|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-374 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 586.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIA 80
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSPS 240
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 241 MNINTHPVINGQAKIGDDTIDLPreavAKLTAEDNGQIIVGFRPEDADLATADDsNAFSLKVVNVEDLGSDGYIYGNIit 320
Cdd:COG3839 239 MNLLPGTVEGGGVRLGGVRLPLP----AALAAAAGGEVTLGIRPEHLRLADEGD-GGLEATVEVVEPLGSETLVHVRL-- 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 321 DGSAAeastmmsdqnkltTVRVNPRALPKIGDTVKIKIDPTKMHLFAPSTELRL 374
Cdd:COG3839 312 GGQEL-------------VARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-375 |
7.93e-178 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 498.21 E-value: 7.93e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIA 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSPS 240
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 241 MNINTHPV-INGQAKIGDDTIDLPREAVAKLTAedNGQIIVGFRPEDADLATADDsnAFSLKVVNVEDLGSDGYIYGNIi 319
Cdd:PRK11650 240 MNLLDGRVsADGAAFELAGGIALPLGGGYRQYA--GRKLTLGIRPEHIALSSAEG--GVPLTVDTVELLGADNLAHGRW- 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 320 tdgsaaeastmmSDQNklTTVRVNPRALPKIGDTVKIKIDPTKMHLFAPSTELRLN 375
Cdd:PRK11650 315 ------------GGQP--LVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRIE 356
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-367 |
3.18e-154 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 437.99 E-value: 3.18e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIA 80
Cdd:COG3842 3 MPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGspS 240
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--E 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 241 MNInthpvINGQ-AKIGDDTIDLPR---EAVAKLTAEDNGQIIVGFRPEDADLATADDSNAFSLKVVNVEDLGSDgYIYg 316
Cdd:COG3842 239 ANL-----LPGTvLGDEGGGVRTGGrtlEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSH-VRY- 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 317 niitdgsaaeasTMMSDQNKLTTVRVNPRAL--PKIGDTVKIKIDPTKMHLFA 367
Cdd:COG3842 312 ------------RVRLGDGQELVVRVPNRAAlpLEPGDRVGLSWDPEDVVVLP 352
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-366 |
2.92e-137 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 395.55 E-value: 2.92e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIA 80
Cdd:PRK11000 1 MASVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSPS 240
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 241 MNIntHPVINGQAKIGDDTIDLPREAVAKLTAEDNG-----QIIVGFRPEdaDLATADDSNA-FSLKVVNVEDLGSDGYI 314
Cdd:PRK11000 239 MNF--LPVKVTATAIEQVQVELPNRQQVWLPVEGRGvqvgaNMSLGIRPE--HLLPSDIADVtLEGEVQVVEQLGNETQI 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 315 YGNIITdgsaaeastmmSDQNklTTVRVNPRALPKIGDTVKIKIDPTKMHLF 366
Cdd:PRK11000 315 HIQIPA-----------IRQN--LVYRQNDVVLVEEGATFAIGLPPERCHLF 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-218 |
2.65e-134 |
|
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: 381.99 E-value: 2.65e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPgnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVF 83
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-237 |
6.95e-115 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 333.43 E-value: 6.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVF 83
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIG 237
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
2.16e-114 |
|
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: 331.79 E-value: 2.16e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVF 83
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-365 |
2.89e-114 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 336.35 E-value: 2.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTT-MQPKDRDIAMVFQNYALYPHMTVADNMG 99
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERRVGFVFQHYALFPHMTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 100 FALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:COG1118 98 FGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 180 ALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGspSMNINTHPVINGQAKIGDDT 259
Cdd:COG1118 178 RLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNVLRGRVIGGQLEADGLT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 260 IDLPREAvakltaeDNGQIIVGFRPEDADLAT-ADDSNAFSLKVVNVEDLGSDGYIYGNIItdgsaaeastmmSDQNKLT 338
Cdd:COG1118 256 LPVAEPL-------PDGPAVAGVRPHDIEVSRePEGENTFPATVARVSELGPEVRVELKLE------------DGEGQPL 316
|
330 340 350
....*....|....*....|....*....|.
gi 2525772010 339 TVRVNPRA----LPKIGDTVKIKIDPTKMHL 365
Cdd:COG1118 317 EAEVTKEAwaelGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-366 |
6.21e-114 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 335.81 E-value: 6.21e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYPGNDKP--SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTT-----MQP 74
Cdd:NF040933 1 VTVRVENVTKIFKKGKKEvvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 75 KDRDIAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREP 154
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 155 KVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAG 234
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 235 FIGspSMNINTHPVINGQAKIGDD-TIDLPREAVakltaeDNGQIIVGFRPEDADLATADDSNAFSLKVVNVEDLGSDGY 313
Cdd:NF040933 241 LIG--DINLLEGKVEEEGLVDGNDlKIPLPNPKL------EAGEVIIGIRPEDIDISESDMRLPPGFVEVGKGRVKVSSY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 314 IYGNIITdgsaaeasTMMSDQNKLTTVRVNPRALPKIGDTVKIKIDPTKMHLF 366
Cdd:NF040933 313 AGGVFRV--------VVSPIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-286 |
1.55e-110 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 328.06 E-value: 1.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYAL 88
Cdd:PRK09452 20 ISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 YPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:PRK09452 98 FPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 169 KLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGspsmNINthpV 248
Cdd:PRK09452 178 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG----EIN---I 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2525772010 249 INGQ--AKIGDDTID-----LPREAVAKLTAEDNGQIIVGFRPED 286
Cdd:PRK09452 251 FDATviERLDEQRVRanvegRECNIYVNFAVEPGQKLHVLLRPED 295
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
21-367 |
4.72e-106 |
|
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: 315.82 E-value: 4.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGF 100
Cdd:TIGR03265 20 LKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALFPNLTVADNIAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 101 ALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAA 180
Cdd:TIGR03265 100 GLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 181 LQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGspSMN-INTHPVINGQAKIGDDT 259
Cdd:TIGR03265 180 LQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVNwLPGTRGGGSRARVGGLT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 260 IDLPREAvakLTAEDNGQIIVgfRPEDADLATADDS-NAFSLKVVNVEDLGSDGYIYGNIIT-DGSAAEASTMMSDQNKL 337
Cdd:TIGR03265 258 LACAPGL---AQPGASVRLAV--RPEDIRVSPAGNAaNLLLARVEDMEFLGAFYRLRLRLEGlPGQALVADVSASEVERL 332
|
330 340 350
....*....|....*....|....*....|
gi 2525772010 338 TTvrvnpralpKIGDTVKIKIDPTKMHLFA 367
Cdd:TIGR03265 333 GI---------RAGQPIWIELPAERLRAFA 353
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-368 |
1.00e-101 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 304.72 E-value: 1.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNdkPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVF 83
Cdd:PRK11432 7 VVLKNITKRFGSN--TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSPsmNI 243
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 244 NTHPVINGQAKIGDDTIDLPREAVAKLTaedNGQIIVGFRPEDADL-ATADDSNAFSLKVVnvedlgsdGYIygniitdG 322
Cdd:PRK11432 243 FPATLSGDYVDIYGYRLPRPAAFAFNLP---DGECTVGVRPEAITLsEQGEESQRCTIKHV--------AYM-------G 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2525772010 323 SAAEASTMMSDQNKLttVRVNPRAL-PKIGDTVKIKIDPTKMHLFAP 368
Cdd:PRK11432 305 PQYEVTVDWHGQELL--LQVNATQLqPDLGEHYYLEIHPYGMFLLAD 349
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-360 |
4.50e-99 |
|
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: 297.10 E-value: 4.50e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 36 LVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKR 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 116 VEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHD 195
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 196 QTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSPSMNINTHPVINGQAKIGDDTIDLPREAVAKLTAEDN 275
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 276 GQIIVGFRPEDADLATADDSNAFSLKVVNVEDlgsdgyiygnIITDGSAAEASTMMSD-QNKLTTVRVNPRAL---PKIG 351
Cdd:TIGR01187 241 QPLHVVLRPEKIVIEEEDEANSSNAIIGHVID----------ITYLGMTLEVHVRLETgQKVLVSEFFNEDDPhmsPSIG 310
|
....*....
gi 2525772010 352 DTVKIKIDP 360
Cdd:TIGR01187 311 DRVGLTWHP 319
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-238 |
2.67e-95 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 284.23 E-value: 2.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPgnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMV 82
Cdd:cd03296 2 SIEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHMTVADNMGFALKI----AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGS 238
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
23-310 |
2.59e-91 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 277.73 E-value: 2.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 KIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQ 182
Cdd:NF040840 98 KLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 183 RQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSPsmNInthpvINGQAKIGDD---- 258
Cdd:NF040840 178 REFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NI-----IEGVAEKGGEgtil 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 259 -----TIDLPREAVakltaednGQIIVGFRPEDADLAT----ADDSNAFSLKVVNVEDLGS 310
Cdd:NF040840 251 dtgniKIELPEEKK--------GKVRIGIRPEDITISTekvkTSARNEFKGKVEEIEDLGP 303
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-238 |
8.01e-90 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 272.35 E-value: 8.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVF 83
Cdd:COG1125 4 FENVTKRYPD-GTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEkaaEILDL-----TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVD---ELLELvgldpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGS 238
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
2.50e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 269.65 E-value: 2.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYP--GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmqPKDRD 78
Cdd:COG1116 5 APALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAV 208
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-237 |
1.57e-87 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 264.35 E-value: 1.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMG 99
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALFKHLTVRDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 100 FALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:TIGR00968 95 FGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 180 ALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIG 237
Cdd:TIGR00968 175 KLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-239 |
1.65e-85 |
|
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: 259.16 E-value: 1.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAM 81
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDL--TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 160 DEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSP 239
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-209 |
2.75e-85 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 257.79 E-value: 2.75e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGND--KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmqPKDRDIAMVF 83
Cdd:cd03293 3 VRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVI 209
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-237 |
1.60e-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: 251.49 E-value: 1.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMG 99
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 100 FALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 180 ALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIG 237
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-360 |
6.60e-81 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 252.06 E-value: 6.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 8 HVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYA 87
Cdd:PRK11607 24 NLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 88 LYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 168 AKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGSpsmnINthp 247
Cdd:PRK11607 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS----VN--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 248 VINGQAK--------IGDDTIDLPREAVAKLTAEDNGQIIVGFRPEDADLAT---ADDSNAFSLKVVNVEDLGsDGYIYG 316
Cdd:PRK11607 255 VFEGVLKerqedglvIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEeppADGCNFAVGEVIHIAYLG-DLSIYH 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2525772010 317 NIITDGSaaeastMMSDQnkLTTVRVNPRALPKIGDTVKIKIDP 360
Cdd:PRK11607 334 VRLKSGQ------MISAQ--LQNAHRYRKGLPTWGDEVRLCWEA 369
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-236 |
9.50e-75 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 232.53 E-value: 9.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD------RDIAMVFQNYALYPHMTV 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 175 RTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFI 236
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-333 |
3.04e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 232.69 E-value: 3.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD------RDIAMVFQNYALYPHMTV 94
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:COG4175 123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 175 RTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGspsmNINTHPVINGQ-- 252
Cdd:COG4175 203 QDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVE----DVDRSKVLTAGsv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 253 AKIGDDTI---DLPREAVAKLtaedngqiivgfRPEDADLATADDSNAFSLKVVNVEDLGS----DGYIYGNIITDGSAA 325
Cdd:COG4175 279 MRPPEAVVsekDGPRVALRRM------------REEGISSLYVVDRDRRLLGVVTADDALEavkgEKDLEEILLTDVPTV 346
|
....*...
