSGGQRQ 158
Cdd:TIGR02769 95 QdSPsAVNPRMTVRQIIGEP--LRHL---------------TSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQ 232
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-246 |
2.76e-40 |
|
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: 142.92 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSG-SIR-LGER----DLLAL------- 70
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGERrggeDVWELrkriglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 71 SPSqrdcamvFQSYaLYPHMTVGGNICTpllmrglGFWGRLpgaGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPA 150
Cdd:COG1119 84 SPA-------LQLR-FPRDETVLDVVLS-------GFFDSI---GLY----REPTDEQRERARELLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 151 QLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|....*.
gi 2536923639 231 LQLGTPEEIYTrPANL 246
Cdd:COG1119 222 VAAGPKEEVLT-SENL 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-239 |
3.87e-40 |
|
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: 141.49 E-value: 3.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN--TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLalspSQRDCA--- 78
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAArqs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 --MVFQSYALYPHMTVggnictpllMRGLGFWGRLPGaglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:cd03263 77 lgYCPQFDALFDELTV---------REHLRFYARLKG---------LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRqalrgeiRQLHD-----QLGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASR-------RAIWDlilevRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
....*...
gi 2536923639 232 QLGTPEEI 239
Cdd:cd03263 212 CIGSPQEL 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-234 |
7.66e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 140.75 E-value: 7.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 5 HISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDllaLSPSQRDCAMVFQSY 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP---LEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALyphmtvggNICTPLLMRGLGFWGRLPGAGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALAR 164
Cdd:cd03235 78 SI--------DRDFPISVRDVVLMGLYGHKGLF----RRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 165 AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMrEGRILQLG 234
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-238 |
1.74e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.00 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RDC-AMVFQSYALYpHMT 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRRQiGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNICtpllmrglgfWGRlPGAglfsanTRR--IKAEAQASARKVAQSL--GIDGLWERKPAQLSGGQRQRVALARAMV 167
Cdd:COG1132 430 IRENIR----------YGR-PDA------TDEevEEAAKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 168 RRPAVFLFDEPLSNLD----ANLRQALRGEIRqlhdqlGVTFIYVTHDQHEAMSMsDRVAVMREGRILQLGTPEE 238
Cdd:COG1132 493 KDPPILILDEATSALDteteALIQEALERLMK------GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEE 560
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-241 |
2.19e-39 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 140.92 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 3 DIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQrdcamVFQ 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYP--HMTVGGNICTPLLMRG----LGFWGRLPGaglfsantrrikaEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:PRK11231 77 RLALLPqhHLTPEGITVRELVAYGrspwLSLWGRLSA-------------EDNARVNQAMEQTRINHLADRRLTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
....*
gi 2536923639 237 EEIYT 241
Cdd:PRK11231 223 EEVMT 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-180 |
5.11e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 136.62 E-value: 5.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA--LSPSQRDCAMVFQSYALYPHMTVGGNI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 CTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERK----PAQLSGGQRQRVALARAMVRRPAV 172
Cdd:pfam00005 81 RLGLLLKGLS------------------KREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKL 142
|
....*...
gi 2536923639 173 FLFDEPLS 180
Cdd:pfam00005 143 LLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-238 |
3.27e-38 |
|
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: 144.13 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTK-VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCA 78
Cdd:COG4988 335 PSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALyPHMTVGGNICtpllmrgLGfwgrLPGAGlfsantrriKAEAQASARKVaqslGIDGLWERKP--------- 149
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLR-------LG----RPDAS---------DEELEAALEAA----GLDEFVAALPdgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 --AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDQHEAMSMsDRVAVMRE 227
Cdd:COG4988 470 ggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDD 546
|
250
....*....|.
gi 2536923639 228 GRILQLGTPEE 238
Cdd:COG4988 547 GRIVEQGTHEE 557
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-243 |
7.05e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 136.89 E-value: 7.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTK---------VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALS 71
Cdd:COG4167 2 SALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 72 PSQRdCA---MVFQ--SYALYPHMTVGGNICTPLlmrglgfwgRLpgaglfsaNTrriKAEAQASARKVAQSLGIDGL-- 144
Cdd:COG4167 82 YKYR-CKhirMIFQdpNTSLNPRLNIGQILEEPL---------RL--------NT---DLTAEEREERIFATLRLVGLlp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 145 --WERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHD----QHeamsM 218
Cdd:COG4167 141 ehANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHlgivKH----I 216
|
250 260
....*....|....*....|....*
gi 2536923639 219 SDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:COG4167 217 SDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-252 |
7.54e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 137.02 E-value: 7.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS---------- 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 -----QRDCAMVFQSYALYPHMTVGGNIC-TPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWER 147
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLS------------------KQEARERAVKYLAKVGIDERAQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 K-PAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANlrqaLRGEIRQLHDQL---GVTFIYVTHDQHEAMSMSDRVA 223
Cdd:PRK10619 148 KyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVI 223
|
250 260
....*....|....*....|....*....
gi 2536923639 224 VMREGRILQLGTPEEIYTRPANLDVARFV 252
Cdd:PRK10619 224 FLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-251 |
7.89e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 140.55 E-value: 7.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ------RDCAMVFQSYALYPHMTV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAV 172
Cdd:PRK10070 124 LDNTAFGMELAGIN------------------AEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 173 FLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDVARF 251
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-244 |
8.97e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 142.98 E-value: 8.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQF--GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDC 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYpHMTVGGNIctpLLMRglgfwgrlPGAGlfsantrriKAEAQASARKVaqslGIDGLWERKP-------- 149
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENL---RLAR--------PDAT---------DEELWAALERV----GLGDWLAALPdgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 ---AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQ-LHDQlgvTFIYVTHDQhEAMSMSDRVAVM 225
Cdd:COG4987 467 eggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGR---TVLLITHRL-AGLERMDRILVL 542
|
250
....*....|....*....
gi 2536923639 226 REGRILQLGTPEEIYTRPA 244
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNG 561
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-234 |
1.41e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 134.72 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LGE------RDLLALSPSQRd 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfDGKpldiaaRNRIGYLPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 camvfqsyALYPHMTVGGNictpllmrgLGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:cd03269 80 --------GLYPKMKVIDQ---------LVYLAQLKGLK---------KEEARRRIDEWLERLELSEYANKRVEELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-239 |
2.81e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.39 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GERdllaLSPSQRDCAmvfq 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEP----LDPEDRRRI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SY-----ALYPHMTVGGNictpllmrgLGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQR 157
Cdd:COG4152 74 GYlpeerGLYPKMKVGEQ---------LVYLARLKGLS---------KAEAKRRADEWLERLGLGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLD---ANLrqaLRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*
gi 2536923639 235 TPEEI 239
Cdd:COG4152 212 SVDEI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-239 |
2.91e-37 |
|
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: 134.10 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR---DCAMVFQ 82
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNictpLLMrglgfwgrlpGAglfsanTRRIKAEAQASarkvaqslgIDGLWERKPA----------QL 152
Cdd:cd03224 83 GRRIFPELTVEEN----LLL----------GA------YARRRAKRKAR---------LERVYELFPRlkerrkqlagTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 153 SGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQ 232
Cdd:cd03224 134 SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVL 212
|
....*..
gi 2536923639 233 LGTPEEI 239
Cdd:cd03224 213 EGTAAEL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-246 |
6.70e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.09 E-value: 6.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDC--AMVF 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARrrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYAL---YPHMTVggnictpLLMrglgfwGRLPGaglfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:COG4559 82 QHSSLafpFTVEEV-------VAL------GRAPH--------GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAM------VRRPAVFLF-DEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:COG4559 141 RVQLARVLaqlwepVDGGPRWLFlDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
250
....*....|....*
gi 2536923639 232 QLGTPEEIYTrPANL 246
Cdd:COG4559 220 AQGTPEEVLT-DELL 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-230 |
1.49e-36 |
|
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: 132.15 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDC 77
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNICTPLlmrglgfwgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERK---PAQLSG 154
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAL---------------------EVTGVPPREIRKRVPAALELVGLSHKHralPAELSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-239 |
1.81e-36 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 138.78 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGS--IRLGER--DLLALSPSQRDCA-----MVFQSY 84
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDGRGRAkryigILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHMTVGGNictplLMRGLGFwgRLPgaglfsantrriKAEAQASARKVAQSLGID-----GLWERKPAQLSGGQRQR 159
Cdd:TIGR03269 375 DLYPHRTVLDN-----LTEAIGL--ELP------------DELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-239 |
2.44e-36 |
|
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: 131.72 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNictpLLMRGlGFWGrLPGAGLfsantrrikaeaqasARKVAQSLGIDGLWE---RKPAQLSGGQRQR 159
Cdd:cd03265 81 DLSVDDELTGWEN----LYIHA-RLYG-VPGAER---------------RERIDELLDFVGLLEaadRLVKTYSGGMRRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-229 |
3.29e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.85 E-value: 3.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RDC-- 77
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNIctpLLmrglgfwGRLPGAGLFSAntrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQR 157
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENI---VL-------GLEPTKGGRLD-----RKAARARIRELSERYGLDVDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-243 |
7.23e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 133.68 E-value: 7.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR-----DCAMVFQS--YALYPH 89
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNICTPLLMrglgFWGRLPGAglfsantrRIKAEAQASARKVAQslgIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:PRK15079 115 MTIGEIIAEPLRT----YHPKLSRQ--------EVKDRVKAMMLKVGL---LPNLINRYPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-232 |
2.53e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 129.55 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQF--GN--TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS---- 73
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakae 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 --QRDCAMVFQSYALYPHMTVGGNICTPLLMRGlgfwgrlpgaglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQ 151
Cdd:PRK11629 84 lrNQKLGFIYQFHHLLPDFTALENVAMPLLIGK------------------KKPAEINSRALEMLAAVGLEHRANHRPSE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAvMREGRIL 231
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLT 224
|
.
gi 2536923639 232 Q 232
Cdd:PRK11629 225 A 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-240 |
3.08e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTK--VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdllALSPS-----Q 74
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEEtvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 RDCAMVFQSyalyPH-----MTVGGNICTPLLMRGLgfwgrlPGAGLfsanTRRIkaeaQASARKVaqslGIDGLWERKP 149
Cdd:PRK13635 81 RQVGMVFQN----PDnqfvgATVQDDVAFGLENIGV------PREEM----VERV----DQALRQV----GMEDFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSmSDRVAVMREGR 229
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250
....*....|.
gi 2536923639 230 ILQLGTPEEIY 240
Cdd:PRK13635 218 ILEEGTPEEIF 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-246 |
4.94e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 130.14 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA------LSPSQRDCAMVFQsyalYP-HM- 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKPLRKKVGIVFQ----FPeHQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 ---TVGGNICtpllmrglgFwgrlpGAGLFSANtrriKAEAQASARKVAQSLGID-GLWERKPAQLSGGQRQRVALARAM 166
Cdd:PRK13634 99 feeTVEKDIC---------F-----GPMNFGVS----EEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANL 246
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-244 |
5.02e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 131.92 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 9 LTKQFGNtkvikgLDLTVRdgefLTL--------LGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL------LALSPSQ 74
Cdd:PRK11144 6 FKQQLGD------LCLTVN----LTLpaqgitaiFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgICLPPEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 RDCAMVFQSYALYPHMTVGGNICtpllmrglgfWGrlpgaglfsantrrIKAEAQASARKVAQSLGIDGLWERKPAQLSG 154
Cdd:PRK11144 76 RRIGYVFQDARLFPHYKVRGNLR----------YG--------------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:PRK11144 132 GEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
250
....*....|
gi 2536923639 235 TPEEIYTRPA 244
Cdd:PRK11144 212 PLEEVWASSA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-244 |
5.50e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 134.81 E-value: 5.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGN----TKVIKGLDLTVRDGEFLTLLGSSGCGKS----TLLKLIAGLDQPDSGSIRLGERDLLALSP 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 73 SQ------RDCAMVFQ--SYALYPHMTVGGNICTPL-LMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDG 143
Cdd:COG4172 84 RElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLrLHRGLS------------------GAAARARALELLERVGIPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 144 LwERK----PAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLrQAlrgEI----RQLHDQLGVTFIYVTHDQHEA 215
Cdd:COG4172 146 P-ERRldayPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-QA---QIldllKDLQRELGMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*....
gi 2536923639 216 MSMSDRVAVMREGRILQLGTPEEIYTRPA 244
Cdd:COG4172 221 RRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-244 |
7.24e-35 |
|
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: 128.18 E-value: 7.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR---DC 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNictpLLMrglgfwgrlpgaglfSANTRRIKAEAQASARKVAQSLGIdgLWERK--PA-QLSG 154
Cdd:COG0410 81 GYVPEGRRIFPSLTVEEN----LLL---------------GAYARRDRAEVRADLERVYELFPR--LKERRrqRAgTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
250
....*....|
gi 2536923639 235 TPEEIYTRPA 244
Cdd:COG0410 219 TAAELLADPE 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-246 |
7.59e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.74 E-value: 7.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRdcAmvfQS 83
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL--A---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYP-HMTVGgnicTPLLMR---GLgfwGRLPGAGLfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQR 159
Cdd:PRK13548 78 RAVLPqHSSLS----FPFTVEevvAM---GRAPHGLS--------RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVR------RPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQL 233
Cdd:PRK13548 143 VQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
250
....*....|...
gi 2536923639 234 GTPEEIYTrPANL 246
Cdd:PRK13548 223 GTPAEVLT-PETL 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-232 |
8.16e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 128.66 E-value: 8.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdllALSPSQRDCAMVFQS 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVE------------------KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMR--EGRILQ 232
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVE 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-244 |
1.02e-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: 127.66 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRdcAMVFQSY- 84
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR--ARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ----ALYPHMTVGGNICTPLLMRGLgfwgrlpgaglfSANTRRIKAEAqasarkVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:cd03218 81 pqeaSIFRKLTVEENILAVLEIRGL------------SKKEREEKLEE------LLEEFHITHLRKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQ-LGVtFIyVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGV-LI-TDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
....*
gi 2536923639 240 YTRPA 244
Cdd:cd03218 221 AANEL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-243 |
1.18e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 128.28 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTVggnictpllmRGL-GFwGRLP---GaglfsantrRIKAEAQasaRKVAQS---LGIDGLWERKPAQLSG 154
Cdd:COG4604 82 QENHINSRLTV----------RELvAF-GRFPyskG---------RLTAEDR---EIIDEAiayLDLEDLADRYLDELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*....
gi 2536923639 235 TPEEIYTRP 243
Cdd:COG4604 219 TPEEIITPE 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-230 |
1.40e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 126.60 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 5 HISGLTKQFG-NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLlALSPSQRDCAMVFQS 83
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 yalyphmtvggnictpllmrglgfwgrlPGAGLFSANTRR-------IKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:cd03226 80 ----------------------------VDYQLFTDSVREelllglkELDAGNEQAETVLKDLDLYALKERHPLSLSGGQ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03226 132 KQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-243 |
4.02e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.03 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALsPSQRDCAM----VF 81
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMgvvrTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTVGGNIC--------TPLLmrglgfwgrlpgAGLF-SANTRRIKAEAQASARKVAQSLGIDGLWERKPAQL 152
Cdd:PRK11300 87 QHVRLFREMTVIENLLvaqhqqlkTGLF------------SGLLkTPAFRRAESEALDRAATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 153 SGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQ 232
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
250
....*....|.