gi 2525772010 326 EASTMMSD 333
Cdd:COG4175 347 SPDTPLRD 354
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-305 |
3.60e-73 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 231.51 E-value: 3.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 KIagTPKDE------IRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRT 176
Cdd:PRK10851 100 TV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 177 QIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGspSMNINTHPVINGQAKIG 256
Cdd:PRK10851 178 WLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--EVNRLQGTIRGGQFHVG 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 257 DDTIDLPreavakLTAEDNGQIIVGFRPEDADLATadDSNAFS---LKVVNV 305
Cdd:PRK10851 256 AHRWPLG------YTPAYQGPVDLFLRPWEVDISR--RTSLDSplpVQVLEV 299
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-212 |
1.10e-69 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 216.28 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM----QPKDRDIAM 81
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHMTVADNMGFalkiagtpkdeirkrvekaaeildlteyldrkpkALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 162 PLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
1.08e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 215.68 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVV-FDHVTRIYP--GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR 77
Cdd:COG1136 1 MSPLLeLRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 78 D------IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIV 151
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 152 REPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQtEALTMGDRIAVIKLGIL 214
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.38e-67 |
|
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: 221.70 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPS---VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---- 76
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 -RDIAMVFQN--YALYPHMTVADNMGFALKIAGT-PKDEIRKRVEKAAEILDL-TEYLDRKPKALSGGQRQRVAMGRAIV 151
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 152 REPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
1.22e-66 |
|
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: 210.04 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPS--VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD--- 78
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 ---IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPK 155
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 156 VFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALtMGDRIAVIK 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELR 214
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-237 |
1.54e-66 |
|
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: 214.72 E-value: 1.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 18 KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQP------KDRDIAMVFQNYALYPH 91
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:TIGR01186 86 MTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 172 VQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIG 237
Cdd:TIGR01186 166 DSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-226 |
1.70e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 210.31 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD-IAMV 82
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 163 LSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-227 |
1.21e-65 |
|
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: 207.96 E-value: 1.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAM 81
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNyalyP-----HMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:COG1122 80 VFQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 157 FLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-222 |
2.46e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 206.83 E-value: 2.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD 78
Cdd:COG2884 2 IRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 159 MDEPLSNLDAKLRVQTrtqIAALQR--QLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:COG2884 161 ADEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-212 |
5.34e-65 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 205.39 E-value: 5.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 5 VFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMV 82
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNyalyP-HM----TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVF 157
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 158 LMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-218 |
9.23e-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: 202.53 E-value: 9.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIK---DGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGG-------KDVTtMQPKDRDIAMVFQNYALYPH 91
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN-LPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKiaGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525772010 172 VQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-229 |
1.22e-63 |
|
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: 203.50 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYP--GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMV 82
Cdd:COG1124 5 RNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNY--ALYPHMTVADNMGFALKIAGtpKDEIRKRVEKAAEILDLT-EYLDRKPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:COG1124 85 FQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 160 DEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:COG1124 163 DEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-237 |
4.90e-62 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 198.83 E-value: 4.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 25 NLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFALKI 104
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 105 AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQ 184
Cdd:COG3840 99 GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 185 LGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIG 237
Cdd:COG3840 179 RGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-223 |
1.27e-61 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 197.89 E-value: 1.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD----- 78
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGT-PKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVF 157
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 158 LMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-288 |
4.06e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 197.22 E-value: 4.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKP--SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD 78
Cdd:COG1135 4 LENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAklrvQTRTQIAAL----QRQLGVTTLYVTHDqtealtMG------DRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:COG1135 164 CDEATSALDP----ETTRSILDLlkdiNRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQ 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 229 NVFVAGFIGSPSmninthpvingqakigddTIDLPREAVAKLTAEDNGQIIV--GFRPEDAD 288
Cdd:COG1135 234 SELTRRFLPTVL------------------NDELPEELLARLREAAGGGRLVrlTFVGESAD 277
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-212 |
4.25e-60 |
|
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: 193.49 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPS--VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR-----D 78
Cdd:cd03257 4 VKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNY--ALYPHMTVADNMGFALKIAGTP-KDEIRKRV--EKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVRE 153
Cdd:cd03257 84 IQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLsKKEARKEAvlLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 154 PKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
1.82e-59 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 193.15 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYPGN--DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmqPkDRD 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--P-GAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAV 208
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-227 |
4.36e-59 |
|
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: 191.26 E-value: 4.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDK--PSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD 78
Cdd:cd03258 4 LKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 159 MDEPLSNLDAklrvQTRTQIAAL----QRQLGVTTLYVTHdQTEAL-TMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:cd03258 164 CDEATSALDP----ETTQSILALlrdiNRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
5.12e-59 |
|
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: 199.36 E-value: 5.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVV-FDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN---KGRILIGGKDVTTMQPKD 76
Cdd:COG1123 1 MTPLLeVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 R--DIAMVFQN--YALYPhMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVR 152
Cdd:COG1123 81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 153 EPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-228 |
7.68e-58 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 191.10 E-value: 7.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIAMVFQN-YA-LYPHMT 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKIAG-TPKDEIRKRVekaAEILDL----TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDa 168
Cdd:COG4608 114 VGDIIAEPLRIHGlASKAERRERV---AELLELvglrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 169 klrVQTRTQI----AALQRQLGVTTLYVTHDqteaLTM----GDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:COG4608 190 ---VSIQAQVlnllEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-228 |
8.53e-58 |
|
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: 191.85 E-value: 8.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV------TTMQPKDRDIAMVFQNYALYPHMTVAD 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 97 NMGFALKiaGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDaklrVQTRT 176
Cdd:COG4148 97 NLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD----LARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 177 QI----AALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:COG4148 171 EIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-212 |
6.95e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.03 E-value: 6.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIA 80
Cdd:COG3638 5 LRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADN--------MGFALKIAGT-PKDEIrkrvEKAAEILD---LTEYLDRKPKALSGGQRQRVAMGR 148
Cdd:COG3638 84 MIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLfPPEDR----ERALEALErvgLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-223 |
7.50e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 182.70 E-value: 7.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIAMVFQNYALYPH 91
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKIAGT-PKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKL 170
Cdd:cd03261 92 LTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 171 RVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:cd03261 172 SGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-209 |
1.22e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.55 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYP 90
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 hMTVADNMGFALKIAGTPKDeiRKRVEKAAEILDLTE-YLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:COG4619 88 -GTVRDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2525772010 170 LRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVI 209
Cdd:COG4619 165 NTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-239 |
1.55e-55 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 182.55 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMT 93
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADN--MGFA--LKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:COG1120 92 VRELvaLGRYphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 170 LRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTE---------LYDRPANVFVAGFIGSP 239
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelleeVYGVEARVIEDPVTGRP 250
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-195 |
2.14e-55 |
|
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: 180.91 E-value: 2.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEvvFDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---- 76
Cdd:TIGR02673 1 MIE--FHNVSKAYPGG-VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 -RDIAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPK 155
Cdd:TIGR02673 78 rRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2525772010 156 VFLMDEPLSNLDAklrvQTRTQIAALQRQL---GVTTLYVTHD 195
Cdd:TIGR02673 158 LLLADEPTGNLDP----DLSERILDLLKRLnkrGTTVIVATHD 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-226 |
1.06e-54 |
|
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: 180.05 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR-DIAMVFQNYALYPHMTV 94
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 175 RTQIAALqRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:COG4555 172 REILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-216 |
1.86e-54 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 178.44 E-value: 1.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAG-LEEV--NKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHM 92
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGFALKiAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRV 172
Cdd:COG4136 92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 173 QTRTQIAALQRQLGVTTLYVTHDQTEALTMGdriAVIKLGILQQ 216
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDAPAAG---RVLDLGNWQH 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-229 |
4.23e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 178.26 E-value: 4.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVtTMQPKD-----RDIAMVFQNYALYPHMTVAD 96
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDinklrRKVGMVFQQFNLFPHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 97 NMGFAL-KIAGTPKDEIRKRvekAAEILD---LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK--- 169
Cdd:COG1126 97 NVTLAPiKVKKMSKAEAEER---AMELLErvgLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvg 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 170 --LRVqtrtqIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:COG1126 174 evLDV-----MRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-224 |
1.39e-53 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 178.01 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDvtTMQPKD-----RDIA 80
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENlweirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNyalyPH-----MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPK 155
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 156 VFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALtMGDRIAVIKLGILQQVGAPTELY 224
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
8.45e-53 |
|
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: 174.62 E-value: 8.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmQPKD--RDIAM 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAarQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 162 PLSNLDaklrVQTRTQI-AALQRQLGVTT-LYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:cd03263 160 PTSGLD----PASRRAIwDLILEVRKGRSiILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
7-209 |
2.25e-52 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 174.54 E-value: 2.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGNDKPS--VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPkdrDIAMVFQ 84
Cdd:NF040729 5 QNISKTFINNKKENevLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP---DRGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 85 NYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLS 164
Cdd:NF040729 82 NYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2525772010 165 NLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVI 209
Cdd:NF040729 162 AVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVM 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-228 |
4.00e-52 |
|
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: 176.01 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN---KGRILIGGKDVTTMQPKD------RDIAMVFQN-Y-ALY 89
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKElrkirgREIQMIFQDpMtSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNMGFALKI-AGTPKDEIRKRVEKAAEILDLT---EYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:COG0444 101 PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 166 LDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:COG0444 181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-223 |
3.38e-51 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 170.44 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 11 RIYPGNDKpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNK-----GRILIGGKDVTTMQPKD----RDIAM 81
Cdd:cd03260 7 NVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVlelrRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPhMTVADNMGFALKIAGT-PKDEIRKRVEKAAEILDLTEYLDRKPKA--LSGGQRQRVAMGRAIVREPKVFL 158
Cdd:cd03260 86 VFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 159 MDEPLSNLD--AKLRVQTRtqIAALQRQlgVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:cd03260 165 LDEPTSALDpiSTAKIEEL--IAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-212 |
3.41e-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: 169.98 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 KIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQ 182
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|
gi 2525772010 183 RQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-238 |
1.21e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 172.68 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKP--SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD 78
Cdd:PRK11153 4 LKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAklrvQTRTQIAAL----QRQLGVTTLYVTHDqtealtMG------DRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:PRK11153 164 CDEATSALDP----ATTRSILELlkdiNRELGLTIVLITHE------MDvvkricDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|
gi 2525772010 229 NVFVAGFIGS 238
Cdd:PRK11153 234 HPLTREFIQS 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-214 |
5.68e-50 |
|
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: 166.81 E-value: 5.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD 78
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 159 MDEPLSNLDAklrvQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGIL 214
Cdd:cd03292 160 ADEPTGNLDP----DTTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-206 |
9.93e-50 |
|
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: 166.17 E-value: 9.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK----DRDIAMVFQNYALYPHM 92
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGFAL-KIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:cd03262 92 TVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2525772010 172 ---VQTRTQIAalqrQLGVTTLYVTHDQTEALTMGDRI 206
Cdd:cd03262 172 gevLDVMKDLA----EEGMTMVVVTHEMGFAREVADRV 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-218 |
1.70e-49 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 165.80 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 25 NLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFALKI 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 105 AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQ 184
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 2525772010 185 LGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-225 |
4.18e-49 |
|
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: 165.43 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIA 80
Cdd:cd03256 3 VENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADN--------MGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVR 152
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 153 EPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYD 225
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-229 |
3.64e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 163.34 E-value: 3.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDI---- 79
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALYPHMTVADNMGFA-LKIAGTPKDEIRKRvekAAEILD---LTEYLDRKPKALSGGQRQRVAMGRAIVREPK 155
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQ---ARELLAkvgLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 156 VFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-227 |
4.08e-48 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 162.64 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPkdrDIAMVFQNYALYPHMTVADNMGF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 101 ALK--IAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQI 178
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 179 AALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL-YDRP 227
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-212 |
8.48e-48 |
|
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: 159.86 E-value: 8.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAM 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYpHMTVADNMgfalkiagtpkdeirkrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 162 PLSNLDAklrvQTRTQI-AALQRQL-GVTTLYVTHDqTEALTMGDRIAVIKLG 212
Cdd:cd03228 123 ATSALDP----ETEALIlEALRALAkGKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-235 |
1.11e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 166.75 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM------QPKDRDIAMVFQNYALYPHMTV 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 175 RTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGF 235
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-227 |
2.39e-47 |
|
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: 162.24 E-value: 2.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIY-PG--NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---- 76
Cdd:TIGR04521 1 IKLKNVSYIYqPGtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 -RDIAMVFQnyalYPHM-----TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTE-YLDRKPKALSGGQRQRVAMGRA 149
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 150 IVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-226 |
2.78e-47 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 170.79 E-value: 2.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYpHMTVADNMGFAlkiAGTPKDEirkRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRA 149
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG---DPDATDE---EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 150 IVREPKVFLMDEPLSNLDAklrvQTRTQI-AALQRQL-GVTTLYVTHDqTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:COG2274 626 LLRNPRILILDEATSALDA----ETEAIIlENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-223 |
3.51e-47 |
|
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: 159.84 E-value: 3.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDkpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmQPKD--RDIAM 81
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREvrRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 162 PLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-218 |
3.60e-47 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 161.00 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQpkdRDIAMVFQNYALYPHMTVADNMGFA 101
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLMFQDARLLPWKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 102 LKiagtpkDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAAL 181
Cdd:PRK11247 106 LK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 2525772010 182 QRQLGVTTLYVTHDQTEALTMGDRIAVIKLGilqQVG 218
Cdd:PRK11247 180 WQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-225 |
3.78e-47 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 160.54 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD 78
Cdd:TIGR02315 2 LEVENLSKVYP-NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADN--------MGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAI 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENvlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 151 VREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYD 225
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-223 |
1.73e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 166.88 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:COG1132 339 EIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYpHMTVADNMGFALKIAGtpkdeiRKRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRA 149
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGRPDAT------DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 150 IVREPKVFLMDEPLSNLDAK--LRVQtrtqiAALQRQL-GVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:COG1132 491 LLKDPPILILDEATSALDTEteALIQ-----EALERLMkGRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-195 |
2.20e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 158.64 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV---TTMQPKD-----RDIAMVFQNYALYPHMTV 94
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAirelrRNVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFA-LKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQ 173
Cdd:PRK11124 100 QQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180
....*....|....*....|..
gi 2525772010 174 TRTQIAALQrQLGVTTLYVTHD 195
Cdd:PRK11124 180 IVSIIRELA-ETGITQVIVTHE 200
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
8.73e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 164.93 E-value: 8.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDI 79
Cdd:COG4988 335 PSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALyPHMTVADNMGFAlkiAGTPKDEirkRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGR 148
Cdd:COG4988 414 AWVPQNPYL-FAGTIRENLRLG---RPDASDE---ELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAklrvQTRTQIAALQRQL--GVTTLYVTHDqTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDA----ETEAEILQALRRLakGRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-195 |
1.23e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGK--------DVTTMQPKDRDIAMVFQNYALYPHMTV 94
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLRQKVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFA-LKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQ 173
Cdd:COG4161 100 MENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180
....*....|....*....|..
gi 2525772010 174 TRTQIAALQrQLGVTTLYVTHD 195
Cdd:COG4161 180 VVEIIRELS-QTGITQVIVTHE 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
2.00e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 152.80 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMTVADNM 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 99 GFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRK----PKALSGGQRQRVAMGRAIVREPKVFLMDEPLS 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-202 |
7.76e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 154.86 E-value: 7.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmqpKDRDIAMVFQNY 86
Cdd:PRK11248 5 SHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---PGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 87 ALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2525772010 167 DAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTM 202
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFM 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.02e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmqpKDRDIA 80
Cdd:COG1121 4 MPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPH--MTVAD--NMGF--ALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREP 154
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDvvLMGRygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 155 KVFLMDEPLSNLDAKlrvqTRTQIAAL---QRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQvGAPTE 222
Cdd:COG1121 159 DLLLLDEPFAGVDAA----TEEALYELlreLRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-205 |
1.26e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 152.63 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK-DRDIAMVFQNYALYPHMTV 94
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRkrVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAklrvQT 174
Cdd:COG4133 93 RENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA----AG 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 2525772010 175 RTQIAAL---QRQLGVTTLYVTHDQTEA-----LTMGDR 205
Cdd:COG4133 167 VALLAELiaaHLARGGAVLLTTHQPLELaaarvLDLGDF 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-214 |
1.57e-44 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 151.40 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPgnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR-DIAMVFQN 85
Cdd:cd03230 4 RNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPHMTVAdnmgfalkiagtpkdeirkrvekaaeildltEYLDrkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:cd03230 82 PSLYENLTVR-------------------------------ENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 166 LDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGIL 214
Cdd:cd03230 126 LDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-212 |
1.91e-44 |
|
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: 151.43 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRdiamvfqnyalyphmtvA 95
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-----------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 96 DNMGFalkiagtpkdeirkrVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTR 175
Cdd:cd03214 73 RKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 2525772010 176 TQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-224 |
2.69e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 154.40 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIAMVFQ 84
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeeTVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 85 NyalyPH-----MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:PRK13635 89 N----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 160 DEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTmGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-199 |
3.11e-44 |
|
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: 152.59 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGNDKPSV--DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMqpkDRD------ 78
Cdd:COG4181 12 RGLTKTVGTGAGELTilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL---DEDararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 ---IAMVFQNYALYPHMTVADNMGFALKIAGTPKDEirkrvEKAAEILD---LTEYLDRKPKALSGGQRQRVAMGRAIVR 152
Cdd:COG4181 89 arhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 153 EPKVFLMDEPLSNLDAKlrvqTRTQIA----ALQRQLGVTTLYVTHDQTEA 199
Cdd:COG4181 164 EPAILFADEPTGNLDAA----TGEQIIdllfELNRERGTTLVLVTHDPALA 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-228 |
4.26e-44 |
|
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: 156.04 E-value: 4.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGkdvTTMQ---------PKDRDIAMVFQNYALYPHMT 93
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFdsrkgiflpPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKIAgTPKDEiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQ 173
Cdd:TIGR02142 92 VRGNLRYGMKRA-RPSER-RISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 174 TRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-218 |
1.13e-43 |
|
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: 150.60 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGNDKP--SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmQPKD--RDIAMV 82
Cdd:cd03266 5 DALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 163 LSNLDAkLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:cd03266 164 TTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
1.39e-43 |
|
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: 158.78 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDI 79
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALYpHMTVADNmgfaLKIA-GTPKDEirkRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMG 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRLArPDATDE---ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 148 RAIVREPKVFLMDEPLSNLDAklrvQTRTQI-AALQRQL-GVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTELYD 225
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDA----ATEQALlADLLEALaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLA 558
|
...
gi 2525772010 226 RPA 228
Cdd:COG4987 559 QNG 561
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
2.20e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 150.50 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 25 NLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYALYPHMTVADNMGFALKI 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 105 AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR---VQTRTQIAAl 181
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqemLTLVSQVCQ- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2525772010 182 QRQLgvTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK10771 178 ERQL--TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-212 |
6.56e-43 |
|
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: 149.12 E-value: 6.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYPHMTVADN 97
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 M----------GFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:cd03219 96 VmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2525772010 168 AKLRVQTRTQIAALqRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03219 176 PEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
1.04e-42 |
|
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: 146.24 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVF 83
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QnyalyphmtvadnmgfalkiagtpkdeirkrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-226 |
1.08e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 149.88 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIAMVFQNyalyPH--- 91
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 --MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:PRK13650 95 vgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 170 LRVQTRTQIAALQRQLGVTTLYVTHDQTEaLTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-211 |
1.47e-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: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 8 HVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RD-IAM 81
Cdd:TIGR03608 3 NISKKF--GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 162 PLSNLDAKlrvqTRTQIAALQRQL---GVTTLYVTHDqTEALTMGDRiaVIKL 211
Cdd:TIGR03608 161 PTGSLDPK----NRDEVLDLLLELndeGKTIIIVTHD-PEVAKQADR--VIEL 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-209 |
5.68e-42 |
|
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: 147.49 E-value: 5.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYPHMTVADN 97
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 M----------GFALKIAGTPK-----DEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:COG0411 100 VlvaaharlgrGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 163 LSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDqtealtMG------DRIAVI 209
Cdd:COG0411 180 AAGLNPEETEELAELIRRLRDERGITILLIEHD------MDlvmglaDRIVVL 226
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-238 |
3.29e-41 |
|
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: 145.36 E-value: 3.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD------- 76
Cdd:TIGR03005 1 VRFSDVTKRF--GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpad 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 --------RDIAMVFQNYALYPHMTVADNMGFA-LKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMG 147
Cdd:TIGR03005 79 ekhlrqmrNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 148 RAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:TIGR03005 159 RALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQP 238
|
250
....*....|.
gi 2525772010 228 ANVFVAGFIGS 238
Cdd:TIGR03005 239 KEERTREFLSK 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-224 |
5.23e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.96 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIY-PGN--DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDI----AM 81
Cdd:PRK13637 8 LTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQ--NYALYPHmTVADNMGFALKIAGTPKDEIRKRVEKAAEI--LDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVF 157
Cdd:PRK13637 88 VFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 158 LMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-223 |
8.84e-41 |
|
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: 143.34 E-value: 8.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYPHMTVADN 97
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 mgfaLKIAGT--PKDEIRKRVEKAAEIL-DLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03224 96 ----LLLGAYarRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 175 RTQIAALqRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:cd03224 172 FEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-227 |
1.42e-40 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 146.00 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR-----DIAMVFQN--YALYPHM 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGFALKI--AGTPKDEIRKRV-EKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 170 LRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-227 |
2.07e-39 |
|
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: 146.75 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEvNKGRILIGGKDVTTMQPKD-----RDIAMVFQN-YA-LYPHMT 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKI--AGTPKDEIRKRVEKAAEILDLT-EYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDakl 170
Cdd:COG4172 381 VGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--- 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 171 rVQTRTQI----AALQRQLGVTTLYVTHDQT--EALTmgDRIAVIKLG-ILQQvGAPTELYDRP 227
Cdd:COG4172 458 -VSVQAQIldllRDLQREHGLAYLFISHDLAvvRALA--HRVMVMKDGkVVEQ-GPTEQVFDAP 517
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
7-212 |
2.57e-39 |
|
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: 140.71 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGND-------KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--- 76
Cdd:TIGR02769 6 RDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrra 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 --RDIAMVFQNY--ALYPHMTVADNMGFALKIAgTPKDEIRkRVEKAAEILDL----TEYLDRKPKALSGGQRQRVAMGR 148
Cdd:TIGR02769 86 frRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHL-TSLDESE-QKARIAELLDMvglrSEDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-210 |
6.02e-39 |
|
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: 138.05 E-value: 6.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQpkdRDIAMVFQN 85
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YAL---YPhMTVAD--NMGFALKI--AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:cd03235 77 RSIdrdFP-ISVRDvvLMGLYGHKglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 159 MDEPLSNLDaklrVQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIK 210
Cdd:cd03235 156 LDEPFAGVD----PKTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-226 |
3.43e-38 |
|
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: 136.98 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAM 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYpHMTVADNMGFalkiaGTPkDEIRKRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGRAI 150
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY-----GRP-GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 151 VREPKVFLMDEPLSNLD--AKLRVQtrtqiAALQR-QLGVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:cd03251 154 LKDPPILILDEATSALDteSERLVQ-----AALERlMKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-212 |
9.49e-38 |
|
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: 135.41 E-value: 9.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYpHMTVADNMGFALKIAgtpKDEirkRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRA 149
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLA---DDE---RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 150 IVREPKVFLMDEPLSNLDAKLRVQTrtqIAALQRQLGVTTLYV-THdQTEALTMGDRIAVIKLG 212
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIiTH-RPSLLDLVDRIIVMDSG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-218 |
2.03e-37 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 134.24 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGndKPSVDDLNLDIKDGeFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD-IAMVFQN 85
Cdd:cd03264 4 ENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 166 LDAKLRVQTRTQIAALQRqlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:cd03264 161 LDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-206 |
2.29e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.60 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPG--NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR--DIAMVFQNYAL 88
Cdd:COG1101 12 NPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 --YPHMTVADNMGFA--------LKIAGTPKDeiRKRVEKAAEILD--LTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:COG1101 92 gtAPSMTIEENLALAyrrgkrrgLRRGLTKKR--RELFRELLATLGlgLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 157 FLMDEPLSNLDAKlrvqTRTQIAALQRQL----GVTTLYVTHDQTEALTMGDRI 206
Cdd:COG1101 170 LLLDEHTAALDPK----TAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-227 |
2.29e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 136.08 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL---EEVNKGRILIGGKDVT--TMQPKDRD 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTakTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNY-ALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVF 157
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 158 LMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEAlTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-209 |
3.28e-37 |
|
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: 142.31 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYpHMTVADNMGFAlkiAGTPKDEirkRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRA 149
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG---APYADDE---EILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 150 IVREPKVFLMDEPLSNLDAklrvQTRTQ-IAALQRQL-GVTTLYVTHdQTEALTMGDRIAVI 209
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDN----RSEERfKDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVM 672
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-214 |
2.89e-36 |
|
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: 130.80 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 8 HVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVFQNYA 87
Cdd:cd03268 5 DLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 88 LYPHMTVADNMGFALKIAGTPKdeirKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525772010 168 AKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGIL 214
Cdd:cd03268 159 PDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-228 |
3.39e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 137.89 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 14 PGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTT----LRMLAGLEEVNKGRILIGGKDVTTMQPKD------RDIAMVF 83
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QN--YALYPHMTVADNMGFALKI-AGTPKDEIRKRvekAAEILDLT------EYLDRKPKALSGGQRQRV--AMgrAIVR 152
Cdd:COG4172 99 QEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARAR---ALELLERVgipdpeRRLDAYPHQLSGGQRQRVmiAM--ALAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 153 EPKVFLMDEPLSNLDaklrVQTRTQI----AALQRQLGVTTLYVTHDqteaLT----MGDRIAVIKLGILQQVGAPTELY 224
Cdd:COG4172 174 EPDLLIADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELF 245
|
....
gi 2525772010 225 DRPA 228
Cdd:COG4172 246 AAPQ 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-195 |
3.61e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 132.50 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM---QPKD--RDIAMVFQNY--ALYPHMT 93
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAfrRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALK-IAGTPKDEIRKRVEKAAEILDLT-EYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180
....*....|....*....|....
gi 2525772010 172 VQTRTQIAALQRQLGVTTLYVTHD 195
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHD 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-224 |
6.12e-36 |
|
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: 131.12 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPgnDKPSV---DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RD 78
Cdd:cd03249 1 IEFKNVSFRYP--SRPDVpilKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPhMTVADNMGFALKIAgtpKDEIRKRVEKAAEILDLTEYLDRK------PKA--LSGGQRQRVAMGRAI 150
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYGKPDA---TDEEVEEAAKKANIHDFIMSLPDGydtlvgERGsqLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 151 VREPKVFLMDEPLSNLDAK--LRVQtrtqiAALQR-QLGVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:cd03249 155 LRNPKILLLDEATSALDAEseKLVQ-----EALDRaMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-212 |
6.92e-36 |
|
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: 130.09 E-value: 6.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMqpKDRDIAMVFQN 85
Cdd:cd03269 3 VENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--ARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525772010 166 LDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-195 |
7.67e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 130.38 E-value: 7.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIA 80
Cdd:PRK10908 4 FEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRqLGVTTLYVTHD 195
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHD 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-229 |
8.33e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.12 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 11 RIYPGNDKpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN-----KGRILIGGKDVTT--MQPKD--RDIAM 81
Cdd:PRK14267 11 RVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEvrREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHMTVADNMGFALKIAG--TPKDEIRKRVE----KAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPK 155
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 156 VFLMDEPLSNLDAKLRVQTRTQIAALQRQLgvTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
1.84e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVF 83
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNyalyPH-----MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:PRK13632 90 QN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALtMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-227 |
2.28e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 132.01 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIAMVFQN-YA-LYPHMT 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKI-AGTPKDEirkRVEKAAEILDL----TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:PRK11308 111 VGQILEEPLLInTSLSAAE---RREKALAMMAKvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 169 KLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-209 |
4.80e-35 |
|
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: 134.72 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDkPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHmTVADNMGFALKIAgtPKDEIRkRVEKAAEILDLTEYL--------DRKPKALSGGQRQRVAMGRAIVR 152
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDA--SDAEIR-EALERAGLDEFVAALpqgldtpiGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 153 EPKVFLMDEPLSNLDAKLRVQTRTQIAALQRqlGVTTLYVTHDqTEALTMGDRIAVI 209
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-228 |
6.36e-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: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYPHMTVADN 97
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 --MGFAlkiAGTPKDEIRKRVEKAAEIL-DLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:COG0410 99 llLGAY---ARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 175 RTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:COG0410 176 FEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-226 |
1.27e-34 |
|
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: 134.07 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIAM 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHmTVADNMGFalkiaGTPKDEIRKRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGRAI 150
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 151 VREPKVFLMDEPLSNLDAKlrvQTRTQIAALQR-QLGVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:TIGR02203 485 LKDAPILILDEATSALDNE---SERLVQAALERlMQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-224 |
3.50e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 126.12 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIAMVF 83
Cdd:cd03218 4 ENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 164 SNLDAKLRVQTRTQIAAL-QRQLGVttLYVTHDQTEALTMGDRIAVIKLG-ILQQvGAPTELY 224
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILkDRGIGV--LITDHNVRETLSITDRAYIIYEGkVLAE-GTPEEIA 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-214 |
6.27e-34 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 125.16 E-value: 6.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR------DIAMVFQNYALYPHMTVA 95
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLPDFTAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 96 DNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTR 175
Cdd:TIGR02211 102 ENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIF 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 2525772010 176 TQIAALQRQLGVTTLYVTHDQTEALTMgDRIAVIKLGIL 214
Cdd:TIGR02211 182 DLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
26-238 |
6.68e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.07 E-value: 6.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 26 LDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTT-------MQPKDRD--------IAMVFQNYALYP 90
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgeLVPADRRqlqrirtrLGMVFQSFNLWS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 HMTVADNMGFA-LKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:COG4598 109 HMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 170 LrVQtrtQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGFIGS 238
Cdd:COG4598 189 L-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-210 |
9.92e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.52 E-value: 9.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 8 HVTRIYPGNdkPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-RD--IAMVFQ 84
Cdd:COG1129 9 GISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 85 NYALYPHMTVADN--MGFALKIAGT-PKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:COG1129 87 ELNLVPNLSVAENifLGREPRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 162 PLSNLDAK-----LRVqtrtqIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIK 210
Cdd:COG1129 167 PTASLTEReverlFRI-----IRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLR 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-212 |
1.00e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 123.10 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNY 86
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 87 ALYPHmTVADNMgfalkiagtpkdeirkrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:cd03246 86 ELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525772010 167 DAKLRVQTRTQIAALQRQlGVTTLYVTHdQTEALTMGDRIAVIKLG 212
Cdd:cd03246 128 DVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDG 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-212 |
1.08e-33 |
|
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: 123.91 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGNDKpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVttmQPKDR--DIAMVFQ 84
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERrkSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 85 N--YALYPHmTVADNMGFALKIAGTPKDEIRKRVEKaaeiLDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:cd03226 79 DvdYQLFTD-SVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 163 LSNLDAKlrvqTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03226 154 TSGLDYK----NMERVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-227 |
1.12e-33 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.90 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 5 VFDHVTRiypgnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTT-----MQPKDRDI 79
Cdd:PRK10261 329 LLNRVTR-----EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgkLQALRRDI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQN-YA-LYPHMTVADNMGFALKIAGT-PKDEIRKRVEKAAEILDLT-EYLDRKPKALSGGQRQRVAMGRAIVREPK 155
Cdd:PRK10261 404 QFIFQDpYAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 156 VFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
2.13e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.25 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAM 81
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNyalyPH-----MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:PRK13648 88 VFQN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 157 FLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTmGDRIAVIKLGILQQVGAPTELYD 225
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
3.26e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.13 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGN---DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIG------GKDVTTMQ 73
Cdd:PRK13634 2 DITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 74 PKDRDIAMVFQnyalYP-HM----TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTE-YLDRKPKALSGGQRQRVAMG 147
Cdd:PRK13634 82 PLRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 148 RAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
.
gi 2525772010 228 A 228
Cdd:PRK13634 238 D 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-229 |
3.30e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN-----KGRILIGGKDVttMQPK-D-----RDIAMVFQ 84
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDI--YDPDvDvvelrRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 85 NYALYPhMTVADNMGFALKIAG-TPKDEIRKRVEKA---AEILD-LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVEESlrkAALWDeVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 160 DEPLSNLDaklrvqtrtQIAALQ-----RQLG--VTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:COG1117 179 DEPTSALD---------PISTAKieeliLELKkdYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-226 |
6.09e-33 |
|
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: 123.11 E-value: 6.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIAM 81
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYpHMTVADNMGFalkiaGTPK--DEirkRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGR 148
Cdd:cd03253 80 VPQDTVLF-NDTIGYNIRY-----GRPDatDE---EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 149 AIVREPKVFLMDEPLSNLDaklrVQTRTQI-AALQRQL-GVTTLYVTHDQTEALTmGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:cd03253 151 AILKNPPILLLDEATSALD----THTEREIqAALRDVSkGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
1.00e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 122.88 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVvfDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RD 78
Cdd:COG4604 1 MIEI--KNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 IAMVFQNYALYPHMTVADNMGFalkiaG---------TPKDeiRKRVEKAAEILDLTEYLDRKPKALSGGQRQR--VAMg 147
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAF-----GrfpyskgrlTAED--REIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 148 rAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAP------- 220
Cdd:COG4604 149 -VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPeeiitpe 227
|
250
....*....|..