gi 2536923639 233 LGTPEEIYTRP 243
Cdd:PRK11300 235 NGTPEEIRNNP 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-222 |
6.64e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 124.27 E-value: 6.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFqsyalyphmtv 92
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSL----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 ggnictPLLMRGL---GFWGRLpgaGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:NF040873 71 ------PLTVRDLvamGRWARR---GLW----RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRV 222
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-243 |
1.32e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 126.03 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDCA 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNICTPLLMRglgfwGRLPGAGLFSanTRRIKAEAqasarkvaqsLGIDGLWERKPAQLSGGQRQ 158
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREH-----TQLPAPLLHS--TVMMKLEA----------VGLRGAAKLMPSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
....*
gi 2536923639 239 IYTRP 243
Cdd:PRK11831 231 LQANP 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-269 |
1.68e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.93 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL----LALSPSQRDCAMVFQ--SYALYPH 89
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 mTVGGNICTPLLMRGLgfwgrlpgaglfsaNTRRIKAEAQASARKVAqsLGIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:PRK13637 100 -TIEKDIAFGPINLGL--------------SEEEIENRVKRAMNIVG--LDYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTrpaNLDVA 249
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK---EVETL 239
|
250 260
....*....|....*....|..
gi 2536923639 250 RFVG--APRINLLDGEVKAHGV 269
Cdd:PRK13637 240 ESIGlaVPQVTYLVRKLRKKGF 261
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-234 |
2.11e-33 |
|
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: 123.46 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGeFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRD-CAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVggnictpllMRGLGFWGRLPGAglfsaNTRRIKAEAQASARKVaqslgidGLWER---KPAQLSGGQRQR 159
Cdd:cd03264 80 EFGVYPNFTV---------REFLDYIAWLKGI-----PSKEVKARVDEVLELV-------NLGDRakkKIGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-239 |
2.16e-33 |
|
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: 130.64 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQrdcamvfqsyaLYPHM------- 90
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE-----------LGRHIgylpqdv 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 -----TVGGNICtpllmrglgfwgRLPgaglfsantrrikaeaQASARKV---AQSLGIDGLWERKP-----------AQ 151
Cdd:COG4618 416 elfdgTIAENIA------------RFG----------------DADPEKVvaaAKLAGVHEMILRLPdgydtrigeggAR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHeAMSMSDRVAVMREGRIL 231
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
....*...
gi 2536923639 232 QLGTPEEI 239
Cdd:COG4618 546 AFGPRDEV 553
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-253 |
2.22e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.42 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVggnictpllmRGLGFWGRLPGAGLFSANTrriKAEAQASARKVAQSlGIDGLWERKPAQLSGGQRQ 158
Cdd:PRK09536 81 SVPQDTSLSFEFDV----------RQVVEMGRTPHRSRFDTWT---ETDRAAVERAMERT-GVAQFADRPVTSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
250
....*....|....*...
gi 2536923639 239 IYTRP---ANLDVARFVG 253
Cdd:PRK09536 226 VLTADtlrAAFDARTAVG 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-243 |
4.82e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.85 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDCAMVFQ 82
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 S-YA-LYPHMTVGGNICTPLLMrglgfwgrlpgaglfsaNTRRIKAEaqaSARKVAQSLGIDGL----WERKPAQLSGGQ 156
Cdd:PRK11308 100 NpYGsLNPRKKVGQILEEPLLI-----------------NTSLSAAE---RREKALAMMAKVGLrpehYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHD----QHEAmsmsDRVAVMREGRILQ 232
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDlsvvEHIA----DEVMVMYLGRCVE 235
|
250
....*....|.
gi 2536923639 233 LGTPEEIYTRP 243
Cdd:PRK11308 236 KGTKEQIFNNP 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-230 |
8.34e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 123.66 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGN-----TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR--D 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYAL--YPHMTVGGNictpLLM---RGLGFwgrlpgaGLFSANTRRIKAEAQASARkvaqSLGIdGLWER---K 148
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEEN----LALayrRGKRR-------GLRRGLTKKRRELFRELLA----TLGL-GLENRldtK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 149 PAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLD---ANLrqalrgeIRQLHDQL----GVTFIYVTHDQHEAMSMSDR 221
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAAL-------VLELTEKIveenNLTTLMVTHNMEQALDYGNR 218
|
....*....
gi 2536923639 222 VAVMREGRI 230
Cdd:COG1101 219 LIMMHEGRI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-251 |
1.01e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR----- 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 ----DCAMVFQsyalypHMTVGGNICTPLLMRGLgfwgrlpgaglfSANTRRIKAEAqasarkVAQSLGIDGLWERKPAQ 151
Cdd:COG1137 81 gylpQEASIFR------KLTVEDNILAVLELRKL------------SKKEREERLEE------LLEEFGITHLRKSKAYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLD----ANLRQalrgEIRQLHDQ-LGVtFIyvT-HDQHEAMSMSDRVAVM 225
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpiavADIQK----IIRHLKERgIGV-LI--TdHNVRETLGICDRAYII 209
|
250 260
....*....|....*....|....*.
gi 2536923639 226 REGRILQLGTPEEIYtrpANLDVARF 251
Cdd:COG1137 210 SEGKVLAEGTPEEIL---NNPLVRKV 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-247 |
3.60e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSI-----RLGERDLLALspsQRDCAMVFQSyalyPH---- 89
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEENVWDI---RHKIGMVFQN----PDnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 -MTVGGNICTPLLMRGLgfwgrlpgaglfsantrrikaEAQASARKVAQSLGIDGLW---ERKPAQLSGGQRQRVALARA 165
Cdd:PRK13650 96 gATVEDDVAFGLENKGI---------------------PHEEMKERVNEALELVGMQdfkEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 166 MVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEaMSMSDRVAVMREGRILQLGTPEEIYTRPAN 245
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
..
gi 2536923639 246 LD 247
Cdd:PRK13650 234 LL 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-239 |
7.38e-32 |
|
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: 119.94 E-value: 7.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR---DCAMVFQ 82
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNICTpllmrglgfwgrlpGAGLFSANTRRIKAEAQASARKVAQSLGidglweRKPAQLSGGQRQRVAL 162
Cdd:TIGR03410 83 GREIFPRLTVEENLLT--------------GLAALPRRSRKIPDEIYELFPVLKEMLG------RRGGDLSGGQQQQLAI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:TIGR03410 143 ARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-238 |
9.02e-32 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 120.03 E-value: 9.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYpHMTVGG 94
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDSLRRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 95 NICtpllmrglgfWGRLpgaglfSANTrrikaEAQASARKVAQslgIDGLWERKPAQ-----------LSGGQRQRVALA 163
Cdd:cd03253 94 NIR----------YGRP------DATD-----EEVIEAAKAAQ---IHDKIMRFPDGydtivgerglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEE 238
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-243 |
1.37e-31 |
|
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: 119.94 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-----GERDLLALSPSQR- 75
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 -----DCAMVFQSYALYPHMTV--GGNICTPLLMRGLGFWGRlpgaglfsantrrIKAEAQASARKVAQSLG-IDGLwer 147
Cdd:TIGR02323 82 rlmrtEWGFVHQNPRDGLRMRVsaGANIGERLMAIGARHYGN-------------IRATAQDWLEEVEIDPTrIDDL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 kPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMRE 227
Cdd:TIGR02323 146 -PRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ 224
|
250
....*....|....*.
gi 2536923639 228 GRILQLGTPEEIYTRP 243
Cdd:TIGR02323 225 GRVVESGLTDQVLDDP 240
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-230 |
1.64e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.82 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDCAMVFQSYALY 87
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 88 PHMTVGGNICTPLLMRGlgfwgrlpgaglfsANTRRIKaeaqasaRKVAQSLGIDGLWERK---PAQLSGGQRQRVALAR 164
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAG--------------ASGDDIR-------RRVSAALDKVGLLDKAknfPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 165 AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLhDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-231 |
2.75e-31 |
|
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: 117.70 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LGERDLLALSPSQRDCAMVfQ 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRIGALI-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNICTPLLMRGLgfwgrlpgaglfsantrrikaeaqaSARKVAQSLGIDGLWE---RKPAQLSGGQRQR 159
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI-------------------------RKKRIDEVLDVVGLKDsakKKVKGFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-230 |
4.81e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.96 E-value: 4.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 9 LTKQFGNTK----VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR------DCA 78
Cdd:PRK10584 12 LKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGES------------------SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAmSMSDRVAVMREGRI 230
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-241 |
6.55e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 118.49 E-value: 6.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGER-----DLLALSPSQR 75
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 ------DCAMVFQSYA--LYPHMTVGGNICTPLLMRGLGFWGrlpgaglfsantrRIKAEAQASARKVAQSLG-IDGLwe 146
Cdd:PRK11701 84 rrllrtEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYG-------------DIRATAGDWLERVEIDAArIDDL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 147 rkPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMR 226
Cdd:PRK11701 149 --PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260
....*....|....*....|..
gi 2536923639 227 EGRILQLG-------TPEEIYT 241
Cdd:PRK11701 227 QGRVVESGltdqvldDPQHPYT 248
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-245 |
1.12e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.45 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLK-------LIAGLDQpdSGSIRLGERDLLA--LSPSQ 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDpdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 75 --RDCAMVFQSYALYPhMTVGGNICTPLLMRGLgfwgrlpgaglfsantrRIKAEAQAsarKVAQSLGIDGLWE------ 146
Cdd:COG1117 90 lrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGI-----------------KSKSELDE---IVEESLRKAALWDevkdrl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 147 RKPAQ-LSGGQRQRVALARAMVRRPAVFLFDEPLSNLD--ANLRqalrgeIRQLHDQLG--VTFIYVTHDQHEAMSMSDR 221
Cdd:COG1117 149 KKSALgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAK------IEELILELKkdYTIVIVTHNMQQAARVSDY 222
|
250 260
....*....|....*....|....
gi 2536923639 222 VAVMREGRILQLGTPEEIYTRPAN 245
Cdd:COG1117 223 TAFFYLGELVEFGPTEQIFTNPKD 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-230 |
1.15e-30 |
|
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: 115.01 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTK--VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RDC-AM 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHmTVGGNIctpllmrglgfwgrlpgaglfsantrrikaeaqasarkvaqslgidglwerkpaqLSGGQRQR 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------------------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLhDQLGVTFIYVTHdQHEAMSMSDRVAVMREGRI 230
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-231 |
1.28e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 123.30 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ------RDCAMVFQSYALY 87
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrEHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 88 PHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMV 167
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLE------------------RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 168 RRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAmSMSDRVAVMREGRIL 231
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-252 |
1.33e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.32 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQ--PD---SGSIRLGERDL--LALSPS 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIfkMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 QRDCAMVFQSYALYPHMTVGGNICTPLLMrglgfwgrlpgaglfsanTRRIKAEAQASARkVAQSLGIDGLWER------ 147
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKL------------------NRLVKSKKELQER-VRWALEKAQLWDEvkdrld 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 KPA-QLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTHDQHEAMSMSDRVAVMR 226
Cdd:PRK14247 142 APAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLY 219
|
250 260
....*....|....*....|....*.
gi 2536923639 227 EGRILQLGTPEEIYTRPANLDVARFV 252
Cdd:PRK14247 220 KGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-238 |
1.35e-30 |
|
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: 116.87 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVFQSYALYPhMTV 92
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNIctpllmrglgfwgrlpGAGLFSAN-TRRIKAEAQASARKVAQSL--GIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:cd03249 94 AENI----------------RYGKPDATdEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHdqLGVTFIYVTHDQHeAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-250 |
1.80e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerDLLALSPS-----QRDCAMVFQSyalyPH--- 89
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---DGITISKEnlkeiRKKIGIIFQN----PDnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 --MTVGGNICtpllmrglgfwgrlpgaglFSANTRRIK-AEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAM 166
Cdd:PRK13632 97 igATVEDDIA-------------------FGLENKKVPpKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMsMSDRVAVMREGRILQLGTPEEIYTRPANL 246
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
....
gi 2536923639 247 DVAR 250
Cdd:PRK13632 237 EKAK 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-225 |
2.89e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 121.62 E-value: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCA 78
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHmTVGGNIctpLLMRglgfwgrlPGAglfsANTRRIKAEAQASARKVAQSL--GIDGLWERKPAQLSGGQ 156
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENI---RLAR--------PDA----SDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDQHEAMSMsDRVAVM 225
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-229 |
5.50e-30 |
|
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: 114.84 E-value: 5.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQF-----GNTK--VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL----GERDLLALSP 72
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 73 SQ----RDCAMVFQSYALY--PHMTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGID-GLW 145
Cdd:COG4778 85 REilalRRRTIGYVSQFLRviPRVSALDVVAEPLLERGVD------------------REEARARARELLARLNLPeRLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 146 ERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDqHEAMS-MSDRVAV 224
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVREaVADRVVD 224
|
....*
gi 2536923639 225 MREGR 229
Cdd:COG4778 225 VTPFS 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-252 |
8.36e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 115.32 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGL-----DQPDSGSIRLGERDLLA--LSPSQ--RDCAMVFQS 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSpdVDPIEvrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMRGLgfwgrlpgaglfsantrrIKAEAQASARkVAQSLGIDGLWER-------KPAQLSGGQ 156
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGL------------------VKSKKELDER-VEWALKKAALWDEvkdrlndYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
250
....*....|....*.
gi 2536923639 237 EEIYTRPANLDVARFV 252
Cdd:PRK14267 233 RKVFENPEHELTEKYV 248
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-254 |
1.20e-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: 114.00 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPD----SGSIRLGERDLLALSPSQRDCAMVFQS--YALYPHMTV 92
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNICTPLLMRGLgfwgrlpgaglFSANTRRIKAEA--QASARKVAQSLgidglwERKPAQLSGGQRQRVALARAMVRRP 170
Cdd:TIGR02770 82 GNHAIETLRSLGK-----------LSKQARALILEAleAVGLPDPEEVL------KKYPFQLSGGMLQRVMIALALLLEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 171 AVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDVAR 250
Cdd:TIGR02770 145 PFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRK 224
|
....
gi 2536923639 251 FVGA 254
Cdd:TIGR02770 225 LLSA 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-239 |
4.06e-29 |
|
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: 118.82 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYpHMTVG 93
Cdd:TIGR03375 478 TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 GNICTpllmrglgfwgrlpGAGLFSantrriKAEAQASARKVaqslGIDGLWERKP-----------AQLSGGQRQRVAL 162
Cdd:TIGR03375 557 DNIAL--------------GAPYAD------DEEILRAAELA----GVTEFVRRHPdgldmqigergRSLSGGQRQAVAL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDAN----LRQALRGEIRqlhdqlGVTFIYVTHDQHeAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRseerFKDRLKRWLA------GKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKDQ 685
|
.
gi 2536923639 239 I 239
Cdd:TIGR03375 686 V 686
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-229 |
4.90e-29 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 117.70 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLAlsPSQRDC-----AMVFQ 82
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAAlaagvAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNIctpllmrglgFWGRLPGAGLFsANTRRIKAEaqasARKVAQSLGIDGLWERKPAQLSGGQRQRVAL 162
Cdd:PRK11288 87 ELHLVPEMTVAENL----------YLGQLPHKGGI-VNRRLLNYE----AREQLEHLGVDIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-252 |
9.70e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.45 E-value: 9.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 5 HISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGER------DLLALSPSQ--RD 76
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKlrKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYALYPHMTVGGNICTPLLMRGLgfwgrlpgaglfsANTRRIKAEAQASARKVaqslgidGLWER------KPA 150
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGI-------------KEKREIKKIVEECLRKV-------GLWKEvydrlnSPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 151 -QLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlgVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:PRK14246 152 sQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGE 229
|
250 260
....*....|....*....|...