gi 2525772010 221 --TELYDRPANV 230
Cdd:COG4604 228 vlSDIYDTDIEV 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-222 |
1.56e-32 |
|
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: 127.94 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDI 79
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALYPHmTVADNmgfalkIA--GTPKDEirkRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAM 146
Cdd:COG4618 409 GYLPQDVELFDG-TIAEN------IArfGDADPE---KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 147 GRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALqRQLGVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-228 |
1.86e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 122.79 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV---TTMQPKDRDIAMV 82
Cdd:PRK13644 4 LENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQN-YALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:PRK13644 83 FQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 162 PLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDqTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
24-227 |
1.89e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 122.17 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD----------RDIAMVFQNYALYPHMT 93
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglirqlrQHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADN-MGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRV 172
Cdd:PRK11264 102 VLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 173 QTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK11264 182 EVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-223 |
2.22e-32 |
|
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: 127.23 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGR--ILIGGK--DVTTMQPKDRD-----IAMVFQNYALYP 90
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDGRGrakryIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 HMTVADNMGFALKIAGTPKDEIRKRV----------EKAAEILDlteyldRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDELARMKAVitlkmvgfdeEKAEEILD------KYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-215 |
9.48e-32 |
|
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: 119.74 E-value: 9.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-RDIAMVF-QNYALYPHMTV 94
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2525772010 175 RTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQ 215
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-229 |
1.73e-31 |
|
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: 119.01 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN----KGRILIGGKDVTTMQPKDRDIAMVFQN--YALYPHMTV 94
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDL---TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 172 VQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
2.48e-31 |
|
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: 116.37 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNdkPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---RDIA 80
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQnyalyphmtvadnmgfalkiagtpkdeirkrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-224 |
2.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.81 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNY-ALYPHM 92
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRV 172
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 173 QTRTQIAALQRQLGVTTLYVTHDQTEALTmGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-212 |
3.60e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.83 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmqPKDRD-IAmvfqn 85
Cdd:COG4152 5 KGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRrIG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 Y-----ALYPHMTVADNMGF--ALKiaGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG4152 75 YlpeerGLYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 159 MDEPLSNLDAkLRVQT-RTQIAALQRQlGVTTLYVTH--DQTEALTmgDRIAVIKLG 212
Cdd:COG4152 153 LDEPFSGLDP-VNVELlKDVIRELAAK-GTTVIFSSHqmELVEELC--DRIVIINKG 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-198 |
3.68e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 117.89 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYP 90
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 HmTVADNMGFALKIAGtpkdeirKRVEKAAEILDLTEY------LDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLS 164
Cdd:PRK10247 95 D-TVYDNLIFPWQIRN-------QQPDPAIFLDDLERFalpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|....
gi 2525772010 165 NLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTE 198
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-224 |
4.61e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.04 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 15 GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQP--KDRDIA-MVFQNyalyPH 91
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 -----MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:PRK13633 96 nqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 167 DAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTmGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-226 |
2.25e-30 |
|
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: 115.79 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYpGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDI 79
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALYPHmTVADNMGFALKIAgtpKDEirkRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGR 148
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLGRPNA---TDE---EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAK--LRVQtrtqiAALQRQL-GVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTELYD 225
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTEteKLIQ-----EALEKLMkGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
.
gi 2525772010 226 R 226
Cdd:cd03254 227 K 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-227 |
2.60e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.61 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDI---------------AMVFQNYAL 88
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrllrtrlTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 YPHMTVADN-MGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRK-PKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:PRK10619 104 WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 167 DAKLrVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK10619 184 DPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
1.12e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.06 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD-IA 80
Cdd:PRK13537 6 APIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 161 EPLSNLDAklrvQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:PRK13537 164 EPTTGLDP----QARHLMWERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-222 |
1.14e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYAL-YPhM 92
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVR------EPKVFLMDEPLSNL 166
Cdd:PRK13548 92 TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 167 DakLRVQTRT-QIA---ALQRQLGVttLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:PRK13548 172 D--LAHQHHVlRLArqlAHERGLAV--IVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
2.76e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 113.99 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDhVTRIYPG-NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNK------GRILIGGKDVTTMQP 74
Cdd:PRK14246 7 AEDVFN-ISRLYLYiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 75 KD--RDIAMVFQNYALYPHMTVADNMGFALKIAGTP-KDEIRKRVEKAAEILDL----TEYLDRKPKALSGGQRQRVAMG 147
Cdd:PRK14246 86 IKlrKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 148 RAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlgVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
....*....
gi 2525772010 228 ANVFVAGFI 236
Cdd:PRK14246 244 KNELTEKYV 252
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-227 |
3.56e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.47 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN-----KGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMT 93
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIElrRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKI--AGTPKDEIRKRVEKAAEILDLTE----YLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:PRK14247 99 IFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 168 AKLRVQTRTQIAALQRQLgvTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK14247 179 PENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-216 |
3.67e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 112.99 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQP------KDRDIAMVFQNYALYPHMTVAD 96
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 97 NMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRT 176
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2525772010 177 QIAALQRQLGVTTLYVTHDQTEALTMgDRIAVIKLGILQQ 216
Cdd:PRK11629 187 LLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
4.13e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQ------- 73
Cdd:COG1137 1 MMTLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 74 -----PKDrdiAMVFQNyalyphMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGR 148
Cdd:COG1137 79 gigylPQE---ASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 149 AIVREPKVFLMDEPLSNLD--AKLRVQtrTQIAAL-QRQLGVttLYVTHDQTEALTMGDRIAVIKLG-ILQQvGAPTELY 224
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpiAVADIQ--KIIRHLkERGIGV--LITDHNVRETLGICDRAYIISEGkVLAE-GTPEEIL 224
|
...
gi 2525772010 225 DRP 227
Cdd:COG1137 225 NNP 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-195 |
1.06e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.40 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNdkPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGkdvttmqpkDRDIAMVFQNYALYPHM 92
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 --TVAD--NMGF--ALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:NF040873 71 plTVRDlvAMGRwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*....
gi 2525772010 167 DAKLRVQTRTQIAALQRQlGVTTLYVTHD 195
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHD 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-235 |
1.11e-28 |
|
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: 118.19 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV-TTMQPKDRDIAMV 82
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 163 LSNLDAKLRVQTRTQIaaLQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELydrpANVFVAGF 235
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-212 |
1.13e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.28 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPG---NDkpsvdDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-RD- 78
Cdd:COG3845 6 LELRGITKRFGGvvaND-----DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 79 -IAMVFQNYALYPHMTVADN--MGF-ALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREP 154
Cdd:COG3845 81 gIGMVHQHFMLVPNLTVAENivLGLePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 155 KVFLMDEPLSNLdaklrvqTRTQIAALQRQL------GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:COG3845 161 RILILDEPTAVL-------TPQEADELFEILrrlaaeGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-199 |
1.52e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.02 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 26 LDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR------DIAMVFQNYALYPHMTVADNMG 99
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 100 FALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAklrvQTRTQIA 179
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR----QTGDKIA 186
|
170 180
....*....|....*....|....
gi 2525772010 180 ----ALQRQLGVTTLYVTHDQTEA 199
Cdd:PRK10584 187 dllfSLNREHGTTLILVTHDLQLA 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
1.95e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.94 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVV-FDHVTRIYPGNDKPS--------------------VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNK 59
Cdd:COG1134 1 MSSMIeVENVSKSYRLYHEPSrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 60 GRILIGGKdVTTMQpkdrDIAMVFQnyalyPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGG 139
Cdd:COG1134 81 GRVEVNGR-VSALL----ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 140 QRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGA 219
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
....*..
gi 2525772010 220 PTELYDR 226
Cdd:COG1134 230 PEEVIAA 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-212 |
3.90e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.79 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYPGNDKPS----VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAG-LEEVN-KGRILIGGKDVTTMQP 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGvSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 75 KDRdIAMVFQNYALYPHMTVADNMGFALKIAGtpkdeirkrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREP 154
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 155 KVFLMDEPLSNLD---AKLRVQTRTQIAalqrQLGVTTLYVTHD-QTEALTMGDRIAVIKLG 212
Cdd:cd03213 131 SLLFLDEPTSGLDsssALQVMSLLRRLA----DTGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-198 |
4.46e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 110.17 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL------EEVnkgRIL---IGGKDVTTMQPKd 76
Cdd:COG1119 6 LRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygNDV---RLFgerRGGEDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 rdIAMV---FQNYaLYPHMTVADnM---GF--ALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGR 148
Cdd:COG1119 80 --IGLVspaLQLR-FPRDETVLD-VvlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTE 198
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-223 |
6.02e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 115.12 E-value: 6.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIA 80
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYpHMTVADNMGFALKiagtpKDEIRKRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGRA 149
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-----EQYSREQIEEAARMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 150 IVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLgvTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-229 |
6.50e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.13 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN-----KGRILIGGKDV----TTMQPKDRDIAMVFQNYALYPh 91
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyerrVNLNRLRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKIAG-TPKDEIRKRVE---KAAEILD-LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:PRK14258 102 MSVYDNVAYGVKIVGwRPKLEIDDIVEsalKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 167 D--AKLRVQTRTQIAALQRQLgvTTLYVTHDQTEALTMGDRIAVIK-----LGILQQVGAPTELYDRPAN 229
Cdd:PRK14258 182 DpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSPHD 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-227 |
7.74e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.20 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGN-DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK--DRDIA 80
Cdd:TIGR00958 479 IEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHmTVADNMGFALKiaGTPKDEIRKRVEKAAE---ILDLTEYLD----RKPKALSGGQRQRVAMGRAIVRE 153
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLT--DTPDEEIMAAAKAANAhdfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 154 PKVFLMDEPLSNLDAklrvQTRTQIAALQRQLGVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:TIGR00958 636 PRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-227 |
1.45e-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: 114.28 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM--QPKDRDIA 80
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLdvQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHmTVADNmgfalkIAG----TPKDeirkrVEKAAEILDLTEYLDRKP-----------KALSGGQRQRVA 145
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFEN------IAGgaplTLDE-----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 146 MGRAIVREPKVFLMDEPLSNLDaklrvqTRTQ---IAALQRqLGVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALD------NRTQaivSESLER-LKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDE 670
|
....*
gi 2525772010 223 LYDRP 227
Cdd:TIGR03797 671 LMARE 675
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-222 |
1.72e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.95 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMTV 94
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFA----LKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKL 170
Cdd:PRK11231 94 RELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 171 RVqtrtQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:PRK11231 174 QV----ELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
1.83e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIAMVFQNyalyPH-----M 92
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaeNEKWVRSKVGLVFQD----PDdqvfsS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRV 172
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 173 QTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-247 |
1.84e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMTVADNM 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 99 GFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIV-------REPKVFLMDEPLSNLDakLR 171
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD--LA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 172 VQTRT-QIAalqRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP--ANVFvagfiGSPsMNINT 245
Cdd:COG4559 175 HQHAVlRLA---RQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEllERVY-----GAD-LRVLA 245
|
..
gi 2525772010 246 HP 247
Cdd:COG4559 246 HP 247
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-229 |
3.00e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.32 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN-----KGRILIGGKDV-----TTMQPKdRDIAMVFQN 85
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprtDTVDLR-KEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPhMTVADNMGFALKIAGTPK----DEIRKRVEKAAEILD-LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK14239 95 PNPFP-MSIYENVVYGLRLKGIKDkqvlDEAVEKSLKGASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLgvTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-212 |
3.17e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 113.28 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIYPGNDKPS--VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD------RDIA 80
Cdd:PRK10535 10 IRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrEHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEAlTMGDRIAVIKLG 212
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDG 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-212 |
5.52e-27 |
|
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: 106.84 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYPHMTVADN-- 97
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTVEENll 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 MGFALkiagtpkdeiRKRVEKA--AEILD----LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:TIGR03410 98 TGLAA----------LPRRSRKipDEIYElfpvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSII 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2525772010 172 VQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:TIGR03410 168 KDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-226 |
5.88e-27 |
|
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: 106.80 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK--DRDIAM 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYpHMTVADNMgfALKIAGTPkdeiRKRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRAI 150
Cdd:cd03252 81 VLQENVLF-NRSIRDNI--ALADPGMS----MERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 151 VREPKVFLMDEPLSNLDAKlrvQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:cd03252 154 IHNPRILIFDEATSALDYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-228 |
8.58e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 109.19 E-value: 8.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 38 GPSGCGKSTTLRMLAGLEEVNKGRILIGGK---DVTT---MQPKDRDIAMVFQNYALYPHMTVADNMGFALKiagtPKDe 111
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----KSM- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 112 iRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLY 191
Cdd:PRK11144 106 -VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 2525772010 192 VTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-218 |
4.27e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 109.36 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHmTVADNmgfalkIAGTPKDEIRKRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRA 149
Cdd:TIGR01842 396 YLPQDVELFPG-TVAEN------IARFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 150 IVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHdQTEALTMGDRIAVIKLGILQQVG 218
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-209 |
6.01e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.32 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDvttmqP-KDR-----DIAMVF-QNYALYPHMT 93
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PfKRRkefarRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNmgFAL--KIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQR--VAMgrAIVREPKVFLMDEPLSNLD-- 167
Cdd:COG4586 113 AIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGLDvv 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 168 AKLRVqtRTQIAALQRQLGVTTLYVTHDQT--EALTmgDRIAVI 209
Cdd:COG4586 189 SKEAI--REFLKEYNRERGTTILLTSHDMDdiEALC--DRVIVI 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-195 |
8.47e-26 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 108.60 E-value: 8.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAM 81
Cdd:TIGR02868 335 LELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYpHMTVADNMGFAlkiAGTPKDEirkRVEKAAEILDLTEYLDRKP-----------KALSGGQRQRVAMGRAI 150
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLA---RPDATDE---ELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525772010 151 VREPKVFLMDEPLSNLDAKLRVQ-TRTQIAALQrqlGVTTLYVTHD 195
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADElLEDLLAALS---GRTVVLITHH 529
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-223 |
8.78e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.82 E-value: 8.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVFDHVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM---QPKDR 77