gi 2536923639 230 ILQLGTPEEIYTRPANLDVARFV 252
Cdd:PRK14246 230 LVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-230 |
9.72e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 117.07 E-value: 9.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS---QRDCA 78
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNICTpllmrglgfwgRLPGaglfsantrrikaeAQASARKVAQ---SLGIDGLWERKPAQLSGG 155
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILF-----------GLPK--------------RQASMQKMKQllaALGCQLDLDSSAGSLEVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-230 |
1.28e-28 |
|
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: 109.83 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRdcamvfqsyalyphmtvggni 96
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 ctplLMRGLGFwgrLPG----AGLFSAntrrikaeaqasaRKVAQSLGIdglwerkPAQLSGGQRQRVALARAMVRRPAV 172
Cdd:cd03215 73 ----IRAGIAY---VPEdrkrEGLVLD-------------LSVAENIAL-------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 173 FLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-230 |
1.42e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 11 KQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR-DCAMVF-----QSY 84
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiRAGIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHMTVGGNICTPLLmrglgfwGRLPGAGLFSantrriKAEAQASARKVAQSLGI--DGLwERKPAQLSGGQRQRVAL 162
Cdd:COG1129 340 GLVLDLSIRENITLASL-------DRLSRGGLLD------RRRERALAEEYIKRLRIktPSP-EQPVGNLSGGNQQKVVL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
2.33e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.93 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerdllalsPSQRDCAMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 86 LYPHMTVGGNIctpllMRGLGFWGRLPGA--------GLFSANTRRIKA-----------EAQASARKVAQSLGIDG-LW 145
Cdd:COG0488 72 LDDDLTVLDTV-----LDGDAELRALEAEleeleaklAEPDEDLERLAElqeefealggwEAEARAEEILSGLGFPEeDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 146 ERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHdqlgVTFIYVTHDQH 213
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHDRY 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-230 |
3.33e-28 |
|
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: 109.99 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYpHMTVG 93
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 GNICTpllmrglgfwgrlpgaGLFSANTRRIKAeaqasarkVAQSLGIDGLWERKP-----------AQLSGGQRQRVAL 162
Cdd:cd03245 96 DNITL----------------GAPLADDERILR--------AAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLD----ANLRQALRGEIRqlhdqlGVTFIYVTHDQhEAMSMSDRVAVMREGRI 230
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDmnseERLKERLRQLLG------DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-269 |
4.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 4.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSI---RLGERDLLALSPSQRDCAMVFQSyalyPHMT 91
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdGLDTSDEENLWDIRNKAGMVFQN----PDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNICTPLLMRGLGFWGRLPgaglfsantRRIKAEAQASARKVaqslgidGLWERK---PAQLSGGQRQRVALARAMVR 168
Cdd:PRK13633 98 IVATIVEEDVAFGPENLGIPP---------EEIRERVDESLKKV-------GMYEYRrhaPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 169 RPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYT-----RP 243
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKevemmKK 240
|
250 260
....*....|....*....|....*.
gi 2536923639 244 ANLDVarfvgaPRINLLDGEVKAHGV 269
Cdd:PRK13633 241 IGLDV------PQVTELAYELKKEGV 260
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-269 |
5.35e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.36 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALS------PSQRDCAMVFQsyalYPH 89
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikPVRKKVGVVFQ----FPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 mtvgGNICTPLLMRGLGFwgrlpGAGLFSANtrriKAEAQASARKVAQSLGIDG-LWERKPAQLSGGQRQRVALARAMVR 168
Cdd:PRK13643 95 ----SQLFEETVLKDVAF-----GPQNFGIP----KEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 169 RPAVFLFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYtRPANLDV 248
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLK 239
|
250 260
....*....|....*....|.
gi 2536923639 249 ARFVGAPRINLLDGEVKAHGV 269
Cdd:PRK13643 240 AHELGVPKATHFADQLQKTGA 260
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-242 |
8.91e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.95 E-value: 8.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 29 GEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-----RDCAMVFQS-YA-LYPHMTVGGNICTPLL 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 102 MRGLGfwgrlpgaglfsantrrikaEAQASARKVAQSLGIDGL-----WeRKPAQLSGGQRQRVALARAMVRRPAVFLFD 176
Cdd:PRK10261 430 VHGLL--------------------PGKAAAARVAWLLERVGLlpehaW-RYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 177 EPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG-------TPEEIYTR 242
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGprravfeNPQHPYTR 561
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-214 |
3.15e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.49 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 12 QFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVFQSYALYPH 89
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 mTVGGNIctpllmrglgfwgrlpgagLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:PRK10247 96 -TVYDNL-------------------IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHE 214
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-257 |
4.36e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.68 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 21 GLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALS------PSQRDCAMVFQsyalYPHmtvgG 94
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikQIRKKVGLVFQ----FPE----S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 95 NICTPLLMRGLGFwgrlpGAGLFSANtrriKAEAQASARKVAQSLGID-GLWERKPAQLSGGQRQRVALARAMVRRPAVF 173
Cdd:PRK13649 97 QLFEETVLKDVAF-----GPQNFGVS----QEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 174 LFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDvARFVG 253
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLE-EKQLG 245
|
....
gi 2536923639 254 APRI 257
Cdd:PRK13649 246 VPKI 249
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-243 |
4.62e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 112.74 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYPHmTVGGN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 IC--TPLLMRglgfwgrlpgaglfsantrrikaEAQASARKVaqslGIDGLWERKP-----------AQLSGGQRQRVAL 162
Cdd:TIGR03797 547 IAggAPLTLD-----------------------EAWEAARMA----GLAEDIRAMPmgmhtviseggGTLSGGQRQRLLI 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDaNLRQALrgeIRQLHDQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALD-NRTQAI---VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMAR 674
|
.
gi 2536923639 243 P 243
Cdd:TIGR03797 675 E 675
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-239 |
7.58e-27 |
|
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: 111.67 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVFQSYALYPHmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNICTpllmrglgfWGRlpgaglfSANTRRIKAEAQ-ASARKVAQSL--GIDGLWERKPAQLSGGQRQRVALARAMVR 168
Cdd:TIGR01842 408 VAENIAR---------FGE-------NADPEKIIEAAKlAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 169 RPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-253 |
1.33e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.97 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRD-CAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGGNictpLLMRGLGFwgrlpgaGLFSANTRRIKAEAQASARkvaqslgIDGLWERKPAQLSGGQRQRV 160
Cdd:PRK13537 86 PQFDNLDPDFTVREN----LLVFGRYF-------GLSAAAARALVPPLLEFAK-------LENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
250
....*....|...
gi 2536923639 241 TRPANLDVARFVG 253
Cdd:PRK13537 227 ESEIGCDVIEIYG 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-243 |
2.44e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 106.03 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRD--CAMVFQ--SYALYPHMTV 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQdpSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNICTPLLMrglgfwgrlpgaglfsaNTrriKAEAQASARKVAQSLGIDGLWERK----PAQLSGGQRQRVALARAMVR 168
Cdd:PRK15112 107 SQILDFPLRL-----------------NT---DLEPEQREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 169 RPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVThdQHEAM--SMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMmkHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-263 |
2.53e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GER---DLLALSPSQRDCAMVFQSyalyPHmt 91
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPikyDKKSLLEVRKTVGIVFQN----PD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 vgGNICTPLLMRGLGFwGRLpgaglfsaNTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:PRK13639 89 --DQLFAPTVEEDVAF-GPL--------NLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT-----RPANL 246
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdietiRKANL 236
|
250
....*....|....*..
gi 2536923639 247 DVARFvgAPRINLLDGE 263
Cdd:PRK13639 237 RLPRV--AHLIEILNKE 251
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-234 |
5.41e-26 |
|
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: 102.78 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSyalYPHmtvgg 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ---RPY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 95 nictpllmrglgfwgrlpgagLFSANTRrikaeaqasarkvaQSLGIdglwerkpaQLSGGQRQRVALARAMVRRPAVFL 174
Cdd:cd03247 86 ---------------------LFDTTLR--------------NNLGR---------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 175 FDEPLSNLDANLRQALrgeIRQLHDQL-GVTFIYVTHdqH-EAMSMSDRVAVMREGRILQLG 234
Cdd:cd03247 122 LDEPTVGLDPITERQL---LSLIFEVLkDKTLIWITH--HlTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-241 |
7.78e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.68 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 9 LTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GER-DLLALSPSQRDCAMVFQSyal 86
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHiQHYASKEVARRIGLLAQN--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 87 yphMTVGGNICT-PLLMRGlgfwgRLPGAGLFSantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARA 165
Cdd:PRK10253 90 ---ATTPGDITVqELVARG-----RYPHQPLFT----RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 166 MVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-238 |
7.96e-26 |
|
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: 103.84 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ--RDCAMVFQSYALYPHmT 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNIctpllmrglgfwgrlpgagLFSANTRRIKAEAQAsarkvAQSLGIDGLWERKP-----------AQLSGGQRQRV 160
Cdd:cd03254 93 IMENI-------------------RLGRPNATDEEVIEA-----AKEAGAHDFIMKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHdqheAMSM---SDRVAVMREGRILQLGTPE 237
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTHD 222
|
.
gi 2536923639 238 E 238
Cdd:cd03254 223 E 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-242 |
1.17e-25 |
|
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: 103.46 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYpHMTVG 93
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdYTLASLRRQIGLVSQDVFLF-NDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 GNICtpllmrglgfWGRlPGAGLfsanTRRIKAEAQASARKVAQSL--GIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:cd03251 94 ENIA----------YGR-PGATR----EEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLhdQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-243 |
1.22e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 108.88 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDC--AMVFQSYALYphmtvGGN 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANsvAMVDQDIFLF-----EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTPLLMrglgfWGR-LPGAGLfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFL 174
Cdd:TIGR03796 569 VRDNLTL-----WDPtIPDADL-----VRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 175 FDEPLSNLDANLRQALRGEIRqlhdQLGVTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:TIGR03796 639 LDEATSALDPETEKIIDDNLR----RRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-238 |
1.25e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.32 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLK----LIAGLDQPDSGSIRLGE---------RDLlal 70
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRtvqregrlaRDI--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 71 SPSQRDCAMVFQSYALYPHMTVGGNIctplLMRGLG---FWgrlpgAGLFSANTRRIKAEA-QASARkvaqsLGIDGLWE 146
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENV----LIGALGstpFW-----RTCFSWFTREQKQRAlQALTR-----VGMVHFAH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 147 RKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMR 226
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
|
250
....*....|..
gi 2536923639 227 EGRILQLGTPEE 238
Cdd:PRK09984 228 QGHVFYDGSSQQ 239
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-243 |
2.04e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.89 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLlalspSQRDCAmvfqsyalYPHMTVGG 94
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-----VQYDHH--------YLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 95 NICTPLLMRGLgfWGRLPGAGLFSANTRRIKAEAQAS-ARKVAQSL--GIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:TIGR00958 560 VGQEPVLFSGS--VRENIAYGLTDTPDEEIMAAAKAAnAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 172 VFLFDEPLSNLDANLRQALrgeiRQLHDQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:TIGR00958 638 VLILDEATSALDAECEQLL----QESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-231 |
2.09e-25 |
|
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: 102.80 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDllalsPSQRDCAMVFQSYALYPHMTVggnic 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRKKFLRRIGVVFGQKTQ----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 98 tpllmrglgFWGRLPGAGLFSANtRRI----KAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVF 173
Cdd:cd03267 106 ---------LWWDLPVIDSFYLL-AAIydlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 174 LFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-243 |
4.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGS--------IRLGERDLLALspsqRD-CAMVFQSyalyP 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDI----REkVGIVFQN----P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 89 H-----MTVGGNICTPLLMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALA 163
Cdd:PRK13640 94 DnqfvgATVGDDVAFGLENRAVP------------------RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAmSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-239 |
5.89e-25 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 101.47 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 24 LTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdllALSPSQRDCAMVFQSYALYPHMtvggnictPLLMR 103
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFAWDF--------PISVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 104 GLGFWGRLPGAGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLD 183
Cdd:TIGR03771 70 HTVMSGRTGHIGWL----RRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 184 aNLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVaVMREGRILQLGTPEEI 239
Cdd:TIGR03771 146 -MPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-230 |
1.29e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDcamvfqs 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 yALYPHMTVGGNIctpllmrglgfWGRLPGAGlfsantrrikaeaQASARKVAQSLGIDG-LWERKPAQLSGGQRQRVAL 162
Cdd:COG0488 389 -ELDPDKTVLDEL-----------RDGAPGGT-------------EQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLAL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALrgeIRQLHDQLGvTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEAL---EEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-239 |
1.43e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LGERDLLALSPSQRDCAMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNictpllmrgLGFWGRlpgagLFSANTRRIKAeaqasarkVAQSLGIDGLWERKP----AQLSGGQRQ 158
Cdd:PRK13536 122 FDNLDLEFTVREN---------LLVFGR-----YFGMSTREIEA--------VIPSLLEFARLESKAdarvSDLSGGMKR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
.
gi 2536923639 239 I 239
Cdd:PRK13536 259 L 259
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-270 |
1.53e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ---RDCAMVFQSyalyPHMTV 92
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirKLVGIVFQN----PETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GG------------NICTPllmrglgfwgrlpgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:PRK13644 91 VGrtveedlafgpeNLCLP-------------------------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEaMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVL 223
|
250 260 270
....*....|....*....|....*....|
gi 2536923639 241 TRPANLDVArfVGAPRINLLDGEVKAHGVV 270
Cdd:PRK13644 224 SDVSLQTLG--LTPPSLIELAENLKMHGVV 251
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-237 |
2.08e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.14 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLD--QPDSGSIRLGERDLLALSPSQRDCA---MV 80
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERARAgifLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQsyalYPhmtVggnictpllmrglgfwgRLPGAGLF-----SANTRRIKA----EAQASARKVAQSLGIDGLWERKP-- 149
Cdd:COG0396 83 FQ----YP---V-----------------EIPGVSVSnflrtALNARRGEElsarEFLKLLKEKMKELGLDEDFLDRYvn 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTH-----DQHEAmsmsDRVAV 224
Cdd:COG0396 139 EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHyqrilDYIKP----DFVHV 213
|
250
....*....|...
gi 2536923639 225 MREGRILQLGTPE 237
Cdd:COG0396 214 LVDGRIVKSGGKE 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-240 |
2.55e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.60 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 29 GEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA--LSPSQRDCAMVFQSyalyPHMTVGGNICTPLLMRGLG 106
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGIVFQN----PDNQFVGSIVKYDVAFGLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 107 FwgrlpgaglFSANTRRIKaeaqasaRKVAQSLGIDGLWER---KPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLD 183
Cdd:PRK13648 111 N---------HAVPYDEMH-------RRVSEALKQVDMLERadyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 184 ANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIY 240
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-239 |
2.96e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERD--LLALspsqrdcAMVFQsyalyPHMTVGGN 95
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsaLLEL-------GAGFH-----PELTGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 IctpllmrglgfwgRLPGA--GLFSANTRRIKAEAQASArkvaqSLG--IDglwerKPAQ-LSGGQRQRVALARAMVRRP 170
Cdd:COG1134 109 I-------------YLNGRllGLSRKEIDEKFDEIVEFA-----ELGdfID-----QPVKtYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 171 AVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:COG1134 166 DILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-228 |
3.00e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.10 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSP---SQRDCA 78
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNIctpllmrglgFWGRLPGAGLFSANTRRIKaEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:PRK09700 84 IIYQELSVIDELTVLENL----------YIGRHLTKKVCGVNIIDWR-EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREG 228
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-262 |
3.55e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.17 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKS-TLLKLIAGLDQP----DSGSIRLGER-----DLLALS 71
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRsrqviELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 72 PSQ------RDCAMVFQS--YALYPHMTVGGNICTPL-LMRGLGfwgrlpgaglfsantrriKAEAQASARKVAQSLGI- 141
Cdd:PRK10261 95 AAQmrhvrgADMAMIFQEpmTSLNPVFTVGEQIAESIrLHQGAS------------------REEAMVEAKRMLDQVRIp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 142 --DGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMS 219
Cdd:PRK10261 157 eaQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2536923639 220 DRVAVMREGRILQLGTPEEIYTRPANLDVARFVGA-PRINLLDG 262
Cdd:PRK10261 237 DRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAvPQLGAMKG 280
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-210 |
4.73e-24 |
|
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: 98.20 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMVFQSYAL 86
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 87 YPHMTVGGNictpllmrgLGFWgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAM 166
Cdd:TIGR01189 85 KPELSALEN---------LHFW-------------AAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQlHDQLGVTFIYVTH 210
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRA-HLARGGIVLLTTH 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-245 |
9.86e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.48 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKST----LLKLIAGldqpdSGSI--------RLGERDLLalsPSQRDCAMVF 81
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIwfdgqplhNLNRRQLL---PVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 Q--SYALYPHMTVggnicTPLLMRGLgfwgRLPGAGLfSAntrrikAEAQASARKVAQSLGID-GLWERKPAQLSGGQRQ 158
Cdd:PRK15134 369 QdpNSSLNPRLNV-----LQIIEEGL----RVHQPTL-SA------AQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
....*..