Cdd:PRK10895 1 MATLTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 78 DIAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRK-RVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 157 FLMDEPLSNLDAKLRVQTRTQIAALqRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-218 |
1.69e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 102.61 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVttmqpkdrdiAMVFQNYALYPHMTVAD 96
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 97 NMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2525772010 177 QIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-224 |
1.75e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGND---KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTT------MQP 74
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 75 KDRDIAMVFQnyalYPHM-----TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLT-EYLDRKPKALSGGQRQRVAMGR 148
Cdd:PRK13643 82 VRKKVGVVFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQrQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-223 |
2.25e-25 |
|
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: 107.91 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK--DRDIAM 81
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYALYPHmTVADNMgfALKIAGTPKDEIRKRVEKAAE---ILDLTE----YLDRKPKALSGGQRQRVAMGRAIVREP 154
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNI--ALCNPGAPFEHVIHAAKLAGAhdfISELPQgyntEVGEKGANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 155 KVFLMDEPLSNLDAKLRvqtrtqiAALQRQL-----GVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:TIGR01846 613 RILIFDEATSALDYESE-------ALIMRNMreicrGRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-194 |
2.28e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.35 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:PRK13657 334 AVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYpHMTVADNmgfaLKIaGTPkDEIRKRVEKAAEILDLTEYLDRKPK-----------ALSGGQRQRVAMGRA 149
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDN----IRV-GRP-DATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2525772010 150 IVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRqlGVTTLYVTH 194
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH 528
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-235 |
3.21e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.16 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT----TMQPKDRDIAMVFQNYALYPHM 92
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVAD-NMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:PRK13638 93 TDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 172 VQtrtQIAALQR--QLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANVFVAGF 235
Cdd:PRK13638 173 TQ---MIAIIRRivAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-194 |
3.84e-25 |
|
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: 106.83 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYPGnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDI 79
Cdd:COG5265 356 GEVRFENVSFGYDP-ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALYpHMTVADNMGFALkiAGTPKDEIRkRVEKAAEILDLTEYLdrkPKA-----------LSGGQRQRVAMGR 148
Cdd:COG5265 435 GIVPQDTVLF-NDTIAYNIAYGR--PDASEEEVE-AAARAAQIHDFIESL---PDGydtrvgerglkLSGGEKQRVAIAR 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 149 AIVREPKVFLMDEPLSNLDaklrvqTRTQiAALQRQL-----GVTTLYVTH 194
Cdd:COG5265 508 TLLKNPPILIFDEATSALD------SRTE-RAIQAALrevarGRTTLVIAH 551
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
3.84e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV----TTMQPKDRDIAMVFQ--NYALYPhMT 93
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVGMVFQdpDNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQ 173
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 174 TRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-212 |
4.81e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 101.39 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGN-DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK--DRDIA 80
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHmTVADNMGFALkiAGTPKDEIRKRVEKAAE---ILDL-----TEyLDRKPKALSGGQRQRVAMGRAIVR 152
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGL--QSCSFECVKEAAQKAHAhsfISELasgydTE-VGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 153 EPKVFLMDEPLSNLDAKLRVQTRTqiaALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQ---ALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-197 |
9.05e-25 |
|
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: 99.15 E-value: 9.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTrIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIggkdvttmqPKDRDIAMVF 83
Cdd:cd03223 1 IELENLS-LATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNyalyPHMTvadnmgfalkiAGTPKDEIrkrvekaaeildlteyldRKP--KALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:cd03223 71 QR----PYLP-----------LGTLREQL------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 2525772010 162 PLSNLDaklrVQTRTQIAALQRQLGVTTLYVTHDQT 197
Cdd:cd03223 118 ATSALD----EESEDRLYQLLKELGITVISVGHRPS 149
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-223 |
1.30e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 105.31 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 12 IYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVnKGRILIGGKDVTTMQPKD--RDIAMVFQNYALy 89
Cdd:PRK11174 357 ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESwrKHLSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNMGFALKIAGtpKDEIRKRVEKAaeilDLTEYLDRKPKAL-----------SGGQRQRVAMGRAIVREPKVFL 158
Cdd:PRK11174 435 PHGTLRDNVLLGNPDAS--DEQLQQALENA----WVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 159 MDEPLSNLDA---KLRVQTRTQIAALQrqlgvTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK11174 509 LDEPTASLDAhseQLVMQALNAASRRQ-----TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-294 |
1.77e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYAL------ 88
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfefdv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 --------YPHMTVADNMgfalkiagTPKDeiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK09536 95 rqvvemgrTPHRSRFDTW--------TETD--RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP-------ANVFVA 233
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlraafdARTAVG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 234 GFIGSPSMNINTHPVINgqakiGDDTIDLPR-----------EAVAKLtAEDNGQIIVGFRPE-DADLATADD 294
Cdd:PRK09536 244 TDPATGAPTVTPLPDPD-----RTEAAADTRvhvvgggqpaaRAVSRL-VAAGASVSVGPVPEgDTAAETAAR 310
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-168 |
2.25e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.18 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRdIAMVFQNYALYPHMTVA 95
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 96 DNMGFALKIAGTPkdeiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:PRK13539 92 ENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-224 |
2.51e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGK----DVTTMQPKDRDIAMVFQN--- 85
Cdd:PRK13639 11 YP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVGIVFQNpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 --YAlyPhmTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:PRK13639 90 qlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 164 SNLDAklrvQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13639 166 SGLDP----MGASQIMKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-212 |
2.66e-24 |
|
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: 98.70 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGND---KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvttmqpkdrdIA 80
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNyALYPHMTVADNMGFalkiaGTPKDEIR-KRVEKAA------EIL---DLTEyLDRKPKALSGGQRQRVAMGRAI 150
Cdd:cd03250 70 YVSQE-PWIQNGTIRENILF-----GKPFDEERyEKVIKACalepdlEILpdgDLTE-IGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 151 VREPKVFLMDEPLSNLDAklrvQTRTQIA--ALQRQL--GVTTLYVTHdQTEALTMGDRIAVIKLG 212
Cdd:cd03250 143 YSDADIYLLDDPLSAVDA----HVGRHIFenCILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-220 |
2.81e-24 |
|
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: 99.11 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIA 80
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHmTVADNMGF-----------ALKIAGtpkdeIRKRVEKAAEILDLTeyLDRKPKALSGGQRQRVAMGRA 149
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLDPfgeysdeelwqALERVG-----LKEFVESLPGGLDTV--VEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 150 IVREPKVFLMDEPLSNLDaklrVQTRTQIAALQRQL--GVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAP 220
Cdd:cd03244 154 LLRKSKILVLDEATASVD----PETDALIQKTIREAfkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-227 |
3.08e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM---QPKDRDIAMVFQNYALYPHMTVADN 97
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQIARMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 MGFA-------------LKIAGTPKDEiRKRVEKAAEILD---LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:PRK11300 101 LLVAqhqqlktglfsglLKTPAFRRAE-SEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 162 PLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQteALTMG--DRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDM--KLVMGisDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-224 |
3.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmQPKDRDI-------AMVFQnyalYPHM--- 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-TSKNKDIkqirkkvGLVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 --TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYL-DRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 170 LRVQTRTQIAALQrQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13649 180 GRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-212 |
3.30e-24 |
|
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: 97.89 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 18 KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD---IAMV---FQNYALYPH 91
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFalkiagtpkdeirkrvekaaeildlteyldrkPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDaklr 171
Cdd:cd03215 93 LSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD---- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 172 VQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:cd03215 137 VGAKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-227 |
5.83e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.45 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-----RDIAMVFQNYALYPH 91
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKI-AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKL 170
Cdd:PRK11831 99 MNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 171 RVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-194 |
7.78e-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: 97.43 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK-DRDIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 KIAGTPkdeiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAA-L 181
Cdd:TIGR01189 99 AIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhL 174
|
170
....*....|...
gi 2525772010 182 QRQLGVttLYVTH 194
Cdd:TIGR01189 175 ARGGIV--LLTTH 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-227 |
8.15e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 8.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQN- 85
Cdd:PRK13652 9 LCYSYSGS-KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 --YALYPhmTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:PRK13652 88 ddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-195 |
1.11e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 97.89 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 19 PSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILI----GGKDVTTMQPKD------RDIAMVFQNYAL 88
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREilalrrRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 YPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYL-DRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:COG4778 105 IPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180
....*....|....*....|....*...
gi 2525772010 168 AKLRVQTRTQIAALQRQlGVTTLYVTHD 195
Cdd:COG4778 185 AANRAVVVELIEEAKAR-GTAIIGIFHD 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-218 |
1.19e-23 |
|
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: 103.17 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTmqpkdrDIAMVFQN 85
Cdd:TIGR01257 1940 LNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPH-------MTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:TIGR01257 2014 MGYCPQfdaiddlLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-224 |
1.25e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYPGN---DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGG-------KDVTTM 72
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 73 QPKDRDIAMVFQ--NYALYPHmTVADNMGFALKIAGTPKDEIRKRVekaAEILDLT----EYLDRKPKALSGGQRQRVAM 146
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKV---PELLKLVqlpeDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 147 GRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-225 |
1.39e-23 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 97.61 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 26 LDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvtTMQPKDRDIAMVFQNYAL---YP---HMTVADNMG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPisvAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 100 FALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDaklrVQTRTQIA 179
Cdd:TIGR03771 78 GHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD----MPTQELLT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 180 ALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKlGILQQVGAPTELYD 225
Cdd:TIGR03771 154 ELFIELagaGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-207 |
2.09e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 12 IYPGNDKpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEV-----NKGRILIGGKDV--TTMQPKD--RDIAMV 82
Cdd:PRK14243 18 VYYGSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEvrRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHmTVADNMGFALKIAGTPK--DEIRKRVEKAAEILD-LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:PRK14243 97 FQKPNPFPK-SIYDNIAYGARINGYKGdmDELVERSLRQAALWDeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 160 DEPLSNLD--AKLRVQtrTQIAALQRQLgvTTLYVTHDQTEALTMGDRIA 207
Cdd:PRK14243 176 DEPCSALDpiSTLRIE--ELMHELKEQY--TIIIVTHNMQQAARVSDMTA 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-168 |
2.43e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 96.96 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNK---GRILIGGKDVTTMQPKDRdIAMVFQNYALYPHMTVADNMG 99
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 100 FALKIAG---TPKDEIRKRVEKAAEI-LDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:cd03234 104 YTAILRLprkSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-194 |
4.65e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTrIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIggkdvttmqPKDRDIAM 81
Cdd:COG4178 361 GALALEDLT-LRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQN-Y--------AL-YPHmtvadnmgfalkIAGTPKDEIRKRVEKAAEILDLTEYLDRK---PKALSGGQRQRVAMGR 148
Cdd:COG4178 431 LPQRpYlplgtlreALlYPA------------TAEAFSDAELREALEAVGLGHLAERLDEEadwDQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAKLRVQTrtqIAALQRQL-GVTTLYVTH 194
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-223 |
6.58e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.58 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGE---FLvlvGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmqPKDRDIAM----VFQNYALYPHMT 93
Cdd:NF033858 282 VDHVSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRRrvgyMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQ 173
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 174 TRTQIAALQRQLGVTTLYVTHDQTEALTMgDRIAVIKLGILQQVGAPTEL 223
Cdd:NF033858 436 FWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-227 |
8.34e-23 |
|
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: 100.02 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMqPKDR---DIAMVFQNYALYpHMT 93
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 94 VADNMgfALKIAGTPKDEIRkRVEKAAEILDLteyLDRKPKA-----------LSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:TIGR03796 569 VRDNL--TLWDPTIPDADLV-RACKDAAIHDV---ITSRPGGydaelaegganLSGGQRQRLEIARALVRNPSILILDEA 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 163 LSNLDAklrvQTRTQIAALQRQLGVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:TIGR03796 643 TSALDP----ETEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-219 |
1.08e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT---TMQPKDRDIAMVFQNYALYPHMTVADNMGF 100
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqTAKIMREAVAIVPEGRRVFSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 101 ALKIAgtPKDEIRKRVEKAAEILD-LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:PRK11614 104 GGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2525772010 180 ALqRQLGVTTLYVTHDQTEALTMGDRIAVIKLG--ILQQVGA 219
Cdd:PRK11614 182 QL-REQGMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGD 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-225 |
1.38e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR-DIAMVFQNYA 87
Cdd:PRK13536 47 VSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 88 LYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 168 AKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYD 225
Cdd:PRK13536 205 PHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-212 |
2.19e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 92.76 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD-IAMV 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYpHMTVADNMGfalkiagtpkdeirkrvekaaeildlteyldrkpKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 163 LSNLDAKLRVQTRTQIAALQRqlGVTTLYVTHDQTeALTMGDRIAVIKLG 212
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENG 172
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-238 |
2.27e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.33 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 8 HVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNkGRI----LIGGKDVTTMQPKD------R 77
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsaTFNGREILNLPEKElnklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 78 DIAMVFQN--YALYPHMTVADNMGFALKIagtpkdeiRKRVEKAAEILDLTEYLD-------RK-----PKALSGGQRQR 143
Cdd:PRK09473 98 QISMIFQDpmTSLNPYMRVGEQLMEVLML--------HKGMSKAEAFEESVRMLDavkmpeaRKrmkmyPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 144 VAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
250
....*....|....*
gi 2525772010 224 YDRPANVFVAGFIGS 238
Cdd:PRK09473 250 FYQPSHPYSIGLLNA 264
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-195 |
3.52e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIggkdvttmqPKDRDIAMVFQN 85
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPHMTVADN--MGFA-------------LKIAGTPKD-----------------EIRKRVEKAAEILDLT-EYLDRK 132
Cdd:COG0488 70 PPLDDDLTVLDTvlDGDAelraleaeleeleAKLAEPDEDlerlaelqeefealggwEAEARAEEILSGLGFPeEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 133 PKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAklrvQTrtqIAALQRQL----GvTTLYVTHD 195
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ES---IEWLEEFLknypG-TVLVVSHD 208
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-196 |
4.05e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLE--EVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYP 90
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 HMTVADNMGFAL-KIAGTPKD--EIRKRVEKAAEILDL-TEYLDRkpkAL----SGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:COG0396 91 GVSVSNFLRTALnARRGEELSarEFLKLLKEKMKELGLdEDFLDR---YVnegfSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2525772010 163 LSNLDaklrvqtrtqIAALQ---------RQLGVTTLYVTHDQ 196
Cdd:COG0396 168 DSGLD----------IDALRivaegvnklRSPDRGILIITHYQ 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-226 |
5.51e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTT----LRMLAgleevNKGRILIGGKDVTT-----MQPKDRDIAMVFQ--NYALY 89
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNlnrrqLLPVRHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNMGFALKI--AGTPKDEIRKRVEKAAEILDL-TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNL 166
Cdd:PRK15134 377 PRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 167 DAKLRVQTRTQIAALQRQLGVTTLYVTHD---------QTEALTMGDriaVIKLGILQQV-GAPTELYDR 226
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDlhvvralchQVIVLRQGE---VVEQGDCERVfAAPQQEYTR 523
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-223 |
7.04e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMTVADNMG 99
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 100 FAlKIAGTP-----KDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK10253 104 RG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 175 RTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK10253 183 LELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-227 |
8.20e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 8.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIY-PGN--DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT------TMQPKD 76
Cdd:PRK13641 5 FENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 RDIAMVFQnyalYPHM-----TVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYL-DRKPKALSGGQRQRVAMGRAI 150
Cdd:PRK13641 85 KKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 151 VREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-212 |
9.05e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV---TTMQPKDRDIAMV 82
Cdd:PRK11288 7 FDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHMTVADN---------MGFALKiaGTPKDEIRKRVEKAAEILDLteylDRKPKALSGGQRQRVAMGRAIVRE 153
Cdd:PRK11288 85 YQELHLVPEMTVAENlylgqlphkGGIVNR--RLLNYEAREQLEHLGVDIDP----DTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 154 PKVFLMDEPLSNLDAKLRVQTRTQIAALqRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-228 |
1.92e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.46 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTT----LRML-AGLEEVNkGRILIGGKDVTTMQPKDRDIAMVFQN--YALY 89
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILpAGVRQTA-GRVLLDGKPVAPCALRGRKIATIMQNprSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNMGFALKIAGTPKDEIR-KRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPADDATlTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 169 KLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-223 |
2.48e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 95.28 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD-RD-IAMVF 83
Cdd:PRK11160 341 LNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHmTVADNmgfaLKIAGTPKDEirkrvEKAAEILD---LTEYLDRKP----------KALSGGQRQRVAMGRAI 150
Cdd:PRK11160 421 QRVHLFSA-TLRDN----LLLAAPNASD-----EALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 151 VREPKVFLMDEPLSNLDAklrvQTRTQIAALQRQL--GVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDA----ETERQILELLAEHaqNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
16-212 |
5.38e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.23 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL---EEVNKGRILIGGKDVTTMQPKDRDI-------AMVFQN 85
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrksrantGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPHMTVADNMGFAlKIAGTP---------KDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:PRK09984 95 FNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 157 FLMDEPLSNLD---AKLRVQTRTQIaalQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK09984 174 ILADEPIASLDpesARIVMDTLRDI---NQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-229 |
5.79e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 19 PSVDDLNLDIKDGEFLVLVGPSGCGKSTT----LRML--AG---------LEEVNKGRILIGGKDVTTMQP-KDRDIAMV 82
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHvRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQN--YALYPHMTVADNMGFALKI-AGTPKDEI---RKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLhQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 157 FLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPAN 229
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-212 |
6.48e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDkpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR---DIA 80
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 81 MVFQNYALYPHMTVADNM--GFAL--KIAGTPKDEIRKRVEKAAEIL---DLTEYLDRKPKALSGGQRQRVAMGRAIVRE 153
Cdd:PRK09700 84 IIYQELSVIDELTVLENLyiGRHLtkKVCGVNIIDWREMRVRAAMMLlrvGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 154 PKVFLMDEPLSNLDAKlrvqTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK09700 164 AKVIIMDEPTSSLTNK----EVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-212 |
8.24e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---RDIAMVFQN---YALY 89
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNMGFAL--KIAGTP---KDEIRKRVEKAAEILDL-TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:COG1129 343 LDLSIRENITLASldRLSRGGlldRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 164 SNLDaklrVQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:COG1129 423 RGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-209 |
1.38e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 18 KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRDIAMVF------QNYALYPH 91
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMgfALKIAGTP---------KDEIRKRVEKAAEILDL-TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDE 161
Cdd:COG3845 351 MSVAENL--ILGRYRRPpfsrggfldRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2525772010 162 PLSNLDAKLRVQTRTQIAALqRQLGVTTLYVTHDQTEALTMGDRIAVI 209
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-228 |
1.50e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 15 GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTT----LRMLAGLEEV-NKGRILIGGKDV------TTMQPKDRDIAMVF 83
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGESLlhaseqTLRGVRGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QN--YALYPHMTVADNMGFALKI-AGTPKDEIRkrvekaAEILDLteyLDRK------------PKALSGGQRQRVAMGR 148
Cdd:PRK15134 99 QEpmVSLNPLHTLEKQLYEVLSLhRGMRREAAR------GEILNC---LDRVgirqaakrltdyPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 149 AIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-224 |
1.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGN---DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTT------MQP 74
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 75 KDRDIAMVFQnyalYPHM-----TVADNMGFALKIAGTPKDEIRKRVEKAaeILDL---TEYLDRKPKALSGGQRQRVAM 146
Cdd:PRK13646 83 VRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRL--LMDLgfsRDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 147 GRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-227 |
2.61e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.57 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEE----VNKGRILIGGKDVTTMQPKDR------DIAMVFQN--YA 87
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 88 LYPHMTVADNMGFALKI-AGTPKdeiRKRVEKAAEIL------DLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVhQGGNK---KTRRQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.86e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.29 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIG----------GKDVTTMQPKD--------RDIAMV 82
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKiknfkelrRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQ--NYALYPHmTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTE-YLDRKPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:PRK13631 122 FQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 160 DEPLSNLDAKLRvQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPA 228
Cdd:PRK13631 201 DEPTAGLDPKGE-HEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-226 |
3.84e-20 |
|
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: 92.11 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFDHVTRIYpGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMqpkDRDIAMV 82
Cdd:TIGR01193 473 DIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNY-ALYPHM---TVADNMGFALKiAGTPKDEIRKRVEkAAEILDLTEY--------LDRKPKALSGGQRQRVAMGRAI 150
Cdd:TIGR01193 549 FINYlPQEPYIfsgSILENLLLGAK-ENVSQDEIWAACE-IAEIKDDIENmplgyqteLSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 151 VREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlgvTTLYVTHDQTEAlTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-227 |
4.21e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 91.70 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 12 IYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALY 89
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHmTVADNMgfALkiaGTPkDEIRKRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGRAIVREPKVFL 158
Cdd:PRK10789 402 SD-TVANNI--AL---GRP-DATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 159 MDEPLSNLDAklrvQTRTQIAALQRQLGVT-TLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK10789 475 LDDALSAVDG----RTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
10-222 |
6.04e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.07 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 10 TRIYPgndkpsvddLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEvNKGRILIGGKDVTTM-------------QPKD 76
Cdd:PRK03695 10 TRLGP---------LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWsaaelarhraylsQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 RDIAM-VFQNYALYPHmtvadnmgfalkiAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVR--- 152
Cdd:PRK03695 80 PPFAMpVFQYLTLHQP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 153 ----EPKVFLMDEPLSNLDAklrvqtrTQIAALQR------QLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:PRK03695 147 dinpAGQLLLLDEPMNSLDV-------AQQAALDRllselcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-227 |
1.10e-19 |
|
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: 87.19 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILI-----GGKDVTTMQPKDR------DIAMVFQNYALYPH 91
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERrrlmrtEWGFVHQNPRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVA--DNMGFAL---------KIAGTPKDEIRKrVEkaaeiLDLTEyLDRKPKALSGGQRQRVAMGRAIVREPKVFLMD 160
Cdd:TIGR02323 101 MRVSagANIGERLmaigarhygNIRATAQDWLEE-VE-----IDPTR-IDDLPRAFSGGMQQRLQIARNLVTRPRLVFMD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 161 EPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:TIGR02323 174 EPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-212 |
1.94e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.90 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGK-----DVTTMQPKDR------DIAMVFQNYA--L 88
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERrrllrtEWGFVHQHPRdgL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 YPHMTVADNMGFALKIAGTPK-DEIRkrvEKAAEILDLTEY----LDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:PRK11701 103 RMQVSAGGNIGERLMAVGARHyGDIR---ATAGDWLERVEIdaarIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 164 SNLDakLRVQTR--TQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK11701 180 GGLD--VSVQARllDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-212 |
2.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL--------------EEVNK--GRILIGGKDVTTMQPKDRDI----- 79
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdEKNKKktKEKEKVLEKLVIQKTRFKKIkkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 -----AMVFQ--NYALYpHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTE-YLDRKPKALSGGQRQRVAMGRAIV 151
Cdd:PRK13651 103 irrrvGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 152 REPKVFLMDEPLSNLDAKlRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQ-GVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-227 |
2.21e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.77 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVT--TMQPKDRDIAMVFQN--YALYPHMTVA 95
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 96 DNMGFALKI-AGTPKDEIRKRVEKAAEILDL-TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQ 173
Cdd:PRK15112 108 QILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 174 TRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK15112 188 LINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-222 |
3.01e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEvNKGRILIGGKDVTTMQPKD--RDIAM------------VFQNYALY 89
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYlsqqqsppfampVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHmtvadnmgfalkiAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVR-------EPKVFLMDEP 162
Cdd:COG4138 94 QP-------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 163 LSNLDAklrvqtrTQIAALQR------QLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTE 222
Cdd:COG4138 161 MNSLDV-------AQQAALDRllrelcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-217 |
9.49e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 9.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFD--HVTRiypgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---R 77
Cdd:PRK09700 263 ETVFEvrNVTS----RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 78 DIAMVFQNY---ALYPHMTVADNMGFA--LKIAG--------TPKDEiRKRVEKAAEILDLT-EYLDRKPKALSGGQRQR 143
Cdd:PRK09700 339 GMAYITESRrdnGFFPNFSIAQNMAISrsLKDGGykgamglfHEVDE-QRTAENQRELLALKcHSVNQNITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 144 VAMGRAIVREPKVFLMDEPLSNLDaklrVQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILQQV 217
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-167 |
1.35e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 83.36 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQpKDRDIAMVFQNYALYPHM 92
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 93 TVADNMGFALKIAGTpkdEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:PRK13543 98 STLENLHFLCGLHGR---RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-222 |
2.07e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVFDHVTRIYPgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRdIAM 81
Cdd:PRK15056 5 AGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 82 VFQNYAL---YP-------HMTVADNMGFaLKIagtPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIV 151
Cdd:PRK15056 83 VPQSEEVdwsFPvlvedvvMMGRYGHMGW-LRR---AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 152 REPKVFLMDEPLSNLDaklrVQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGILqqVGAPTE 222
Cdd:PRK15056 159 QQGQVILLDEPFTGVD----VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVL--ASGPTE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-195 |
2.09e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPgnDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGgkdvTTMQ----PKDRDi 79
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVKigyfDQHQE- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 amvfqnyALYPHMTVADNMGfALKIAGTPKdEIRKRVEKaaeiLDLT-EYLDRKPKALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:COG0488 389 -------ELDPDKTVLDELR-DGAPGGTEQ-EVRGYLGR----FLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190
....*....|....*....|....*....|....*...
gi 2525772010 159 MDEPLSNLDaklrVQTRTQIA-ALQRQLGvTTLYVTHD 195
Cdd:COG0488 456 LDEPTNHLD----IETLEALEeALDDFPG-TVLLVSHD 488
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-212 |
2.39e-18 |
|
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: 82.54 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPK-DRDIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 KIAGTpkdeirKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQ 182
Cdd:cd03231 99 ADHSD------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170 180 190
....*....|....*....|....*....|
gi 2525772010 183 RQLGVTTLYVTHDQTEAltmGDRIAVIKLG 212
Cdd:cd03231 173 ARGGMVVLTTHQDLGLS---EAGARELDLG 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-235 |
2.62e-18 |
|
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: 86.39 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLE--EVNKGRIL------------------------IGGK--- 67
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpskvgepcpvCGGTlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 68 -DVTTMQPKD-------RDIAMVFQ-NYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSG 138
Cdd:TIGR03269 92 eEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 139 GQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHdQTEALT-MGDRIAVIKLGILQQV 217
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDKAIWLENGEIKEE 250
|
250
....*....|....*...
gi 2525772010 218 GAPTELydrpANVFVAGF 235
Cdd:TIGR03269 251 GTPDEV----VAVFMEGV 264
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-223 |
3.45e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 24 LNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHMTVADNMGF- 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELVAIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 101 ------ALkiaGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK10575 110 rypwhgAL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 175 RTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-208 |
3.80e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 82.84 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 27 DIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRIligGKDVTTMQPKDRDIAMVFQnyalyphMTVADNMGFALKIAG 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYE-------GTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 107 TP---KDEIrkrvekaAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQR 183
Cdd:cd03237 91 THpyfKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*
gi 2525772010 184 QLGVTTLYVTHDQTEALTMGDRIAV 208
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-196 |
7.73e-18 |
|
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: 81.03 E-value: 7.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLE--EVNKGRILIGGKDVTTMQPKDR---DIAMVFQNYALYP 90
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 HMTVAD-----NMGFalkiagtpkdeirkrvekaaeildlteyldrkpkalSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:cd03217 91 GVKNADflryvNEGF------------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190
....*....|....*....|....*....|..
gi 2525772010 166 LDAK-LRVQTRTqIAALqRQLGVTTLYVTHDQ 196
Cdd:cd03217 135 LDIDaLRLVAEV-INKL-REEGKSVLIITHYQ 164
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-237 |
8.70e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 8.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 18 KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEV-----NKGRILIGGKDVTTMQPK---DRDIAMVFQNYALY 89
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlefRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PhMTVADNMGFALKIAG-TPKDEIR----KRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLS 164
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHKlVPRKEFRgvaqARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 165 NLDAKLRVQTRTQIAALQRQLgvTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRPANV----FVAGFIG 237
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-169 |
4.68e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmqpKDRDiamVFQNYALY--------PHMT 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 94 VADNMGFALKIAGTPKDEirkRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-217 |
6.69e-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: 78.46 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN---KGRILIGGKDVTTMQPK-DRDIAMVFQNYALYPH 91
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKIAGTpkDEIRKrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:cd03233 98 LTVRETLDFALRCKGN--EFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2525772010 172 VQTRTQIAALQRQLGVTTLyVTHDQT--EALTMGDRIAVIKLGilQQV 217
Cdd:cd03233 155 LEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEG--RQI 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-223 |
6.99e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.48 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLR-MLAGLEEVNKGRILIGGKdvttmqpkdrdIAMVFQNYALYpHMTV 94
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----------VAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFalkiaGTPKDeiRKRVEKAAEIL------------DLTEYLDRKPKaLSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:PLN03130 696 RDNILF-----GSPFD--PERYERAIDVTalqhdldllpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 163 LSNLDAKLRVQTRTQiaALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PLN03130 768 LSALDAHVGRQVFDK--CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-216 |
1.06e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.56 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVF 83
Cdd:PRK10522 325 LRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYPHMtvadnmgfaLKIAGTPKDEirKRVEKAAEILDLTEYLDRKPK-----ALSGGQRQRVAMGRAIVREPKVFL 158
Cdd:PRK10522 404 TDFHLFDQL---------LGPEGKPANP--ALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 159 MDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQtEALTMGDRIAVIKLGILQQ 216
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSE 529
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-227 |
2.28e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.18 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEE----VNKGRILIGGKDVTTMQPKDR------DIAMVFQN--YAL 88
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 YPHMTVADNMGFALkiagtPKDEIRK--------RVEKAAEIL------DLTEYLDRKPKALSGGQRQRVAMGRAIVREP 154
Cdd:COG4170 103 DPSAKIGDQLIEAI-----PSWTFKGkwwqrfkwRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 155 KVFLMDEPLSNLDAKlrvqTRTQI----AALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:COG4170 178 RLLIADEPTNAMEST----TQAQIfrllARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-225 |
1.10e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 31 GEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQP---KDRDIAMVFQNYALYPHMTVADNMGFALkiAGT 107
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPLLFPNLSVKENILFGL--PKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 108 PKDEirKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAklrVQTR---TQIAALQrQ 184
Cdd:PRK15439 115 QASM--QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP---AETErlfSRIRELL-A 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2525772010 185 LGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYD 225
Cdd:PRK15439 189 QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-195 |
1.11e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 28 IKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILiggkdvttmqpKDRDIAMVFQNYALYPHMTVADNMGFALKIAGT 107
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-----------PELKISYKPQYIKPDYDGTVEDLLRSITDDLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 108 P--KDEIRKRvekaaeiLDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQL 185
Cdd:PRK13409 431 SyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170
....*....|
gi 2525772010 186 GVTTLYVTHD 195
Cdd:PRK13409 504 EATALVVDHD 513
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-212 |
1.37e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM--QPKDRDIAMVF 83
Cdd:PRK10790 343 IDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALyphmtVADNMgFALKIAGTPKDEirKRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGRAIVR 152
Cdd:PRK10790 422 QDPVV-----LADTF-LANVTLGRDISE--EQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 153 EPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlgvTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRG 550
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-196 |
1.84e-15 |
|
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: 72.87 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvttmqpkdrdiamvf 83
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 qnyalyphmtvadnmgfaLKIAgtpkdeirkrvekaaeildlteYLDRkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:cd03221 63 ------------------VKIG----------------------YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|....
gi 2525772010 164 SNLDaklrVQTRTQ-IAALQRQLGvTTLYVTHDQ 196
Cdd:cd03221 99 NHLD----LESIEAlEEALKEYPG-TVILVSHDR 127
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-195 |
2.30e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 75.10 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 29 KDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRilIGGKD-----------------VTTMQPKDRDIAMVFQNYALYPH 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrgselqnyFTKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 mTVADNMGFALKiagtPKDEiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:cd03236 102 -AVKGKVGELLK----KKDE-RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....*..
gi 2525772010 172 VqtrtQIAALQRQL---GVTTLYVTHD 195
Cdd:cd03236 176 L----NAARLIRELaedDNYVLVVEHD 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-204 |
2.39e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGG----KDVTTMQpkdRDIAMVFQNYALYPH 91
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQ---KQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKIAGTPKDeirkrVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|...