gi 2536923639 239 IYTRPAN 245
Cdd:PRK15134 513 VFAAPQQ 519
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-265 |
1.39e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.01 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQP-----DSGSIRLGERDLLALSPS--- 73
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlef 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 QRDCAMVFQSYALYPhMTVGGNICtpllmrglgfwgrlpgaglfsANTRRIKAEAQASARKVAQS-LGIDGLWER----- 147
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVL---------------------AGVRAHKLVPRKEFRGVAQArLTEVGLWDAvkdrl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 --KPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTHDQHEAMSMSDRVAVM 225
Cdd:PRK14271 158 sdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2536923639 226 REGRILQLGTPEEIYTRPANLDVARFVGAprinlLDGEVK 265
Cdd:PRK14271 236 FDGRLVEEGPTEQLFSSPKHAETARYVAG-----LSGDVK 270
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-242 |
1.98e-23 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 97.56 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYpHMTVGGN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 IC---TPLLMRGLGFWGRLPGAGLFSANTRrikaeaqasarkvaqsLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAV 172
Cdd:cd03252 96 IAladPGMSMERVIEAAKLAGAHDFISELP----------------EGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 173 FLFDEPLSNLDAnlrQALRGEIRQLHDQL-GVTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:cd03252 160 LIFDEATSALDY---ESEHAIMRNMHDICaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-229 |
2.81e-23 |
|
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: 101.05 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPD---SGSIRLGERDLLALSPSQRDCA-- 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 -MVFQSYALYPHMTVGGNICtpllmrgLGFWGRLPGAGL-FSANTRRikaeaqasARKVAQSLGIDGLWERKP-AQLSGG 155
Cdd:TIGR02633 81 vIIHQELTLVPELSVAENIF-------LGNEITLPGGRMaYNAMYLR--------AKNLLRELQLDADNVTRPvGDYGGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-244 |
3.59e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPD---SGSIRLGERDLLALSPSQ------RDCAMVFQS- 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklraEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 -YALYPHMTVGGNictplLMRGLGFWGRLPGAGLFSANTRRIKAEAQASARKVAQSLgidglwerkPAQLSGGQRQRVAL 162
Cdd:PRK09473 107 mTSLNPYMRVGEQ-----LMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMY---------PHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
..
gi 2536923639 243 PA 244
Cdd:PRK09473 253 PS 254
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-239 |
3.85e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 101.36 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYPHmTVGGN 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICtpllmrglgfwgrLPGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:TIGR01846 551 IA-------------LCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 176 DEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-239 |
5.93e-23 |
|
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: 100.58 E-value: 5.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 3 DIHISGLTKQFG-NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLlalspSQRDCAMVF 81
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-----KDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTV--GGNICTPLLMrglgfwGRLPGAG----LFSANTRRIKAEAQASARKVAQSLGIDGlwerkpAQLSGG 155
Cdd:TIGR01193 548 QFINYLPQEPYifSGSILENLLL------GAKENVSqdeiWAACEIAEIKDDIENMPLGYQTELSEEG------SSISGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlgvTFIYVTHdQHEAMSMSDRVAVMREGRILQLGT 235
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGS 691
|
....
gi 2536923639 236 PEEI 239
Cdd:TIGR01193 692 HDEL 695
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-244 |
6.37e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.00 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPD---SGSIRLGERDLLALS---PSQRDCAMVF 81
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNirdTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTVGGNIctpllmrglgFWGRLPGAGLFsANTRRIKAEAQASARKVaqSLGIDGlwERKPAQLSGGQRQRVA 161
Cdd:PRK13549 89 QELALVKELSVLENI----------FLGNEITPGGI-MDYDAMYLRAQKLLAQL--KLDINP--ATPVGNLGLGQQQLVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 162 LARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRilqlgtpeEIYT 241
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--------HIGT 224
|
...
gi 2536923639 242 RPA 244
Cdd:PRK13549 225 RPA 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-245 |
6.60e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDS-----GSIRLGERDL----LALS 71
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 72 PSQRDCAMVFQSYALYPhMTVGGNICTPLLMRGlgfWgrlpgaglfsantrRIKAEAQA---SARKVAQslgidgLWE-- 146
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVG---W--------------RPKLEIDDiveSALKDAD------LWDei 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 147 -----RKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDR 221
Cdd:PRK14258 141 khkihKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
250 260
....*....|....*....|....*....
gi 2536923639 222 VAVMR--EGRILQL---GTPEEIYTRPAN 245
Cdd:PRK14258 221 TAFFKgnENRIGQLvefGLTKKIFNSPHD 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-246 |
7.73e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA--LSPSQRDCAMVFQSyalyPHMTVGGNI 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenVWNLRRKIGMVFQN----PDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 CTPLLMRGLGFWGrLPgaglfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFD 176
Cdd:PRK13642 99 VEDDVAFGMENQG-IP------------REEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 177 EPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYTRPANL 246
Cdd:PRK13642 166 ESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
8.02e-23 |
|
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: 92.90 E-value: 8.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRlgerdllalspsqrdcamvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 yalyphmtvggnictpllmrglgfWGRLPGAGLFsantrrikaeaqasarkvaqslgidglwerkpAQLSGGQRQRVALA 163
Cdd:cd03221 59 ------------------------WGSTVKIGYF--------------------------------EQLSGGEKMRLALA 82
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlgvTFIYVTHDQH 213
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRY 128
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-230 |
9.39e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLT-KQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RDCAMVF-- 81
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYip 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 ---QSYALYPHMTVGGNIctpllmrGLGFWGRLPGAGLFSANTRRIKAEAQASARK---VAQSLgidglwERKPAQLSGG 155
Cdd:COG3845 340 edrLGRGLVPDMSVAENL-------ILGRYRRPPFSRGGFLDRKAIRAFAEELIEEfdvRTPGP------DTPARSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
16-250 |
1.26e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.46 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL----LALSPSQRDCAMVFQSyalyphmt 91
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVGMVFQD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 vggnictpllmrglgfwgrlPGAGLFSA-----------NTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:PRK13636 91 --------------------PDNQLFSAsvyqdvsfgavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
250
....*....|....*
gi 2536923639 241 T-----RPANLDVAR 250
Cdd:PRK13636 231 AekemlRKVNLRLPR 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-234 |
1.64e-22 |
|
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: 93.77 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGL--DQPDSGSIRLGERDLLALSPSQRdCAMVFQSYALYPHMT 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNIctpllmrglgfwgrlpgagLFSANTRrikaeaqasarkvaqslgidglwerkpaQLSGGQRQRVALARAMVRRPA 171
Cdd:cd03213 99 VRETL-------------------MFAAKLR----------------------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHD-QHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-240 |
1.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA------LSPSQRDCAMVFQsyalyphm 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 tvggnictpllmrglgfwgrLPGAGLFSANTRR------------IKaEAQASARKVAQSLGID-GLWERKPAQLSGGQR 157
Cdd:PRK13646 93 --------------------FPESQLFEDTVEReiifgpknfkmnLD-EVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 158 QRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPE 237
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
...
gi 2536923639 238 EIY 240
Cdd:PRK13646 232 ELF 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-261 |
2.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 11 KQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGE--------RDLLALSPSQRD------ 76
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknNHELITNPYSKKiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 ----CAMVFQ--SYALYPHmTVGGNIctpllMRGlgfwgrlpgaglfSANTRRIKAEAQASARKVAQSLGIDGLW-ERKP 149
Cdd:PRK13631 114 lrrrVSMVFQfpEYQLFKD-TIEKDI-----MFG-------------PVALGVKKSEAKKLAKFYLNKMGLDDSYlERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 150 AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250 260 270
....*....|....*....|....*....|..
gi 2536923639 230 ILQLGTPEEIYTRPANLDVARFVGAPRINLLD 261
Cdd:PRK13631 254 ILKTGTPYEIFTDQHIINSTSIQVPRVIQVIN 285
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-230 |
3.01e-22 |
|
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: 94.07 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYPHmTV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNIctpllmrglgfwgrlpGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWE---RKPAQLSGGQRQRVALARAMVRR 169
Cdd:cd03248 105 QDNI----------------AYGLQSCSFECVKEAAQKAHAHSFISELASGYDTevgEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 170 PAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIyvTHdQHEAMSMSDRVAVMREGRI 230
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVI--AH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-250 |
3.51e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GERDLLA-LSPSQRDCAMVFQSyalyphmt 91
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKEnIREVRKFVGLVFQN-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNICTPLLMRGLGFwgrlpGAGLFSANTRRIKAEAQASARkvaqSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:PRK13652 87 PDDQIFSPTVEQDIAF-----GPINLGLDEETVAHRVSSALH----MLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANLDVAR 250
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVH 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-249 |
4.97e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 7 SGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSI-------RLGERDLLALspsQRDCAM 79
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkplDYSKRGLLAL---RQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSyalyPHMTVggnictpllmrglgFWGRLPGAGLFSanTRRIKAEAQASARKVAQSLG-IDGL-WERKPAQ-LSGGQ 156
Cdd:PRK13638 82 VFQD----PEQQI--------------FYTDIDSDIAFS--LRNLGVPEAEITRRVDEALTlVDAQhFRHQPIQcLSHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
250
....*....|...
gi 2536923639 237 EEIYTRPANLDVA 249
Cdd:PRK13638 221 GEVFACTEAMEQA 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-268 |
9.40e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 9.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 20 KGLD---LTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL---------GERDLLALspsQRDCAMVFQsyalY 87
Cdd:PRK13641 21 KGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetGNKNLKKL---RKKVSLVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 88 PHMTVGGNICTPLLMRGLGFWGrlpgaglFSANtrrikaEAQASARKVAQSLGI-DGLWERKPAQLSGGQRQRVALARAM 166
Cdd:PRK13641 94 PEAQLFENTVLKDVEFGPKNFG-------FSED------EAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRgEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTRPANL 246
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
250 260
....*....|....*....|..
gi 2536923639 247 DvARFVGAPRINLLDGEVKAHG 268
Cdd:PRK13641 240 K-KHYLDEPATSRFASKLEKGG 260
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-242 |
9.93e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 96.71 E-value: 9.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 3 DIHISGLTKQFGNT--KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCA 78
Cdd:TIGR02203 330 DVEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLadYTLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHmTVGGNICtpllmrglgfWGRLPGAGlfSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIA----------YGRTEQAD--RAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLhdQLGVTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNE 553
|
....
gi 2536923639 239 IYTR 242
Cdd:TIGR02203 554 LLAR 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-242 |
1.15e-21 |
|
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: 96.41 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQ--PDSGSI-----------------RLGE 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 65 R-------------DLLALSPS-----QRDCAMVFQ-SYALYPHMTVGGNIctpllMRGLgfwgrlpgaglfsantRRIK 125
Cdd:TIGR03269 81 PcpvcggtlepeevDFWNLSDKlrrriRKRIAIMLQrTFALYGDDTVLDNV-----LEAL----------------EEIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 126 AEAQASARKVAQSLGIDGLWERK---PAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLG 202
Cdd:TIGR03269 140 YEGKEAVGRAVDLIEMVQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASG 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2536923639 203 VTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:TIGR03269 220 ISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-210 |
1.45e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.47 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRdCAMVFQSYALYPHMTVG 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 GNictpllmrgLGFWgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVF 173
Cdd:PRK13539 92 EN---------LEFW-------------AAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 2536923639 174 LFDEPLSNLDANlRQALRGEIRQLHDQLGVTFIYVTH 210
Cdd:PRK13539 150 ILDEPTAALDAA-AVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-237 |
1.51e-21 |
|
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: 91.43 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLD--QPDSGSIRLGERDLLALSPSQRDCA---MV 80
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgifLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVGgnictpLLMRGL--GFwgrlpgaglfsantrrikaeaqasarkvaqslgidglwerkpaqlSGGQRQ 158
Cdd:cd03217 83 FQYPPEIPGVKNA------DFLRYVneGF---------------------------------------------SGGEKK 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDA-NLRQALRGeIRQLHDQlGVTFIYVTHDQHEAMSM-SDRVAVMREGRILQLGTP 236
Cdd:cd03217 112 RNEILQLLLLEPDLAILDEPDSGLDIdALRLVAEV-INKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
.
gi 2536923639 237 E 237
Cdd:cd03217 190 E 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-243 |
1.74e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.48 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRlgerdllalSPSQRDCAMVFQSYALYPHMtv 92
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQKLYLDTTL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 ggnictPLLMRGlgFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDglwerKPAQ-LSGGQRQRVALARAMVRRPA 171
Cdd:PRK09544 83 ------PLTVNR--FLRLRPGTK---------KEDILPALKRVQAGHLID-----APMQkLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMrEGRILQLGTPEEIYTRP 243
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-245 |
3.28e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQ--PD---SGSIRLGERDLlaLSPS--- 73
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNI--YSPRtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 ---QRDCAMVFQSYALYPhMTVGGNIctpllMRGLgfwgRLPGaglfsantrrIKAEAQASArKVAQSLGIDGLWER--- 147
Cdd:PRK14239 82 vdlRKEIGMVFQQPNPFP-MSIYENV-----VYGL----RLKG----------IKDKQVLDE-AVEKSLKGASIWDEvkd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 148 ----KPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTHDQHEAMSMSDRVA 223
Cdd:PRK14239 141 rlhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTG 218
|
250 260
....*....|....*....|..
gi 2536923639 224 VMREGRILQLGTPEEIYTRPAN 245
Cdd:PRK14239 219 FFLDGDLIEYNDTKQMFMNPKH 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-210 |
4.70e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKV-IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GERDLLALSpsQRdcam 79
Cdd:COG4178 361 GALALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--QR---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 vfqsyalyPHMtvggnictPLlmrglgfwGRLPGAGLFSANTRRIKAEAQASA-RKV-----AQSLGIDGLWERkpaQLS 153
Cdd:COG4178 435 --------PYL--------PL--------GTLREALLYPATAEAFSDAELREAlEAVglghlAERLDEEADWDQ---VLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALrgeIRQLHDQL-GVTFIYVTH 210
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-246 |
5.66e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.06 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 21 GLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPDSGSIRLGERDLLALSPSQ--RDCAMVFQSYALYPHMTVggnict 98
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPV------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 99 pllmrglgfWGRLpgaGLFSANTRRIKAEAQASARkVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVR-------RPA 171
Cdd:COG4138 87 ---------FQYL---ALHQPAGASSEAVEQLLAQ-LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYTrPANL 246
Cdd:COG4138 154 LLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PENL 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-234 |
7.68e-21 |
|
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: 90.02 E-value: 7.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQpdSGSIRLGERdLLALSPSQRD-----CAMVFQSYALYPHMT 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQI-LFNGQPRKPDqfqkcVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNIctpllmrglgfwgrlpgagLFSAN--TRRIKAEAQASARKVAQSL---GIDGLWERKPAQLSGGQRQRVALARAM 166
Cdd:cd03234 98 VRETL-------------------TYTAIlrLPRKSSDAIRKKRVEDVLLrdlALTRIGGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 167 VRRPAVFLFDEPLSNLDAN--------LRQ-ALRGEIrqlhdqlgvtfIYVTHDQ--HEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFtalnlvstLSQlARRNRI-----------VILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-241 |
8.40e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 8.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR-DCAMVF-----QSYALYPHMTVGGN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTpLLMRGLGFWgrlpgaglfsantRRIKAEAqASARKVAQSLGIDGLWERKPAQ-LSGGQRQRVALARAMVRRPAVFL 174
Cdd:PRK15439 362 VCA-LTHNRRGFW-------------IKPAREN-AVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 175 FDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINV 492
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-234 |
9.33e-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: 89.51 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIrlgerdllalspsqrdcamvfqsyalyphmTVGGNIc 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------------------------TVRGRV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 98 TPLLMRGLGFWGRLPG------AGLFSANTRRikaEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:cd03220 86 SSLLGLGGGFNPELTGreniylNGRLLGLSRK---EIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-238 |
1.52e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 14 GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQSYALYphmtvg 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVH------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 gnictpllmrglgfwgrlpgagLFSANTRRIKAEAQASA-----RKVAQSLGIDGLWERKPA----------QLSGGQRQ 158
Cdd:PRK11160 425 ----------------------LFSATLRDNLLLAAPNAsdealIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQalrgEIRQL---HDQlGVTFIYVTHDQHEAMSMsDRVAVMREGRILQLGT 235
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETER----QILELlaeHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
...
gi 2536923639 236 PEE 238
Cdd:PRK11160 557 HQE 559
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-239 |
5.44e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.38 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LG------ERDLLalspsqRDCAMVF-QSYALYP 88
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpfkrRKEFA------RRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 89 HmtvggnictpllmrglgfwgrLPGAGLFSANtRRI----KAEAQASARKVAQSLGIDGLWeRKPA-QLSGGQRQRVALA 163
Cdd:COG4586 110 D---------------------LPAIDSFRLL-KAIyripDAEYKKRLDELVELLDLGELL-DTPVrQLSLGQRMRCELA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-243 |
5.87e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.58 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPDSGSI-----RLGERDLLALS 71
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 72 PSQR------DCAMVFQ--SYALYPHMTVGGNICTPLLMRGLG--FWGRlpgaglfsANTRriKAEAQASARKVaqslGI 141
Cdd:COG4170 80 PRERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFKgkWWQR--------FKWR--KKRAIELLHRV----GI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 142 ---DGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLR-QALR--GEIRQLHdqlGVTFIYVTHDQHEA 215
Cdd:COG4170 146 kdhKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQaQIFRllARLNQLQ---GTSILLISHDLESI 222
|
250 260
....*....|....*....|....*...
gi 2536923639 216 MSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:COG4170 223 SQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-239 |
1.10e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.26 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLAL---SPSQRDC 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNICTPLLMRglgfwgrlpgaglfsantRRIKAEAQAS-ARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIR------------------DDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
...
gi 2536923639 237 EEI 239
Cdd:PRK10895 222 TEI 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-241 |
1.35e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA-------LSPSQRDCAMVFQ--SYALY 87
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikeVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 88 PHmTVGGNICTPLLMRGlgfwgrlpgaglfsantrrikAEAQASARKVAQSLGIDGLWE----RKPAQLSGGQRQRVALA 163
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLG---------------------ENKQEAYKKVPELLKLVQLPEdyvkRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-229 |
1.63e-19 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 85.60 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 10 TKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLAlspSQrdcamvfQSYALypH 89
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYV---SQ-------EPWIQ--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNIctpllmrglgfwgrlpgagLFSA--NTRRIKAEAQASA-RKVAQSL--------GIDGLwerkpaQLSGGQRQ 158
Cdd:cd03250 80 GTIRENI-------------------LFGKpfDEERYEKVIKACAlEPDLEILpdgdlteiGEKGI------NLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDAN-----LRQALRGEIRqlhdqLGVTFIYVTHdQHEAMSMSDRVAVMREGR 229
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHvgrhiFENCILGLLL-----NNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-236 |
1.76e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.84 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQF---GNTKVIKgLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL-LALSPSQRD 76
Cdd:TIGR01257 926 VPGVCVKNLVKIFepsGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 CAMVFQSYALYPHMTVGGNICtpllmrglgFWGRLPGaglfsantrRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQ 156
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHIL---------FYAQLKG---------RSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGM 1066
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIrqLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-210 |
2.09e-19 |
|
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: 85.24 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS-QRDCAMVFQSYAL 86
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 87 YPHMTVGGNictpllmrgLGFWGRLPG-AGLFSANTRrikaeaqasarkvaqsLGIDGLWERKPAQLSGGQRQRVALARA 165
Cdd:cd03231 85 KTTLSVLEN---------LRFWHADHSdEQVEEALAR----------------VGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2536923639 166 MVRRPAVFLFDEPLSNLDANLRQALRGEIRQlHDQLGVTFIYVTH 210
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAG-HCARGGMVVLTTH 183
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-239 |
3.81e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.13 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPDSGSIRLGERDLLALSPSQ--RDCAMVFQSYALyPHMTVGGNIctp 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 100 LLmrglgfwgrlpgaGLFSANTRRIK---AEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFD 176
Cdd:PRK11174 444 LL-------------GNPDASDEQLQqalENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 177 EPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTH--DQHEAMsmsDRVAVMREGRILQLGTPEEI 239
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-239 |
4.55e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL---------------LALSPS-------- 73
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktkekekvlekLVIQKTrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 74 ---QRDCAMVFQ--SYALYpHMTVGGNIctpllmrglgfwgrlpgagLFSANTRRI-KAEAQASARKVAQSLGID-GLWE 146
Cdd:PRK13651 101 keiRRRVGVVFQfaEYQLF-EQTIEKDI-------------------IFGPVSMGVsKEEAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 147 RKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMR 226
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|...
gi 2536923639 227 EGRILQLGTPEEI 239
Cdd:PRK13651 240 DGKIIKDGDTYDI 252
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-238 |
5.04e-19 |
|
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: 88.72 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYpHMTVGG 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 95 NICtpllmrglgfWGRlPGAGlfsantrriKAEAQASARkVAQslgIDGLWERKPAQ-----------LSGGQRQRVALA 163
Cdd:COG5265 451 NIA----------YGR-PDAS---------EEEVEAAAR-AAQ---IHDFIESLPDGydtrvgerglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLhdQLGVTFIYVTH------DqheamsmSDRVAVMREGRILQLGTPE 237
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHA 577
|
.
gi 2536923639 238 E 238
Cdd:COG5265 578 E 578
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-237 |
6.85e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLlalspSQRDC-------AMVFQSyalyp 88
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-----NAENEkwvrskvGLVFQD----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 89 hmtvggnictpllmrglgfwgrlPGAGLFSA-----------NTRRIKAEAQasaRKVAQSLGIDGLW---ERKPAQLSG 154
Cdd:PRK13647 88 -----------------------PDDQVFSStvwddvafgpvNMGLDKDEVE---RRVEEALKAVRMWdfrDKPPYHLSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLG 234
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
...
gi 2536923639 235 TPE 237
Cdd:PRK13647 221 DKS 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-265 |
1.06e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.37 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCA--- 78
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNIctpllmrglgFWGRLPGAGLFSANTRRIKAEAQasarKVAQSLGIDGLWERKPAQLSGGQRQ 158
Cdd:PRK10762 83 IIHQELNLIPQLTIAENI----------FLGREFVNRFGRIDWKKMYAEAD----KLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 159 RVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRIlqlgtpee 238
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQF-------- 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 2536923639 239 IYTRP-ANLD----VARFVGA------PRINLLDGEVK 265
Cdd:PRK10762 220 IAEREvADLTedslIEMMVGRkledqyPRLDKAPGEVR 257
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-239 |
1.14e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSP---SQRDCAMVFQSY---ALYPHM 90
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITESRrdnGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 TVGGNICTPLLMRGLGFWGRLpgaGLFSANTRRIKAEAQasaRKVAQ----SLgidglwERKPAQLSGGQRQRVALARAM 166
Cdd:PRK09700 357 SIAQNMAISRSLKDGGYKGAM---GLFHEVDEQRTAENQ---RELLAlkchSV------NQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQL------GTPEEI 239
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQIltnrddMSEEEI 502
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-239 |
1.24e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYPHMTVggnictp 99
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTV------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 100 llmRGLGFWGRLP--GA-GLFSANTRRIKAEAQAsarkvaqSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFD 176
Cdd:PRK10575 103 ---RELVAIGRYPwhGAlGRFGAADREKVEEAIS-------LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 177 EPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-242 |
1.48e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKS-TLLKLIAGLDQPD----SGSIRLGERDLL-ALSPSQR-----DCAMVFQS--Y 84
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLhASEQTLRgvrgnKIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHMTVGGNICTPL-LMRGLGfwgRLPgaglfsANTRRIKAEAQASARKVAQSLGidglweRKPAQLSGGQRQRVALA 163
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLsLHRGMR---REA------ARGEILNCLDRVGIRQAAKRLT------DYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQ-------LGTP 236
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEqnraatlFSAP 248
|
....*.
gi 2536923639 237 EEIYTR 242
Cdd:PRK15134 249 THPYTQ 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-268 |
1.50e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 84.00 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 25 TVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgERDLLALSPSQRDcamvfqsyALYPhMTVggnicTPLLMrg 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIK--------ADYE-GTV-----RDLLS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 105 lgfwGRLPGAGlfsaNTRRIKAEaqasarkVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDA 184
Cdd:cd03237 84 ----SITKDFY----THPYFKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 185 NLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAV----------------MREG--RILqlgtpeeiytrpANL 246
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVfegepsvngvanppqsLRSGmnRFL------------KNL 216
|
250 260 270
....*....|....*....|....*....|.
gi 2536923639 247 DVArF-----VGAPRIN----LLDGEVKAHG 268
Cdd:cd03237 217 DIT-FrrdpeTGRPRINklgsVKDREQKESG 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-236 |
1.73e-18 |
|
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: 83.31 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RdcamvfQSYALYPHmtvggni 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlR------SRISIIPQ------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 cTPLLMRG-----LGFWGRLPGAGLFSAntrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:cd03244 86 -DPVLFSGtirsnLDPFGEYSDEELWQA-----LERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 172 VFLFDEPLSNLD----ANLRQALRGEIRqlhdqlGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTP 236
Cdd:cd03244 160 ILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
3.81e-18 |
|
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: 85.88 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ-RDCAM 79
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALYPHMTVGGNIctpLLMRGLG----FWGRLPGAGLFSantrrikaEAQASARKVAQSLGIDGlwerkpAQLSGG 155
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENL---RLARPDAtdeeLWAALERVGLAD--------WLRALPDGLDTVLGEGG------ARLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHD 211
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-239 |
4.63e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GE----RDLlalSPSQRDCAMVfQ 82
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQpvdaGDI---ATRRRVGYMS-Q 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNictpLLMRglgfwgrlpgAGLFSAntrrikAEAQASAR--KVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:NF033858 347 AFSLYGELTVRQN----LELH----------ARLFHL------PAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTfIYV-THDQHEAMSmSDRVAVMREGRILQLGTPEEI 239
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-230 |
6.48e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQR-DCAMVFQSY-----ALYPHMTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNIctpllmrglgfwgRLPGAGLFSANTRRIKAEAQasarKVAQSLGIDGLWERKPAQ------LSGGQRQRVALARAM 166
Cdd:PRK10762 348 KENM-------------SLTALRYFSRAGGSLKHADE----QQAVSDFIRLFNIKTPSMeqaiglLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQalrgEIRQLHDQL---GVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKK----EIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-246 |
7.05e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.29 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPDSGSIRLGERDLLALSP----------SQRD---CAM-VFQSYALy 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAaelarhraylSQQQtppFAMpVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 88 pHMTVGGNIctpllmrglgfwgrlpgaglfsantrrikAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALAramv 167
Cdd:PRK03695 93 -HQPDKTRT-----------------------------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 168 rrpAVFL--------------FDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQL 233
Cdd:PRK03695 139 ---AVVLqvwpdinpagqlllLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
250
....*....|...
gi 2536923639 234 GTPEEIYTrPANL 246
Cdd:PRK03695 215 GRRDEVLT-PENL 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-190 |
8.27e-18 |
|
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: 84.99 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDcamvfqs 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 yALYPHMTVggnictpllmrglgfWGRLP-GAGLFSANTRRIKAEAQASA---RKVAQslgidglwERKPAQLSGGQRQR 159
Cdd:TIGR03719 396 -ALDPNKTV---------------WEEISgGLDIIKLGKREIPSRAYVGRfnfKGSDQ--------QKKVGQLSGGERNR 451
|
170 180 190
....*....|....*....|....*....|..
gi 2536923639 160 VALARaMVRRPA-VFLFDEPLSNLDANLRQAL 190
Cdd:TIGR03719 452 VHLAK-TLKSGGnVLLLDEPTNDLDVETLRAL 482
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-243 |
2.27e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 82.10 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKV-IKGLD---LTVRDGEFLTLLGSSGCGKSTLLKLIAGL-DQPD---SGSIRLGERDLLALSP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGrvmAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 73 SQR------DCAMVFQS--YALYPHMTVGGNICTPLLMRGLGfwgrlpgaglfSANTRRikaeaqASARKVAQSLGIDGL 144
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG-----------NKKTRR------QRAIDLLNQVGIPDP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 145 WER---KPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDR 221
Cdd:PRK11022 144 ASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHK 223
|
250 260
....*....|....*....|..
gi 2536923639 222 VAVMREGRILQLGTPEEIYTRP 243
Cdd:PRK11022 224 IIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-234 |
3.18e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLAlspsQRDcamVFQSYA 85
Cdd:PRK13538 4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR----QRD---EYHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 86 LY--------PHMTVGGNictpllmrgLGFWGRLPGaglfsantrrikaeaQASARKVAQSLGIDGL--WERKPA-QLSG 154
Cdd:PRK13538 77 LYlghqpgikTELTALEN---------LRFYQRLHG---------------PGDDEALWEALAQVGLagFEDVPVrQLSA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQlHDQLGVTFIYVTHdqHEAMSMSDRVavmregRILQLG 234
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ-HAEQGGMVILTTH--QDLPVASDKV------RKLRLG 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-262 |
3.79e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 81.71 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLlKLIAGLDQPDSGSirlgerdllalsPSQRDCAMVFQS 83
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR------------RPWRF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALypHMTVGGNicTPLLM-RGLGFWGRlPGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVAL 162
Cdd:NF000106 81 RAL--RRTIG*H--RPVR*gRRESFSGR-ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT- 241
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTk 234
|
250 260 270
....*....|....*....|....*....|
gi 2536923639 242 --------RPAN-LDVARFVGAPRINLLDG 262
Cdd:NF000106 235 vggrtlqiRPAHaAELDRMVGAIAQAGLDG 264
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-229 |
4.11e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.47 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LGERDLLALSPSQRD--CAMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIDFKSSKEALEngISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNIctpllmrglgfW-GRLPGAGLFSANTRRIKaeaqaSARKVAQSLGIDGLWERKPAQLSGGQRQRVA 161
Cdd:PRK10982 81 ELNLVLQRSVMDNM-----------WlGRYPTKGMFVDQDKMYR-----DTKAIFDELDIDIDPRAKVATLSVSQMQMIE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 162 LARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-252 |
4.24e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLK-------LIAGLDQpdSGSIRLGERDLLA--LSPSQ--RDCAMVF 81
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYApdVDPVEvrRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHmTVGGNIctpllmrglGFWGRLPGaglFSANTRRIkaeaqasarkVAQSLGIDGLWE------RKPAQ-LSG 154
Cdd:PRK14243 98 QKPNPFPK-SIYDNI---------AYGARING---YKGDMDEL----------VERSLRQAALWDevkdklKQSGLsLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTHDQHEAMSMSDRVAVM--------- 225
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnvelteggg 232
|
250 260
....*....|....*....|....*..