gi 2525772010 172 VQTRTQIAALQRQLGVTTLyvTHDQTEALTMGD 204
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLL--TSHQDLPLNKAD 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-168 |
2.43e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 28 IKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN---KGRILIGGKDVTTMQPKDRDiAMVFQNYALYPHMTVADNMGFA--L 102
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQahL 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 103 KI-AGTPKDEIRKRVEKAAEILDLTEYLDRK------PKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:TIGR00955 127 RMpRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-212 |
2.61e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 8 HVTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN--KGRILIGGKDVTTMQPKDRD---IAMV 82
Cdd:PRK13549 10 NITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTEragIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNYALYPHMTVADNMGFALKIagTPK-----DEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVF 157
Cdd:PRK13549 88 HQELALVKELSVLENIFLGNEI--TPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 158 LMDEPLSNLDAKlrvQTRTQIAALQ--RQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK13549 166 ILDEPTASLTES---ETAVLLDIIRdlKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-196 |
2.93e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEevnKGRILIGGKDVTTMQpkdrdiamvfqnyaLYPHMTVADNMGfa 101
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDVPDNQ--------------FGREASLIDAIG-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 102 lkIAGTPKDeirkrvekAAEILDLTEYLD-----RKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRT 176
Cdd:COG2401 108 --RKGDFKD--------AVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|
gi 2525772010 177 QIAALQRQLGVTTLYVTHDQ 196
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-226 |
5.06e-15 |
|
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: 76.91 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvttmqpkdrdIAMVFQNyALYPHMTVA 95
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 96 DNMGFalkiaGTPKDEIRKR--VEKAA-----EIL---DLTEyLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:TIGR00957 717 ENILF-----GKALNEKYYQqvLEACAllpdlEILpsgDRTE-IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 166 LDAKLRVQTRTQIAALQRQL-GVTTLYVTHDQTeALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-168 |
1.52e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 31 GEFLVLVGPSGCGKSTTLRMLAGLEEVN--KGRILIGGKDVTtmQPKDRDIAMVFQNYALYPHMTVADNMGFA--LKIAG 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT--KQILKRTGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 107 T-PKDEIRKRVEKAAEILDLTE-----YLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:PLN03211 172 SlTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-212 |
1.68e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVF--DHVTRIYPGN-DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL-EEVNKGRILIGGKDVTTMQPKD-- 76
Cdd:PRK13549 257 EVILevRNLTAWDPVNpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 -RDIAMVFQN---YALYPHMTVADNMGFAL--KIAGtpkdeiRKRVEKAAEILDLTEYLDR-KPKA---------LSGGQ 140
Cdd:PRK13549 337 aQGIAMVPEDrkrDGIVPVMGVGKNITLAAldRFTG------GSRIDDAAELKTILESIQRlKVKTaspelaiarLSGGN 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 141 RQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-195 |
2.05e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.44 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 29 KDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRIliggkdvtTMQPKDRDIAMVFQNYALYPHMT-VADNmgfALKIA-- 105
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG---EIKVAhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 106 ------------GTPK------DEiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:COG1245 166 pqyvdlipkvfkGTVRellekvDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|.
gi 2525772010 168 aklrVQTRTQIAALQRQL---GVTTLYVTHD 195
Cdd:COG1245 245 ----IYQRLNVARLIRELaeeGKYVLVVEHD 271
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-212 |
2.38e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 9 VTRIYPGndKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDV---TTMQPKDRDIAMVFQN 85
Cdd:PRK10982 4 ISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 YALYPHMTVADNM---GFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:PRK10982 82 LNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 163 LSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
4-194 |
2.48e-14 |
|
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: 74.40 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKpSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIggkdvttmqPKDRDIAMVF 83
Cdd:TIGR00954 452 IKFENIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNyalyPHMTVadnmgfalkiaGTPKDEI---------------RKRVEKAAEILDLTEYLDRK---------PKALSGG 139
Cdd:TIGR00954 522 QR----PYMTL-----------GTLRDQIiypdssedmkrrglsDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 140 QRQRVAMGRAIVREPKVFLMDEPLSnldaKLRVQTRTQIAALQRQLGVTTLYVTH 194
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-208 |
2.62e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.68 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 25 NLDIKDGEFLVLVGPSGCGKSTTLRMlagleevNKGRILIGGKDVTTMQPKD-RDIAMVFQNYALYPHMTVADNMGFAlk 103
Cdd:PTZ00265 1249 NVGMKNVNEFSLTKEGGSGEDSTVFK-------NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG-- 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 104 iagtPKDEIRKRVEKAAEILDLTEYLDRKP-----------KALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRV 172
Cdd:PTZ00265 1320 ----KEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
170 180 190
....*....|....*....|....*....|....*.
gi 2525772010 173 QTRTQIAALQRQLGVTTLYVTHdQTEALTMGDRIAV 208
Cdd:PTZ00265 1396 LIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVV 1430
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-195 |
2.63e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILiggkdvttMQPKDRdIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQKLYLDTTLPLTVNRFLRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 KiAGTPKDEIR---KRVEKAaeildltEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:PRK09544 93 R-PGTKKEDILpalKRVQAG-------HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170
....*....|....*.
gi 2525772010 180 ALQRQLGVTTLYVTHD 195
Cdd:PRK09544 165 QLRRELDCAVLMVSHD 180
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-195 |
2.69e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.05 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 27 DIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRIliggkdvttmqPKDRDIAMVFQnyalYP----HMTVADNMGFAL 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKISYKPQ----YIspdyDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 K--IAGTP-KDEIRKRvekaaeiLDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:COG1245 427 TddFGSSYyKTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|....*.
gi 2525772010 180 ALQRQLGVTTLYVTHD 195
Cdd:COG1245 500 RFAENRGKTAMVVDHD 515
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-214 |
3.01e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDR-DIAMVF-----QNYALYPHMTVA- 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 96 -------DNMGFALKiagtPKDEiRKRVEKAAEILDLT-EYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:PRK15439 361 nvcalthNRRGFWIK----PARE-NAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 168 aklrVQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLGIL 214
Cdd:PRK15439 436 ----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-227 |
9.42e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 70.66 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 19 PSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvttmqpkdrdIAMVFQNYALYPHmTVADNM 98
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 99 gfalkIAGTPKDEIR-KRVEKAAEIL-DLTEYLDRKPKA-------LSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDak 169
Cdd:cd03291 119 -----IFGVSYDEYRyKSVVKACQLEeDITKFPEKDNTVlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD-- 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 170 lrVQTRTQI--AALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYD-RP 227
Cdd:cd03291 192 --VFTEKEIfeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSlRP 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-218 |
9.81e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVN--KGRILIGGKDVTTMQPKDRD---IAMVFQNYALYPHMTV 94
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTEragIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADN--MGFALKIAG--TPKDEIRKRVEKAAEILDLTEYLDRKPKA-LSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:TIGR02633 96 AENifLGNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 170 lRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGilQQVG 218
Cdd:TIGR02633 176 -ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVA 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-220 |
2.18e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.59 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYP 90
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 HmTVADNMgfalkiagTPKDEIRKrvEKAAEILDLTEYLDRkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDakl 170
Cdd:cd03369 96 G-TIRSNL--------DPFDEYSD--EEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASID--- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 171 rVQTRTQIAALQRQL--GVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAP 220
Cdd:cd03369 158 -YATDALIQKTIREEftNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-212 |
2.55e-13 |
|
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: 68.51 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 15 GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD------IAMVFQNYAL 88
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 89 YpHMTVADNMGFalkiaGTPKDEIR-KRVEKAAEI---LDLTEYLDR-----KPKALSGGQRQRVAMGRAIVREPKVFLM 159
Cdd:cd03290 91 L-NATVEENITF-----GSPFNKQRyKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 160 DEPLSNLDAKLRVQTRTQ-IAALQRQLGVTTLYVTHdQTEALTMGDRIAVIKLG 212
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-224 |
5.95e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLR-MLAGLEEVNKGRILIGGKDVTTMQpkdrdIAMVFqnyalypHMTVA 95
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYVPQ-----VSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 96 DNMGFALKIAGtpkdeirKRVEKAAEILDLTEYLDRKPKA-----------LSGGQRQRVAMGRAIVREPKVFLMDEPLS 164
Cdd:PLN03232 697 ENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 165 NLDAKLRVQTRTqiAALQRQL-GVTTLYVThDQTEALTMGDRIAVIKLGILQQVGAPTELY 224
Cdd:PLN03232 770 ALDAHVAHQVFD--SCMKDELkGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-215 |
6.46e-13 |
|
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: 69.85 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 3 EVVFD--HVTRIYPGNDK-PSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL-EEVNKGRILIGGKDVTTMQPKD-- 76
Cdd:TIGR02633 255 DVILEarNLTCWDVINPHrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQai 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 77 -RDIAMVFQN---YALYPHMTVADNmgfaLKIAGTPKDEIRKRVEKAAEILDLTEYLDR-KPKA---------LSGGQRQ 142
Cdd:TIGR02633 335 rAGIAMVPEDrkrHGIVPILGVGKN----ITLSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 143 RVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQ 215
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-194 |
9.17e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGG----KDVTTMQPKDRdIAMVFQNYALYPHmTVADNM 98
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSK-IGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 99 GFAL--------------------------------KIAGTPKDEIRK-------RVEKAAEILDLTEYLDRKPKAL--- 136
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDMSNTtdsneliEMRKNYQTIKDSEVVDVSKKVLihd 560
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 137 --------------------SGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTH 194
Cdd:PTZ00265 561 fvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
1.02e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.19 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 2 AEVVF--DHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIggkdvttmQPkDRDI 79
Cdd:TIGR03719 1 AQYIYtmNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QP-GIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 80 AMVFQNYALYPHMTVADN--MGFALKIA------------GTPKDEIRKRVEKAAEILDLTEY-----LDRK-------- 132
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENveEGVAEIKDaldrfneisakyAEPDADFDKLAAEQAELQEIIDAadawdLDSQleiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 133 --P------KALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKlrvqtrtQIAALQRQL----GvTTLYVTHD 195
Cdd:TIGR03719 151 rcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLqeypG-TVVAVTHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-223 |
1.06e-12 |
|
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: 69.55 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 19 PSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvttmqpkdrdIAMVFQNYALYPHmTVADNM 98
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 99 GFalkiaGTPKDEIRKR-VEKAAEILDLTEYLDRKPK--------ALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDak 169
Cdd:TIGR01271 508 IF-----GLSYDEYRYTsVIKACQLEEDIALFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD-- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 170 lrVQTRTQI--AALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:TIGR01271 581 --VVTEKEIfeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-206 |
1.27e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGgKDVTT---MQPKDRDIA-MVFqNYalyphm 92
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVarlQQDPPRNVEgTVY-DF------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 tVADNM---GFALK--------IAGTPKDEIRKRVEKAAEILD----------LTEYL-------DRKPKALSGGQRQRV 144
Cdd:PRK11147 87 -VAEGIeeqAEYLKryhdishlVETDPSEKNLNELAKLQEQLDhhnlwqlenrINEVLaqlgldpDAALSSLSGGWLRKA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 145 AMGRAIVREPKVFLMDEPLSNLDaklrVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRI 206
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRI 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
1.35e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 19 PSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---RDIAMVFQNY---ALYPHM 92
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 93 TVADNMGF-ALKIAGTPKDEIRKRVEKAA--EILDL----TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSN 165
Cdd:PRK10762 346 SVKENMSLtALRYFSRAGGSLKHADEQQAvsDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2525772010 166 LDaklrVQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK10762 426 VD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-167 |
2.03e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLE--EVNKGRILIGGKDVTTMQPKDR---DIAMVFQnyalYPH 91
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKiagTPKDEIRK-RVEKAAEILDLTEYLDRKPKAL---------------SGGQRQRVAMGRAIVREPK 155
Cdd:PRK09580 89 EIPGVSNQFFLQ---TALNAVRSyRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPE 165
|
170
....*....|..
gi 2525772010 156 VFLMDEPLSNLD 167
Cdd:PRK09580 166 LCILDESDSGLD 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-195 |
2.58e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 1 MAEVVF--DHVTRIYPGnDKPSVDDLNL----DIKDGeflvLVGPSGCGKSTTLRMLAGLEEVNKGR------ILIG--- 65
Cdd:PRK11819 2 MAQYIYtmNRVSKVVPP-KKQILKDISLsffpGAKIG----VLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVGylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 66 -------GKDVT---------TMQPKDR--DIAMvfqNYALYPHMT--VADNMGfAL--KIAGTPKDEIRKRVEKAAEIL 123
Cdd:PRK11819 77 qepqldpEKTVRenveegvaeVKAALDRfnEIYA---AYAEPDADFdaLAAEQG-ELqeIIDAADAWDLDSQLEIAMDAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 124 DLTEYlDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKlrvqtrtQIAALQRQL----GvTTLYVTHD 195
Cdd:PRK11819 153 RCPPW-DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLEQFLhdypG-TVVAVTHD 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-212 |
2.58e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDRD---IAMVFQNYALYPHMTVADN- 97
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLIPQLTIAENi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 -MG--FALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLdaklrvqT 174
Cdd:PRK10762 101 fLGreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL-------T 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 175 RTQIAAL------QRQLGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK10762 174 DTETESLfrvireLKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-231 |
3.94e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 7 DHVTRIYPGNdKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQ 84
Cdd:PLN03232 1239 DVHLRYRPGL-PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 85 NYALYphmtvadnmgfalkiAGTPKDEIRKRVE-------KAAEILDLTEYLDRKPKAL-----------SGGQRQRVAM 146
Cdd:PLN03232 1318 SPVLF---------------SGTVRFNIDPFSEhndadlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 147 GRAIVREPKVFLMDEPLSNLDakLRVQTRTQIAALQRQLGVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTELYDR 226
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVD--VRTDSLIQRTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
....*
gi 2525772010 227 PANVF 231
Cdd:PLN03232 1460 DTSAF 1464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-212 |
4.63e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.88 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILiggkdvttmqpKDRDIAMVFQNyALYPHMTVADNMGFAl 102
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFF- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 103 kiagTPKDEirKRVEKAAEILDL------------TEyLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKL 170
Cdd:PTZ00243 745 ----DEEDA--ARLADAVRVSQLeadlaqlgggleTE-IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 171 --RVQTRTQIAALQrqlGVTTLYVTHdQTEALTMGDRIAVIKLG 212
Cdd:PTZ00243 818 geRVVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDG 857
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
23-171 |
5.29e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.12 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDrdIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 103 KIAGTPKdeirkRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLR 171
Cdd:PRK13541 96 EIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-167 |
1.25e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGgkdvTTMQpkdrdIAMVFQN 85
Cdd:TIGR03719 325 AENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVK-----LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 86 Y-ALYPHMTVADNMGFALKIAGTPKDEIRKRVekaaeildlteYLDR----------KPKALSGGQRQRVAMGRAIVREP 154
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----------YVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|...
gi 2525772010 155 KVFLMDEPLSNLD 167
Cdd:TIGR03719 463 NVLLLDEPTNDLD 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-195 |
1.35e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKdvttmqpkdRDIAMvF 83
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK---------LEVAY-F 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNY--ALYPHMTVADNMGfalkiagTPKDEI----RKRvekaaEILD-LTEYL-----DRKP-KALSGGQRQRVAMGRAI 150
Cdd:PRK11147 388 DQHraELDPEKTVMDNLA-------EGKQEVmvngRPR-----HVLGyLQDFLfhpkrAMTPvKALSGGERNRLLLARLF 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2525772010 151 VREPKVFLMDEPLSNLDaklrVQTRTQIAALQRQLGVTTLYVTHD 195
Cdd:PRK11147 456 LKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-168 |
1.38e-11 |
|
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: 63.03 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 14 PGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEE--VNKGRILIGGKdvttmqPKD----RDIAMVFQNYA 87
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR------PLDknfqRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 88 LYPHMTVADNMGFALKIAGtpkdeirkrvekaaeildlteyldrkpkaLSGGQRQRVAMGRAIVREPKVFLMDEPLSNLD 167
Cdd:cd03232 90 HSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
.