gi 2536923639 226 REGRILQLGTPEEIYTRPANLDVARFV 252
Cdd:PRK14243 233 RYGYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-250 |
5.35e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.74 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 19 IKGLDLTVRDGEFLTLLGSSGCGKStlLKLIAGLDQPDSGSIRLGERDLL---ALSPSQ---RDCAMVFQS--YALYPHM 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLdgkPVAPCAlrgRKIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 91 TVGGNICTPLLMRGLgfwgrlpgaglfsantrrikaeaQASARKVAQSLGIDGLWERK------PAQLSGGQRQRVALAR 164
Cdd:PRK10418 97 TMHTHARETCLALGK-----------------------PADDATLTAALEAVGLENAArvlklyPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 165 AMVRRpAVFLF-DEPLSNLDAnLRQA----LRGEIRQLHDqLGVtfIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK10418 154 ALLCE-APFIIaDEPTTDLDV-VAQArildLLESIVQKRA-LGM--LLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
250
....*....|.
gi 2536923639 240 YTRPANlDVAR 250
Cdd:PRK10418 229 FNAPKH-AVTR 238
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-230 |
8.03e-17 |
|
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: 78.07 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 11 KQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPD---SGSIRLGERDLL-ALSPSQRDCAMVFQSYAL 86
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKeFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 87 YPHMTVGGNICTPLLMRGlgfwgrlpgaglfSANTRRIkaeaqasarkvaqslgidglwerkpaqlSGGQRQRVALARAM 166
Cdd:cd03233 95 FPTLTVRETLDFALRCKG-------------NEFVRGI----------------------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLG-VTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-238 |
8.27e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 27 RDGEFLTLLGSSGCGKSTLLKLIAGLDQPD---SGSIRL-GERdlLALSPSQRDCAMVFQSYALYPHMTVggnictpllM 102
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLnGMP--IDAKEMRAISAYVQQDDLFIPTLTV---------R 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 103 RGLGFWGRLPGAGLFSANTRRIKAEA---QASARKVAQSL-GIDGLWErkpaQLSGGQRQRVALARAMVRRPAVFLFDEP 178
Cdd:TIGR00955 118 EHLMFQAHLRMPRRVTKKEKRERVDEvlqALGLRKCANTRiGVPGRVK----GLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 179 LSNLDA----NLRQALRGEIrqlhdQLGVTFIYVTHD-QHEAMSMSDRVAVMREGRILQLGTPEE 238
Cdd:TIGR00955 194 TSGLDSfmaySVVQVLKGLA-----QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
9.16e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.77 E-value: 9.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQ---RDC 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 78 AMVFQSYALYPHMTVGGNictpllmrglgfwgrLPGAGLFsantrrikAEAQASARKVAQSLGI-DGLWERK---PAQLS 153
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEEN---------------LAMGGFF--------AERDQFQERIKWVYELfPRLHERRiqrAGTMS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRIL 231
Cdd:PRK11614 140 GGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-268 |
3.86e-16 |
|
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: 79.83 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTK--VIKGldlTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdlLA-----LSPSQrd 76
Cdd:COG1245 342 VEYPDLTKSYGGFSleVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--ISykpqyISPDY-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 77 camvfqsyalypHMTVGGNictpllmrglgfwgrlpgagLFSANTRRI-----KAEaqasarkVAQSLGIDGLWERKPAQ 151
Cdd:COG1245 415 ------------DGTVEEF--------------------LRSANTDDFgssyyKTE-------IIKPLGLEKLLDKNVKD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDqheaMSM----SDRVAV--- 224
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVfeg 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 225 -------------MREG--RILqlgtpeeiytrpANLDVArF-----VGAPRIN----LLDGEVKAHG 268
Cdd:COG1245 532 epgvhghasgpmdMREGmnRFL------------KELGIT-FrrdeeTGRPRINkpgsYLDREQKERG 586
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-210 |
9.48e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.11 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSI-RLGERDLLALSpsQRdcamvfqsyalyPHMTVG 93
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLP--QR------------PYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 ---GNICTPllmrglgfwgrlpgaglfsantrrikaeaqasarkvaqslgidglWERKpaqLSGGQRQRVALARAMVRRP 170
Cdd:cd03223 79 tlrEQLIYP---------------------------------------------WDDV---LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2536923639 171 AVFLFDEPLSNLDANLRQALrgeiRQLHDQLGVTFIYVTH 210
Cdd:cd03223 111 KFVFLDEATSALDEESEDRL----YQLLKELGITVISVGH 146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-241 |
1.22e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGlDQPDS---------GSIRLGERDLLALSPSQRDCAMVFQSYALYP 88
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 89 HMtvggnictPLLMRGLGFWGRLPGA---GLFSANTRRIKAEAQASArkvaqslGIDGLWERKPAQLSGGQRQRVALARA 165
Cdd:PRK13547 95 AF--------AFSAREIVLLGRYPHArraGALTHRDGEIAWQALALA-------GATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 166 M---------VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTP 236
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
....*
gi 2536923639 237 EEIYT 241
Cdd:PRK13547 240 ADVLT 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-234 |
1.90e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDS--GSIRLGERDLlaLSPSQRDCAMVFQS 83
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP--TKQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNICTPLLMrglgfwgRLPgaglfSANTRRIKAEAqasARKVAQSLG--------IDGLWERKpaqLSGG 155
Cdd:PLN03211 149 DILYPHLTVRETLVFCSLL-------RLP-----KSLTKQEKILV---AESVISELGltkcentiIGNSFIRG---ISGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHdQLGVTFIYVTHD-QHEAMSMSDRVAVMREGRILQLG 234
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-230 |
3.88e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 24 LTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPsqRD--------CAMVFQSYALYPHMTVGGN 95
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP--RDairagimlCPEDRKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 I---CTPLLMRglgfwgrlpgAGLFSANtrriKAEAQaSARKVAQSLGIDglwERKPAQ----LSGGQRQRVALARAMVR 168
Cdd:PRK11288 352 InisARRHHLR----------AGCLINN----RWEAE-NADRFIRSLNIK---TPSREQlimnLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2536923639 169 RPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-212 |
3.92e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAG--LDQPDSGSIRLGErdllalSPSQRDCAMVfqsYALYPHMTVG 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPD------NQFGREASLI---DAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 94 GNIctpllmrglgfwGRLPGAGLfsantrrikAEAQasarkvaqslgidgLWERKPAQLSGGQRQRVALARAMVRRPAVF 173
Cdd:COG2401 114 DAV------------ELLNAVGL---------SDAV--------------LWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2536923639 174 LFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQ 212
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-262 |
4.70e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKV-IKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LGERDLLALSpsQRDCAM 79
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISiLGQPTRQALQ--KNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSYALyphmtvggNICTPLLMRGLGFWGRLPGAGLFsantRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQR 159
Cdd:PRK15056 83 VPQSEEV--------DWSFPVLVEDVVMMGRYGHMGWL----RRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDrVAVMREGRILQLGTPEEI 239
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETT 228
|
250 260
....*....|....*....|...
gi 2536923639 240 YTrPANLDVArFVGAPRINLLDG 262
Cdd:PRK15056 229 FT-AENLELA-FSGVLRHVALNG 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-239 |
5.35e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 3 DIHISGLTKQFGNTK-VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAM 79
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 80 VFQSyalyphmtvggnictPLLMrglgfwgrlpgAGLFSANT---RRIKAEAQASARKVAQSLGI-----DGLWERKPAQ 151
Cdd:PRK10790 420 VQQD---------------PVVL-----------ADTFLANVtlgRDISEEQVWQALETVQLAELarslpDGLYTPLGEQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 ---LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlgVTFIYVTHdQHEAMSMSDRVAVMREG 228
Cdd:PRK10790 474 gnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLHRG 550
|
250
....*....|.
gi 2536923639 229 RILQLGTPEEI 239
Cdd:PRK10790 551 QAVEQGTHQQL 561
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-239 |
7.17e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTK-VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYpH 89
Cdd:PRK13657 344 YDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIrtVTRASLRRNIAVVFQDAGLF-N 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNIctpllmrglgfwgRLPGAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRR 169
Cdd:PRK13657 423 RSIEDNI-------------RVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 170 PAVFLFDEPLSNLD----ANLRQALRgEIRQLHdqlgVTFIyVTHdQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK13657 490 PPILILDEATSALDveteAKVKAALD-ELMKGR----TTFI-IAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-233 |
9.88e-15 |
|
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: 75.36 E-value: 9.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 5 HISGLTKQF-GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerdllalSPSQRdCAMVFQS 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QPGIK-VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNIctpllMRGLGFWGRL-------------PGAGLFSANTRRIKAEAQASA-------RKVAQSlgIDG 143
Cdd:TIGR03719 77 PQLDPTKTVRENV-----EEGVAEIKDAldrfneisakyaePDADFDKLAAEQAELQEIIDAadawdldSQLEIA--MDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 144 L----WERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRgeiRQLHDQLGvTFIYVTHDQHeamsMS 219
Cdd:TIGR03719 150 LrcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPG-TVVAVTHDRY----FL 221
|
250
....*....|....
gi 2536923639 220 DRVAvmreGRILQL 233
Cdd:TIGR03719 222 DNVA----GWILEL 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-239 |
1.24e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYpHMTV 92
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLASLRNQVALVSQNVHLF-NDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GGNICtpllmrglgfwgrlpgaglFSANTRRIKAEAQASArKVAQSL--------GIDGLWERKPAQLSGGQRQRVALAR 164
Cdd:PRK11176 434 ANNIA-------------------YARTEQYSREQIEEAA-RMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 165 AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLhdQLGVTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-243 |
2.71e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQF----GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPD----SGSIRLGERDLLALSP 72
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 73 SQR------DCAMVFQ--SYALYPHMTVGGNictplLMRGLGFW---GRLpgAGLFSANTRRikaeaqasARKVAQSLGI 141
Cdd:PRK15093 81 RERrklvghNVSMIFQepQSCLDPSERVGRQ-----LMQNIPGWtykGRW--WQRFGWRKRR--------AIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 142 ---DGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSM 218
Cdd:PRK15093 146 kdhKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
250 260
....*....|....*....|....*
gi 2536923639 219 SDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-268 |
3.87e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 7 SGLTKQFGNTK--VIKGldlTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdlLALSPsqrdcamvfQSY 84
Cdd:PRK13409 344 PDLTKKLGDFSleVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKP---------QYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHMTVGgnictpllmrglgfwgrlpgAGLFSANTR----RIKAEaqasarkVAQSLGIDGLWERKPAQLSGGQRQRV 160
Cdd:PRK13409 410 KPDYDGTVE--------------------DLLRSITDDlgssYYKSE-------IIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAV---------------- 224
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVfegepgkhghasgpmd 542
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 225 MREG--RILqlgtpeeiytrpANLDVArF-----VGAPRIN----LLDGEVKAHG 268
Cdd:PRK13409 543 MREGmnRFL------------KELGIT-FrrdeeTGRPRVNkpgsYLDREQKERG 584
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-211 |
4.51e-14 |
|
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: 71.24 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 25 TVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDsgsirLGERDLlalSPSQRDCAMVFQSYALYPHMT--VGGNICTpllM 102
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGKFDD---PPDWDEILDEFRGSELQNYFTklLEGDVKV---I 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 103 RGLGFWGRLPGAglFSANTRRI--KAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLS 180
Cdd:cd03236 91 VKPQYVDLIPKA--VKGKVGELlkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|.
gi 2536923639 181 NLDANLRQALRGEIRQLHDQlGVTFIYVTHD 211
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-238 |
1.06e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.23 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPsqRDCAMVF-QSY 84
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYA--QDHAYDFeNDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 85 ALYPHM----TVGGNIctpLLMRglGFWGRLpgagLFSANtrrikaEAQASArKVaqslgidglwerkpaqLSGGQRQRV 160
Cdd:PRK15064 400 TLFDWMsqwrQEGDDE---QAVR--GTLGRL----LFSQD------DIKKSV-KV----------------LSGGEKGRM 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 161 ALARAMVRRPAVFLFDEPLSNLD----ANLRQALrgeirqlhDQLGVTFIYVTHDQHEAMSMSDRVAVMREGRILQ-LGT 235
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDmesiESLNMAL--------EKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGT 519
|
...
gi 2536923639 236 PEE 238
Cdd:PRK15064 520 YEE 522
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-190 |
1.20e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDcamvfqs 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRD------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 yALYPHMTVGGNICTpllmrglgfwgrlpGAGLFSANTRRIKAEAQASArkvaqsLGIDGLWERKPA-QLSGGQRQRVAL 162
Cdd:PRK11819 398 -ALDPNKTVWEEISG--------------GLDIIKVGNREIPSRAYVGR------FNFKGGDQQKKVgVLSGGERNRLHL 456
|
170 180
....*....|....*....|....*....
gi 2536923639 163 ARaMVRRPA-VFLFDEPLSNLDANLRQAL 190
Cdd:PRK11819 457 AK-TLKQGGnVLLLDEPTNDLDVETLRAL 484
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-251 |
1.84e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPS--QRDCAMVFQSYALYphmtvggnictp 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAVFTDFHLF------------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 100 llmrglgfwGRLPGAGLFSANTRRIkaEAQASARKVAQSLGIDGlWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPL 179
Cdd:PRK10522 410 ---------DQLLGPEGKPANPALV--EKWLERLKMAHKLELED-GRISNLKLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 180 SNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHeAMSMSDRVAVMREGRILQL-GTPEEIYTRPAnldVARF 251
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH-YFIHADRLLEMRNGQLSELtGEERDAASRDA---VART 546
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-237 |
4.26e-13 |
|
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: 70.60 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdllALSPSQRDC-----AMVFQSYALYPHMtvggni 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAyrqlfSAVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 ctpllmrgLGFWGrlpgaglfsantrrikAEAQASARKVAQSLGIDglweRKPA---------QLSGGQRQRVALARAMV 167
Cdd:COG4615 422 --------LGLDG----------------EADPARARELLERLELD----HKVSvedgrfsttDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 168 -RRPaVFLFDEPLSNLDANLRQ--------ALRgeirqlhdQLGVTFIYVTHDQHeAMSMSDRVAVMREGRILQLGTPE 237
Cdd:COG4615 474 eDRP-ILVFDEWAADQDPEFRRvfytellpELK--------ARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGPA 542
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
22-232 |
4.58e-13 |
|
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: 70.37 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerDLLALSPSQRD-----CAMVFQSYALYPHMTVGGNI 96
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILL---DGAAVSADSRDdyrdlFSAIFADFHLFDDLIGPDEG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 CTPLLMRGLGFWGRLpgaglfsantrrikaeaqasarKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFD 176
Cdd:TIGR01194 438 EHASLDNAQQYLQRL----------------------EIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 177 EPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQhEAMSMSDRVAVMREGRILQ 232
Cdd:TIGR01194 496 EWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCIVK 550
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-236 |
5.14e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.44 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 3 DIHISGLTKQFGN--TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLlalspSQRDCAMV 80
Cdd:cd03369 6 EIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----STIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALYPHMTVggnictpllmrglgfwgrlpgagLFSANTR-RIKAEAQASARKVAQSLGIDGLWErkpaQLSGGQRQR 159
Cdd:cd03369 81 RSSLTIIPQDPT-----------------------LFSGTIRsNLDPFDEYSDEEIYGALRVSEGGL----NLSQGQRQL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 160 VALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDQHEAMSMsDRVAVMREGRILQLGTP 236
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-230 |
8.18e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDS-GSIRLGERDLLALSPSQ---RDCAMVFQS---YALYPH 89
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNICTPLLMRgLGFWGRLPGAglfsANTRRIKAEAQASARKVAQSlgidglwERKPAQLSGGQRQRVALARAMVRR 169
Cdd:PRK13549 356 MGVGKNITLAALDR-FTGGSRIDDA----AELKTILESIQRLKVKTASP-------ELAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 170 PAVFLFDEPLSNLDANLRQalrgEIRQLHDQL---GVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKY----EIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-230 |
1.95e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 68.73 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 21 GLDLTVRdgefLTLLGSSGCGKSTLLKLIAGLDQPDSGSIrlgerdllALSPSQRdcAMVFQSyalypHMTVGGNIC-TP 99
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV--------FRSAKVR--MAVFSQ-----HHVDGLDLSsNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 100 LLMRGLGFwgrlPGAglfsantrrikaeAQASARKVAQSLGIDGLWERKPA-QLSGGQRQRVALARAMVRRPAVFLFDEP 178
Cdd:PLN03073 592 LLYMMRCF----PGV-------------PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 179 LSNLDANLRQALrgeIRQLH-DQLGVtfIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PLN03073 655 SNHLDLDAVEAL---IQGLVlFQGGV--LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-234 |
6.31e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.20 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLD--QPDSGSIRLGERDLLALSPSQRDCAMVFQSYAlYP----- 88
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQ-YPveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 89 ---HMTVGGNICTPLLMRGLGFWGRLPGAGLFSANTRRIKAEAQASARKVaqSLGidglwerkpaqLSGGQRQRVALARA 165
Cdd:PRK09580 93 vsnQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSV--NVG-----------FSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 166 MVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMS-DRVAVMREGRILQLG 234
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-242 |
6.71e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYPHmTVGGN 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakFGLTDLRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTPLLMRGLGFWGRLPGAGLFSANTRrikaeaqasarkvaQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIKDVIDR--------------NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 176 DEPLSNLDANLRQALRGEIRQlhDQLGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-230 |
8.75e-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: 66.39 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGL-DQPDSGSIRLGERDLLALSPSQ---RDCAMVFQS---YALYPH 89
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNICTPLLMRglgfwgrlpgaglFSANTRRIKAEAQASARKVAQSLGIDGLWERKP-AQLSGGQRQRVALARAMVR 168
Cdd:TIGR02633 354 LGVGKNITLSVLKS-------------FCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 169 RPAVFLFDEPLSNLDAnlrqALRGEIRQLHDQL---GVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:TIGR02633 421 NPRVLILDEPTRGVDV----GAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-242 |
8.90e-12 |
|
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: 66.89 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLK-LIAGLDQPDsGSIRLgeRDLLALSPSQrdcaMVFQ 82
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHM--KGSVAYVPQQ----AWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 SYALYPHMTVGGNICTPLLMRGLGFWGRLPGAGLFSANTRRIKAEaqasarkvaqslgidglwerKPAQLSGGQRQRVAL 162
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGE--------------------KGVNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQL-GVTFIYVTHDQhEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
.
gi 2536923639 242 R 242
Cdd:TIGR00957 851 R 851
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-242 |
1.35e-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: 66.58 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTK--VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLAlspsqrDCAMVF 81
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYPHMTVGGNICTPllMRGLGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVA 161
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTG--REHLYLYARLRGVP---------AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 162 LARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
.
gi 2536923639 242 R 242
Cdd:TIGR01257 2160 K 2160
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-239 |
1.82e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 133 RKVAQSLGIDGLWERKPAQ-----------LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQL 201
Cdd:PTZ00265 1329 KRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1408
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2536923639 202 GVTFIYVTHdQHEAMSMSDRVAVM----REGRILQL-GTPEEI 239
Cdd:PTZ00265 1409 DKTIITIAH-RIASIKRSDKIVVFnnpdRTGSFVQAhGTHEEL 1450
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-222 |
1.88e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGlDQP-DSGSIRLgERDL----LALSPSQR 75
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIY-EQDLivarLQQDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 DCAMVF---------QSYAL--YPHMT--VGGNICTPLLMRGLGFWGRLPGAGLFSANTRrIKaeaqasarKVAQSLGID 142
Cdd:PRK11147 79 VEGTVYdfvaegieeQAEYLkrYHDIShlVETDPSEKNLNELAKLQEQLDHHNLWQLENR-IN--------EVLAQLGLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 143 GlwERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDAN----LRQAL---RGEIrqlhdqlgvtfIYVTHDQHEA 215
Cdd:PRK11147 150 P--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIEtiewLEGFLktfQGSI-----------IFISHDRSFI 216
|
....*..
gi 2536923639 216 MSMSDRV 222
Cdd:PRK11147 217 RNMATRI 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
152-239 |
2.17e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANL-RQA----LRGEIRqlhdqlGVTFIYVTHDQHeAMSMSDRVAVMR 226
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVfdkcIKDELR------GKTRVLVTNQLH-FLSQVDRIILVH 813
|
90
....*....|...
gi 2536923639 227 EGRILQLGTPEEI 239
Cdd:PLN03130 814 EGMIKEEGTYEEL 826
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-211 |
2.29e-11 |
|
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: 65.19 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 25 TVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIrlgERDllalsPSQRDCAMVFQSYALYPHMT--VGGNICT---P 99
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEE-----PSWDEVLKRFRGTELQDYFKklANGEIKVahkP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 100 LLMRglgfwgRLPGAglFSANTRRI--KAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDE 177
Cdd:COG1245 167 QYVD------LIPKV--FKGTVRELleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....
gi 2536923639 178 PLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHD 211
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-211 |
3.79e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 5 HISGLTKQFGNTKVI-KGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerdllalSPSQRdCAMVFQS 83
Cdd:PRK11819 8 TMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGIK-VGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 84 YALYPHMTVGGNIctpllMRGLGfwgrlpgaGLFSANTR--RIK---AEAQASARKVAQSLG-----ID--GLWE----- 146
Cdd:PRK11819 79 PQLDPEKTVRENV-----EEGVA--------EVKAALDRfnEIYaayAEPDADFDALAAEQGelqeiIDaaDAWDldsql 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 147 -------RKP------AQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRgeiRQLHDQLGvTFIYVTHD 211
Cdd:PRK11819 146 eiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE---QFLHDYPG-TVVAVTHD 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-239 |
4.84e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 1 MPDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGldqpdsgsirlgerDLLALSpSQRDCAmv 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG--------------ELPLLS-GERQSQ-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 FQSYALyphmtvggnictpllmrgLGF----------WGRL------PGAGLFSANTRR-IKAEAQASAR--KVAQSLGI 141
Cdd:PRK10938 64 FSHITR------------------LSFeqlqklvsdeWQRNntdmlsPGEDDTGRTTAEiIQDEVKDPARceQLAQQFGI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 142 DGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDR 221
Cdd:PRK10938 126 TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQF 204
|
250
....*....|....*...
gi 2536923639 222 VAVMREGRILQLGTPEEI 239
Cdd:PRK10938 205 AGVLADCTLAETGEREEI 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-229 |
8.08e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 8 GLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPD---SGSIRL-GE----RDllaLSPS-QRDCA 78
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFdGEvcrfKD---IRDSeALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 79 MVFQSYALYPHMTVGGNIctpllmrglgFWGRLPGAGLFsANTRRIKAEAQASARKVaqslgidGLWERkPAQLSG---- 154
Cdd:NF040905 82 IIHQELALIPYLSIAENI----------FLGNERAKRGV-IDWNETNRRARELLAKV-------GLDES-PDTLVTdigv 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 155 GQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGR 229
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-252 |
1.16e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIR-LG-------ERDllALSPsqr 75
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGgdmadarHRR--AVCP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 76 DCAMVFQSYA--LYPHMTVGGNIctpllmrglGFWGRLPGAGlfsantrriKAEAQASARKVAQSLGIDGLWERKPAQLS 153
Cdd:NF033858 77 RIAYMPQGLGknLYPTLSVFENL---------DFFGRLFGQD---------AAERRRRIDELLRATGLAPFADRPAGKLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEP------LSNldanlRQ--ALRGEIRQLHDQLGVtfIYVTHDQHEAMSMsDRVAVM 225
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPttgvdpLSR-----RQfwELIDRIRAERPGMSV--LVATAYMEEAERF-DWLVAM 210
|
250 260
....*....|....*....|....*....
gi 2536923639 226 REGRILQLGTPEEIY--TRPANLDVArFV 252
Cdd:NF033858 211 DAGRVLATGTPAELLarTGADTLEAA-FI 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-215 |
1.48e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 12 QFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGlDQPDSGSIRL---GER--------DLlalspsQRDCAMV 80
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSNDLtlfGRRrgsgetiwDI------KKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 81 fqSYALYPHMTVGGNICTPLLMrglGFWGRLpgaGLFSANTRRikaeaqasARKVAQS----LGIDGLWERKPAQ-LSGG 155
Cdd:PRK10938 342 --SSSLHLDYRVSTSVRNVILS---GFFDSI---GIYQAVSDR--------QQKLAQQwldiLGIDKRTADAPFHsLSWG 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 156 QrQRVAL-ARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEA 215
Cdd:PRK10938 406 Q-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-240 |
1.57e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLkliagldqpdsgSIRLGErdllaLSPSQRDCAMVFQSYALYPHM------TVGGN 95
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLI------------SAMLGE-----LSHAETSSVVIRGSVAYVPQVswifnaTVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTPLLMRGLGFWgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKpAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:PLN03232 699 ILFGSDFESERYW-------------RAIDVTALQHDLDLLPGRDLTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 176 DEPLSNLDANL-RQALRGEIRqlHDQLGVTFIYVTHDQHeAMSMSDRVAVMREGRILQLGTPEEIY 240
Cdd:PLN03232 765 DDPLSALDAHVaHQVFDSCMK--DELKGKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-230 |
2.92e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 17 KVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIrLGERDLlALSPSQrdcamvfqsyALYPHMTVGGNI 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSI-AYVPQQ----------AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 97 CtpllmrglgFWGRLPGAGLFSAnTRRIKAEAQasarkVAQ-SLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:PTZ00243 742 L---------FFDEEDAARLADA-VRVSQLEAD-----LAQlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 176 DEPLSNLDAN-----LRQALRGEIRqlhdqlGVTFIYVTHDQHeAMSMSDRVAVMREGRI 230
Cdd:PTZ00243 807 DDPLSALDAHvgervVEECFLGALA------GKTRVLATHQVH-VVPRADYVVALGDGRV 859
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-211 |
2.97e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 25 TVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDsgsirLGERDllalSPSQRDcaMVFQSYA---LYPHMT--VGGNIctp 99
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYE----EEPSWD--EVLKRFRgteLQNYFKklYNGEI--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 100 llmrglgfwgR----------LPGAglFSANTRRI--KAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMV 167
Cdd:PRK13409 161 ----------KvvhkpqyvdlIPKV--FKGKVRELlkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2536923639 168 RRPAVFLFDEPLSNLDanLRQALRGE--IRQLHDqlGVTFIYVTHD 211
Cdd:PRK13409 229 RDADFYFFDEPTSYLD--IRQRLNVArlIRELAE--GKYVLVVEHD 270
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-243 |
3.10e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYPHmTVGGN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtkLQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTpllmrglgfwGRlPGAglfsantrrIKAEAQASAR---------KVAQslGIDGLWERKPAQLSGGQRQRVALARAM 166
Cdd:PRK10789 409 IAL----------GR-PDA---------TQQEIEHVARlasvhddilRLPQ--GYDTEVGERGVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 167 VRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLgvTFIYVTHdQHEAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-183 |
8.55e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA---LSPSQRDCAMVFQSYALYPHmT 91
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinLKWWRSKIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 92 VGGNICTPLL-MRGLGFWG--------------------RLPGAGLFSANTRRIKAEAQASARK------------VAQS 138
Cdd:PTZ00265 476 IKNNIKYSLYsLKDLEALSnyynedgndsqenknkrnscRAKCAGDLNDMSNTTDSNELIEMRKnyqtikdsevvdVSKK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2536923639 139 LGI-----------DGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLD 183
Cdd:PTZ00265 556 VLIhdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-243 |
9.67e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.10 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdlLALSPsqrdcamvfQSYALYPHmTVGGN 95
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSS---------QFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICtpllmrglgfwgrlpgAGLfSANTRRIKAEAQAS---------ARKVAQSLGIDGLwerkpaQLSGGQRQRVALARAM 166
Cdd:cd03291 118 II----------------FGV-SYDEYRYKSVVKACqleeditkfPEKDNTVLGEGGI------TLSGGQRARISLARAV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 167 VRRPAVFLFDEPLSNLD-ANLRQALRGEIRQLhdQLGVTFIYVThDQHEAMSMSDRVAVMREGRILQLGTPEEIYT-RP 243
Cdd:cd03291 175 YKDADLYLLDSPFGYLDvFTEKEIFESCVCKL--MANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSlRP 250
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-183 |
1.01e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 2 PDIHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerDLLALSPSQRDCAMVF 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI---DGKTATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSY--ALYPHMTVggnictpllMRGLGFWGRLPGaglfsantRRIKaeaqasaRKVAQSLGIDGLWERKPA---QLSGGQ 156
Cdd:PRK13543 87 LGHlpGLKADLST---------LENLHFLCGLHG--------RRAK-------QMPGSALAIVGLAGYEDTlvrQLSAGQ 142
|
170 180
....*....|....*....|....*..
gi 2536923639 157 RQRVALARAMVRRPAVFLFDEPLSNLD 183
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-237 |
1.31e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGldQPD----SGSIRLGERDLLALSPSQRDCAMVF 81
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYAlYPhMTVGGNICTPLLMrglgfwgrlpgaglFSANTRRI-----KAEAQASARKVAQSLGIDGLwerKPAQL---- 152
Cdd:CHL00131 88 LAFQ-YP-IEIPGVSNADFLR--------------LAYNSKRKfqglpELDPLEFLEIINEKLKLVGM---DPSFLsrnv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 153 ----SGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQH--EAMSmSDRVAVMR 226
Cdd:CHL00131 149 negfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRllDYIK-PDYVHVMQ 226
|
250
....*....|.
gi 2536923639 227 EGRILQLGTPE 237
Cdd:CHL00131 227 NGKIIKTGDAE 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-230 |
1.69e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 13 FGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSpSQRDCAMVFQSYALYPHMTv 92
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYF-AQHQLEFLRADESPLQHLA- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 ggnictpllmrglgfwgrlpgaglfsantRRIKAEAQASARKVAQSLGIDGLWERKP-AQLSGGQRQRVALARAMVRRPA 171
Cdd:PRK10636 400 -----------------------------RLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 172 VFLFDEPLSNLDANLRQALRGEIRQLHDQLGVtfiyVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDFEGALVV----VSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-220 |
1.91e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 29 GEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA-LSPSQRDCAMVFQSYALYPHMTVGGNiCtpllmrglgf 107
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLREN-C---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 108 wgrlpgagLFSANTRRIKAEAQASARKVAQSLGID---GLwerkpaqLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDA 184
Cdd:PRK13540 96 --------LYDIHFSPGAVGITELCRLFSLEHLIDypcGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2536923639 185 NLRQALRGEIRQLHDQLGVtfIYVTHDQHEAMSMSD 220
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-183 |
2.72e-09 |
|
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: 59.15 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 16 TKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERdlLALSP--------SQRDCAMVFQSYALY 87
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPqtswimpgTIKDNIIFGLSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 88 PHMTVggnictpllmrglgfwgrlpgaglfsANTRRIKAEAQASARKVAQSLGIDGLwerkpaQLSGGQRQRVALARAMV 167
Cdd:TIGR01271 517 RYTSV--------------------------IKACQLEEDIALFPEKDKTVLGEGGI------TLSGGQRARISLARAVY 564
|
170
....*....|....*.
gi 2536923639 168 RRPAVFLFDEPLSNLD 183
Cdd:TIGR01271 565 KDADLYLLDSPFTHLD 580
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
146-222 |
6.33e-09 |
|
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: 55.02 E-value: 6.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 146 ERKPAQLSGGQRQRVALARAMVRRP--AVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQhEAMSMSDRV 222
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNL-DVLSSADWI 158
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
152-224 |
6.93e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.89 E-value: 6.93e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQLGVTFIYVTHDQHEAMSMSDRVAV 224
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-183 |
8.46e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 12 QFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALspsqrdcamvFQSY--ALYPH 89
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAY----------FDQHraELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNIctpllmrglgfwgrlpGAGlfsantrriKAEAQASARKvAQSLGI--DGLWERKPAQ-----LSGGQRQRVAL 162
Cdd:PRK11147 398 KTVMDNL----------------AEG---------KQEVMVNGRP-RHVLGYlqDFLFHPKRAMtpvkaLSGGERNRLLL 451
|
170 180
....*....|....*....|.
gi 2536923639 163 ARAMVRRPAVFLFDEPLSNLD 183
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD 472
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-228 |
8.70e-09 |
|
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: 55.41 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQRDCAMVFQ-SYALYP----H 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAAQKpwllN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 90 MTVGGNIC--TPLlmrglgfwgrlpgaglfsaNTRRIKAEAQASARKVAQSLGIDG----LWERKpAQLSGGQRQRVALA 163
Cdd:cd03290 93 ATVEENITfgSPF-------------------NKQRYKAVTDACSLQPDIDLLPFGdqteIGERG-INLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 164 RAMVRRPAVFLFDEPLSNLDANLRQAL--RGEIRQLHDQlGVTFIYVTHdQHEAMSMSDRVAVMREG 228
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDD-KRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-190 |
1.33e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLALSPSQrdCAMVFQSYALYPHMTVGG 94
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 95 NictpllmrgLGFWgrlpgaglfsantrrikAEAQASARKVAQSL---GIDGLWERKPAQLSGGQRQRVALARAMVRRPA 171
Cdd:PRK13541 90 N---------LKFW-----------------SEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSD 143
|
170
....*....|....*....
gi 2536923639 172 VFLFDEPLSNLDANLRQAL 190
Cdd:PRK13541 144 LWLLDEVETNLSKENRDLL 162
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-243 |
1.95e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDLLA--LSPSQRDCAMVFQSYALYPHmTVGGN 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ICTPLLMRGLGFWGRLPGAGLfsantrrikaeaqaSARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVF-L 174
Cdd:PTZ00243 1404 VDPFLEASSAEVWAALELVGL--------------RERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFiL 1469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 175 FDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVTHDQHeAMSMSDRVAVMREGRILQLGTPEEIYTRP 243
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLH-TVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-239 |
6.56e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 18 VIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL--LALSPSQRDCAMVFQSYALYPHmTVGGN 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskFGLMDLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 96 ictpllmrgLGFWGRLPGAGLFSANTRrikAEAQASARKvaQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLF 175
Cdd:PLN03130 1333 ---------LDPFNEHNDADLWESLER---AHLKDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 176 DEPLSNL----DANLRQALRGEIRqlhdqlGVTFIYVTHDQHEAMSmSDRVAVMREGRILQLGTPEEI 239
Cdd:PLN03130 1399 DEATAAVdvrtDALIQKTIREEFK------SCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-230 |
1.39e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQfgNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLGERDL---LALSPSQRDCAMVFQ 82
Cdd:PRK10982 253 VRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALVTE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 83 ---SYALYPHMTVGGNICTPLLMRGLGFWGRLpgaglfsaNTRRIKAEAQASarkvaqslgIDGLWERKPAQ------LS 153
Cdd:PRK10982 331 errSTGIYAYLDIGFNSLISNIRNYKNKVGLL--------DNSRMKSDTQWV---------IDSMRVKTPGHrtqigsLS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 154 GGQRQRVALARAMVRRPAVFLFDEPLSNLDAnlrqALRGEIRQLHDQL---GVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDV----GAKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-237 |
8.48e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 29 GEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIrlgerdllalspsqrdcamvfqsyalyphmtvggnictpllmrglgfw 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------------ 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 109 grlpgaglFSANTRRIKAEAQASARKVAQslgidglwERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQ 188
Cdd:smart00382 34 --------IYIDGEDILEEVLDQLLLIIV--------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2536923639 189 ALRGEIR-----QLHDQLGVTFIYVTHDQHEAMSMsdrVAVMREGRILQLGTPE 237
Cdd:smart00382 98 LLLLLEElrlllLLKSEKNLTVILTTNDEKDLGPA---LLRRRFDRRIVLLLIL 148
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-210 |
1.81e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.75 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 15 NTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLdQPDSGSIRlgerdllalsPSQRDCAMVF--QSyalyPHMTV 92
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRL----------TKPAKGKLFYvpQR----PYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 93 GG---NICTP-----LLMRGLGfwgrlpgaglfsantrrikaeaQASARKVAQSLGIDGLWERKPA---------QLSGG 155
Cdd:TIGR00954 529 GTlrdQIIYPdssedMKRRGLS----------------------DKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2536923639 156 QRQRVALARAMVRRPAVFLFDEPLSNLDANLRQAlrgeIRQLHDQLGVTFIYVTH 210
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY----MYRLCREFGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
2.45e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 4 IHISGLTKQFGNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL--GERdLLALSPSQrdcamvf 81
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpNER-LGKLRQDQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 qsYAlYPHMTVggnICTpLLMRGLGFWG---------RLPGA----GLFSANTRRIKAE-----AQASARKVAQSLGID- 142
Cdd:PRK15064 74 --FA-FEEFTV---LDT-VIMGHTELWEvkqerdriyALPEMseedGMKVADLEVKFAEmdgytAEARAGELLLGVGIPe 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 143 ----GLWerkpAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANlrqalrgEIRQLHDQL---GVTFIYVTHDQH 213
Cdd:PRK15064 147 eqhyGLM----SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN-------TIRWLEDVLnerNSTMIIISHDRH 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
151-226 |
4.56e-06 |
|
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: 46.20 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 151 QLSGGQRQRVALA-----RAMVRRPaVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDqHEAMSMSDRVAVM 225
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHL-PELAELADKLIHI 153
|
.
gi 2536923639 226 R 226
Cdd:cd03227 154 K 154
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-238 |
5.50e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 146 ERKPAQLSGGQRQRVALARAMVRRPA--VFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQhEAMSMSDRV- 222
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLADRIi 548
|
90 100
....*....|....*....|.
gi 2536923639 223 -----AVMREGRILQLGTPEE 238
Cdd:PRK00635 549 digpgAGIFGGEVLFNGSPRE 569
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
152-239 |
8.90e-06 |
|
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: 48.02 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIR-QLHDqlgVTFIYVTHDQHEAMSMSdRVAVMREGRI 230
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFED---CTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
....*....
gi 2536923639 231 LQLGTPEEI 239
Cdd:TIGR00957 1498 AEFGAPSNL 1506
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
130-242 |
9.52e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.44 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 130 ASARKVAQSL--GIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEI-RQLHDQLGVTfi 206
Cdd:cd03288 133 AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVT-- 210
|
90 100 110
....*....|....*....|....*....|....*.
gi 2536923639 207 yVTHDQHEAMSmSDRVAVMREGRILQLGTPEEIYTR 242
Cdd:cd03288 211 -IAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-184 |
1.34e-05 |
|
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: 45.31 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 26 VRDGEFLTLLGSSGCGKSTLLKLIAGldQPDSGSIRlGERDL--LALSPS-QRDCAMVFQSYALYPHMTVGGNIctpllm 102
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEILIngRPLDKNfQRSTGYVEQQDVHSPNLTVREAL------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 103 rglgfwgrlpgagLFSANTRRIKAEaqasarkvaqslgidglwerkpaqlsggQRQRVALARAMVRRPAVFLFDEPLSNL 182
Cdd:cd03232 101 -------------RFSALLRGLSVE----------------------------QRKRLTIGVELAAKPSILFLDEPTSGL 139
|
..
gi 2536923639 183 DA 184
Cdd:cd03232 140 DS 141
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-196 |
2.07e-05 |
|
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: 46.83 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 6 ISGLTKQF--GNTKVIKGLDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDsGSIRLG--ERDLLALSPSQRDCAMVF 81
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDgvSWNSVTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 82 QSYALYphmtvggnictpllmrglgfwgrlpgAGLFSANTRRIKAEAQASARKVAQSLGIDGLWERKPAQL--------- 152
Cdd:TIGR01271 1299 QKVFIF--------------------------SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggy 1352
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2536923639 153 --SGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQ 196
Cdd:TIGR01271 1353 vlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-246 |
2.63e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 146 ERKPAQLSGGQRQRVALARAMVRR--PAVFLFDEPLSNLDANLRQALRGEIRQLHDqLGVTFIYVTHDQhEAMSMSDRV- 222
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDE-DTIRAADYVi 560
|
90 100
....*....|....*....|....*....
gi 2536923639 223 -----AVMREGRILQLGTPEEIYTRPANL 246
Cdd:TIGR00630 561 digpgAGEHGGEVVASGTPEEILANPDSL 589
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-211 |
4.45e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 4.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 141 IDGLWERKPAQLSGGQRQ------RVALARAMVRRPAVFLFDEPLSNLDA-NLRQALRGEIRQLHDQLGVTFIYVTHD 211
Cdd:cd03240 105 SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
134-232 |
5.46e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 134 KVAQSLGIDGLWERKPAQL-----------SGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDqlG 202
Cdd:cd03289 110 KVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--D 187
|
90 100 110
....*....|....*....|....*....|
gi 2536923639 203 VTFIYVTHdQHEAMSMSDRVAVMREGRILQ 232
Cdd:cd03289 188 CTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
126-183 |
5.69e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 5.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2536923639 126 AEAQASARKVAQSLGIDgLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLSNLD 183
Cdd:PLN03073 320 AEARAASILAGLSFTPE-MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-183 |
7.19e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 25 TVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRLgerdllalsPSQRDCAMVFQSYALYPHMTVGGNICTPLLMRG 104
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQLAWVNQETPALPQPALEYVIDGDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 105 LgfwgrlpGAGLFSANTR-----------RIKAEAQASARKVAQSLgIDGL------WERKPAQLSGGQRQRVALARAMV 167
Cdd:PRK10636 94 L-------EAQLHDANERndghaiatihgKLDAIDAWTIRSRAASL-LHGLgfsneqLERPVSDFSGGWRMRLNLAQALI 165
|
170
....*....|....*.
gi 2536923639 168 RRPAVFLFDEPLSNLD 183
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-230 |
7.94e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 7.94e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 152 LSGGQRQRVALARAMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRI 230
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-241 |
1.97e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSIRL-GERDLLALSPsqrdcamvfqsyALYPHMTVGGNICTPL 100
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISS------------GLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 101 LMRGLgfwgrlpgaglfsantrrIKAEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLS 180
Cdd:PRK13545 111 LMMGL------------------TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2536923639 181 NLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEIYT 241
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
306-362 |
2.38e-04 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 39.14 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2536923639 306 VEGTLVNVEYTGAELIASLQVDGIEDACVFCFPANSPAIRVGQALRVSVPIGEIHLF 362
Cdd:pfam08402 17 LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
151-209 |
2.45e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 42.25 E-value: 2.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2536923639 151 QLSGGQRQRVALAR--AMVR-RPAVF-LFDEPLSNLDANLRQALRGEIRQLHDqlGVTFIYVT 209
Cdd:cd03272 158 QLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDAQYRTAVANMIKELSD--GAQFITTT 218
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-222 |
1.57e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 138 SLGIDGL-WERKPAQLSGGQRQRVALARAMVRR--PAVFLFDEPLSNLDANLRQALRGEIRQLHDqLGVTFIYVTHDQhE 214
Cdd:cd03270 123 DVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDE-D 200
|
....*...
gi 2536923639 215 AMSMSDRV 222
Cdd:cd03270 201 TIRAADHV 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-239 |
1.73e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 138 SLGIDGLWERKP-AQLSGGQRQRVALAR---AMVRRPAVFLFDEPLSNLDANLRQALRGEIRQLHDQlGVTFIYVTHDQH 213
Cdd:PRK00635 795 SLGLDYLPLGRPlSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMH 873
|
90 100 110
....*....|....*....|....*....|..
gi 2536923639 214 eAMSMSDRVAVM------REGRILQLGTPEEI 239
Cdd:PRK00635 874 -VVKVADYVLELgpeggnLGGYLLASCSPEEL 904
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-239 |
2.37e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 22 LDLTVRDGEFLTLLGSSGCGKSTLLKLIAGLDQPDSGSI-RLGERDLLALSPsqrdcamvfqsyALYPHMTVGGNICTPL 100
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISA------------GLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 101 LMrgLGFwgrlpgaglfsanTRRikaEAQASARKVAQSLGIDGLWERKPAQLSGGQRQRVALARAMVRRPAVFLFDEPLS 180
Cdd:PRK13546 111 LC--MGF-------------KRK---EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2536923639 181 NLDANLRQALRGEIRQLHDQlGVTFIYVTHDQHEAMSMSDRVAVMREGRILQLGTPEEI 239
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-239 |
4.23e-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: 39.23 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 152 LSGGQRQRVALARAMVRR---PAVFLFDEPLSNLD-ANLRQALRgEIRQLHDQlGVTFIYVTHDQHeAMSMSDRVAVM-- 225
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfDDIKKLLE-VLQRLVDK-GNTVVVIEHNLD-VIKTADYIIDLgp 906
|
90
....*....|....*...
gi 2536923639 226 ----REGRILQLGTPEEI 239
Cdd:TIGR00630 907 eggdGGGTVVASGTPEEV 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-227 |
6.61e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.88 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 151 QLSGGQRQRVALAR--AMVR-RPAVF-LFDE---PLSnlDANLRQALRgEIRQLHDQlgVTFIYVTHDQHeAMSMSDRV- 222
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvKPAPFcILDEvdaPLD--DANVERFAN-LLKEFSKN--TQFIVITHNKG-TMEVADQLy 1162
|
....*.
gi 2536923639 223 -AVMRE 227
Cdd:TIGR02168 1163 gVTMQE 1168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-215 |
8.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2536923639 142 DGLWeRKPAQLSGGQR-Q-----RVALARAMVRRPAVFLFDEPLSNLDAN-LRQALR-----GEIRQlhdqlgvtFIYVT 209
Cdd:COG4717 550 DGRT-RPVEELSRGTReQlylalRLALAELLAGEPLPLILDDAFVNFDDErLRAALEllaelAKGRQ--------VIYFT 620
|
....*.
gi 2536923639 210 HDQHEA 215
Cdd:COG4717 621 CHEELV 626
|
|
| |