gi 2525772010 168 A 168
Cdd:cd03232 141 S 141
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-195 |
1.44e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 28 IKDGEFLVLVGPSGCGKSTTLRMLAGL---------EEVNKGRIL--------------IGGKDVTTMQ-PKDRD-IAMV 82
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVLkrfrgtelqnyfkkLYNGEIKVVHkPQYVDlIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 83 FQNyalyphmTVADnmgfALKIAgtpkDEiRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:PRK13409 176 FKG-------KVRE----LLKKV----DE-RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 2525772010 163 LSNLDaklrVQTRTQIAALQRQL--GVTTLYVTHD 195
Cdd:PRK13409 240 TSYLD----IRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-167 |
2.35e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLE--EVNKGRILIGGKDVTTMQPKDRD---IAMVFQnyalYP 90
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQ----YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 -HMTVADNMGFaLKIAGTPKDEIRKRVEKAA--------EILDLTE----YLDRK-PKALSGGQRQRVAMGRAIVREPKV 156
Cdd:CHL00131 94 iEIPGVSNADF-LRLAYNSKRKFQGLPELDPlefleiinEKLKLVGmdpsFLSRNvNEGFSGGEKKRNEILQMALLDSEL 172
|
170
....*....|.
gi 2525772010 157 FLMDEPLSNLD 167
Cdd:CHL00131 173 AILDETDSGLD 183
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-209 |
2.49e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.82 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 27 DIKDGEFLVLVGPSGCGKSTTLRMLAGLEEvnkgriliggkdvttmqPKDRDIAmvfqnyalYPHMTVAdnmgfalkiag 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLI-----------------PNGDNDE--------WDGITPV----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 107 tpkdeirkrvekaaeildlteyldRKPK--ALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQ 184
Cdd:cd03222 65 ------------------------YKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 2525772010 185 LGVTTLYVTHDQTEALTMGDRIAVI 209
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-168 |
8.31e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 28 IKDGEFLVLVGPSGCGKSTTLRMLA----GLEEVNKGRILIGGKDVTTMQPKDR-DIAMVFQNYALYPHMTVADNMGFAL 102
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 103 KIAG--------TPKDEIRKRVEKAAEILDLTEYLDRKP-----KALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDA 168
Cdd:TIGR00956 164 RCKTpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-218 |
1.44e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.99 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 15 GNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRIliggkdvttmqPKDRDIAMVFQNYALYPHMTV 94
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 95 ADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 175 RTQIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVG 218
Cdd:PRK13546 183 LDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-146 |
2.94e-10 |
|
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: 61.74 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPS---VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmqPKDRD---- 78
Cdd:COG4615 330 LRGVTYRYPGEDGDEgftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREayrq 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2525772010 79 -IAMVFQNYALYPHMtvadnmgfaLKIAGTPKDeirkrvEKAAEILDLTEyLDRKPK---------ALSGGQRQRVAM 146
Cdd:COG4615 407 lFSAVFSDFHLFDRL---------LGLDGEADP------ARARELLERLE-LDHKVSvedgrfsttDLSQGQRKRLAL 468
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-230 |
4.15e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 21 VDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAG--LEEVNKGRILIGGKDVTTMQPKDR-DIAMVFQNYALYPHmtvADN 97
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRLARLRAVLPQ---AAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 MGFALKI--------------AGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAI---------VREP 154
Cdd:PRK13547 94 PAFAFSAreivllgrypharrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2525772010 155 KVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYdRPANV 230
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAHI 248
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-227 |
4.28e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 20 SVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEE----VNKGRILIGGKDVTTMQPKDR------DIAMVFQ--NYA 87
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQepQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 88 LYPhmtvADNMGFALK--IAG-TPKDEIRKRV----EKAAEILDLTEYLDRK------PKALSGGQRQRVAMGRAIVREP 154
Cdd:PRK15093 102 LDP----SERVGRQLMqnIPGwTYKGRWWQRFgwrkRRAIELLHRVGIKDHKdamrsfPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 155 KVFLMDEPLSNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTELYDRP 227
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-212 |
5.00e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 25 NLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD---RDIAMVFQNY---ALYPHMTVADNM 98
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 99 GFALKIAGTPKDEI--RKRVEKAAE--ILDL---TEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDaklr 171
Cdd:PRK11288 353 NISARRHHLRAGCLinNRWEAENADrfIRSLnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID---- 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2525772010 172 VQTRTQIAALQRQL---GVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK11288 429 VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-212 |
6.02e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 28 IKDGEFLVLVGPSGCGKSTTLRMLAglEEVNKGrILIGGKDVTTMQPKD----RDIAMVFQNYALYPHMTVADNMGFALK 103
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 104 I---AGTPKDEIRKRVEKAAEILDLTEYLDrkpkALSG--------GQRQRVAMGRAIVREPKVFL-MDEPLSNLDAklr 171
Cdd:TIGR00956 863 LrqpKSVSKSEKMEYVEEVIKLLEMESYAD----AVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS--- 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2525772010 172 vQTRTQIAALQRQL---GVTTLYVTHdQTEALTMG--DRIAVIKLG 212
Cdd:TIGR00956 936 -QTAWSICKLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-162 |
6.97e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTtmQPKDRD-----IAMVFQ----NyaLYPHM 92
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRavcprIAYMPQglgkN--LYPTL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 93 TVADNMGFALKIAGTPKDEIRKRVekaAEILD---LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEP 162
Cdd:NF033858 94 SVFENLDFFGRLFGQDAAERRRRI---DELLRatgLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-223 |
1.12e-09 |
|
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: 60.34 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYphmtvADNMGF 100
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF-----SGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 101 ALKIAGTPKDEirkRVEKAAEILDLTEYLDRKP-----------KALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:TIGR00957 1379 NLDPFSQYSDE---EVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 170 ----LRVQTRTQIAAlqrqlgVTTLYVTHDQTealTMGD--RIAVIKLGILQQVGAPTEL 223
Cdd:TIGR00957 1456 tdnlIQSTIRTQFED------CTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-195 |
7.79e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 17 DKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRI------LIG----------GKDVTTM-------Q 73
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGyyaqdhaydfENDLTLFdwmsqwrQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 74 PKDRDIA-------MVFQNyalyphmtvadnmgfalkiagtpkDEIRKRVekaaeildlteyldrkpKALSGGQRQRVAM 146
Cdd:PRK15064 411 EGDDEQAvrgtlgrLLFSQ------------------------DDIKKSV-----------------KVLSGGEKGRMLF 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 147 GRAIVREPKVFLMDEPLSNLDAKlrvqtrtQIAALQRQLGV---TTLYVTHD 195
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDME-------SIESLNMALEKyegTLIFVSHD 494
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-231 |
1.20e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 55.30 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTM--QPKDRDIAMVFQNYALYp 90
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILF- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 91 hmtvADNMGFALKIAGTPKDEirkRVEKAAEILDLTEYLDRKPKAL-----------SGGQRQRVAMGRAIVREPKVFLM 159
Cdd:cd03288 108 ----SGSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2525772010 160 DEPLSNLD-AKLRVQTRTQIAALQRQLGVTTLYVTHDQTEAltmgDRIAVIKLGILQQVGAPTELYDRPANVF 231
Cdd:cd03288 181 DEATASIDmATENILQKVVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-231 |
1.25e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 28 IKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVFQNYALYPHmTVADNMG-F---- 100
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVDpFleas 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 101 ------ALKIAGtpkdeIRKRVEKAAEILDlteyldrkPKALSG------GQRQRVAMGRAIVREPKVF-LMDEPLSNLD 167
Cdd:PTZ00243 1412 saevwaALELVG-----LRERVASESEGID--------SRVLEGgsnysvGQRQLMCMARALLKKGSGFiLMDEATANID 1478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2525772010 168 AKLRVQTR-TQIAALQRQLGVTTLYVTHdqteALTMGDRIAVIKLGILQQVGAPTELYDRPANVF 231
Cdd:PTZ00243 1479 PALDRQIQaTVMSAFSAYTVITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
109-223 |
1.50e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 109 KDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVT 188
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100 110
....*....|....*....|....*....|....*
gi 2525772010 189 TLYVTHDQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-199 |
2.01e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 16 NDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAG--LEEVNKGRILIG---GKDVTTMQPKdRDIAMVFQNYAL-Y 89
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhPQGYSNDLTLFGrrrGSGETIWDIK-KHIGYVSSSLHLdY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNM---GF--ALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKP-KALSGGQRQRVAMGRAIVREPKVFLMDEPL 163
Cdd:PRK10938 350 RVSTSVRNVilsGFfdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPL 429
|
170 180 190
....*....|....*....|....*....|....*.
gi 2525772010 164 SNLDAKLRVQTRTQIAALQRQLGVTTLYVTHDQTEA 199
Cdd:PRK10938 430 QGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
237-286 |
6.27e-08 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 48.73 E-value: 6.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2525772010 237 GSPSMN-INTHPVINGQAKIGDD-TIDLPREAVAKLTAEDNGQIIVGFRPED 286
Cdd:pfam17912 1 GSPPMNfLPATVVEDGLLVLGGGvTLPLPEGQVLALKLYVGKEVILGIRPEH 52
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-167 |
1.40e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYpgNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGgkdvTTMQpkdrdIAMVF 83
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----ETVK-----LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNY-ALYPHMTVADNMGFALKIAGTPKDEIRKRVekaaeildlteYLDR----------KPKALSGGQRQRVAMGRAIVR 152
Cdd:PRK11819 394 QSRdALDPNKTVWEEISGGLDIIKVGNREIPSRA-----------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQ 462
|
170
....*....|....*
gi 2525772010 153 EPKVFLMDEPLSNLD 167
Cdd:PRK11819 463 GGNVLLLDEPTNDLD 477
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-223 |
1.84e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 6 FDHVTRIYPGNDKPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKD--RDIAMVF 83
Cdd:PLN03130 1240 FEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 84 QNYALYphmtvADNMGFALKIAGTPKD-EIRKRVEKAaeilDLTEYLDRKPKAL-----------SGGQRQRVAMGRAIV 151
Cdd:PLN03130 1320 QAPVLF-----SGTVRFNLDPFNEHNDaDLWESLERA----HLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2525772010 152 REPKVFLMDEplsnldAKLRVQTRTQiAALQRQL-----GVTTLYVTHdQTEALTMGDRIAVIKLGILQQVGAPTEL 223
Cdd:PLN03130 1391 RRSKILVLDE------ATAAVDVRTD-ALIQKTIreefkSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-194 |
2.59e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 4 VVFDHVTRIYPGNDKPS--VDDLNLDIKDGEF----------------LVLVGPSGCGKSTTLRMLAGLEEVNKGRILIG 65
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFdkLKDLFFRSKDGEYhyalnnisfevpegeiVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 66 GKdvttmqpkdrdIAMVFQNYALYPHMTVADNMGFALKIAGTPKDEIRKRVEKAAEILDLTEYLDRKPKALSGGQRQRVA 145
Cdd:PRK13545 85 GS-----------AALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 146 MGRAIVREPKVFLMDEPLSNLDAKLRVQTRTQIAALQRQlGVTTLYVTH 194
Cdd:PRK13545 154 FAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISH 201
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-196 |
2.93e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 13 YPGNdkPSV-DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILiggkdvttMQPKDRdIAMVFQNYALYPH 91
Cdd:PLN03073 518 YPGG--PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR-MAVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMGFALKIAGTPKDEIRKRVEKaaeiLDLTEYLDRKPK-ALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKl 170
Cdd:PLN03073 587 LSSNPLLYMMRCFPGVPEQKLRAHLGS----FGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD- 661
|
170 180
....*....|....*....|....*.
gi 2525772010 171 RVQTRTQIAALqRQLGVttLYVTHDQ 196
Cdd:PLN03073 662 AVEALIQGLVL-FQGGV--LMVSHDE 684
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-208 |
4.84e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 31 GEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIggkdvttmqpkdrdiamvfqnyalyphmtvadnmgfalkIAGTpkd 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDGE--- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 111 eirkRVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK-----LRVQTRTQIAALQRQL 185
Cdd:smart00382 40 ----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLKSEK 115
|
170 180
....*....|....*....|...
gi 2525772010 186 GVTTLYVTHDQTEALTMGDRIAV 208
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-185 |
5.22e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 25 NLDIKDGEFLVLVGPSGCGKSTTLRMLAGleEVnkgrILIGGKDVTTMQPKDR--------DIAMVFQNyaLYPHMTVAD 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG--EL----PLLSGERQSQFSHITRlsfeqlqkLVSDEWQR--NNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 97 NMGFALKIAGTPKDEIRK--RVEKAAEILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDaklrVQT 174
Cdd:PRK10938 95 EDDTGRTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD----VAS 170
|
170
....*....|.
gi 2525772010 175 RTQIAALQRQL 185
Cdd:PRK10938 171 RQQLAELLASL 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-167 |
7.56e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 36 LVGPSGCGKSTTLRMLA--GLEEVNKG-RIL-----IGGKDVTTMQ-PKDRDI---------AMVFQNYALYPHMTVADN 97
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAmhAIDGIPKNcQILhveqeVVGDDTTALQcVLNTDIertqlleeeAQLVAQQRELEFETETGK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 MGFALKiAGTPKD-------EIRKRVE---------KAAEILD----LTEYLDRKPKALSGGQRQRVAMGRAIVREPKVF 157
Cdd:PLN03073 288 GKGANK-DGVDKDavsqrleEIYKRLElidaytaeaRAASILAglsfTPEMQVKATKTFSGGWRMRIALARALFIEPDLL 366
|
170
....*....|
gi 2525772010 158 LMDEPLSNLD 167
Cdd:PLN03073 367 LLDEPTNHLD 376
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-212 |
2.69e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 22 DDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGL------EevnkGRILIGGKdvtTMQPKD-RD-----IAMVFQNYALY 89
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGE---VCRFKDiRDsealgIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 90 PHMTVADNM--GfalkiagtpkDEIRKR--------VEKAAEILD---LTEYLDRKPKALSGGQRQRVAMGRAIVREPKV 156
Cdd:NF040905 91 PYLSIAENIflG----------NERAKRgvidwnetNRRARELLAkvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2525772010 157 FLMDEPLSNL-----DAKLRVqtrtqIAALQRQlGVTTLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:NF040905 161 LILDEPTAALneedsAALLDL-----LLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-212 |
6.08e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 18 KPSVDDLNLDIKDGEFLVLVGPSGCGKSTTLRMLAGLEEVNKGRILIGGKDVTTMQPKDrdiamvfqnyalyphmtvADN 97
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE------------------AIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 98 MGFALKIAGTPKDEIRKR--VEKAAEILDLTEYL-------DRKPK----------------------ALSGGQRQRVAM 146
Cdd:PRK10982 323 HGFALVTEERRSTGIYAYldIGFNSLISNIRNYKnkvglldNSRMKsdtqwvidsmrvktpghrtqigSLSGGNQQKVII 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2525772010 147 GRAIVREPKVFLMDEPLSNLD--AKLRV-QTRTQIAalQRQLGVttLYVTHDQTEALTMGDRIAVIKLG 212
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDvgAKFEIyQLIAELA--KKDKGI--IIISSEMPELLGITDRILVMSNG 467
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-169 |
7.49e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 31 GEFLVLVGPSGCGKSTTLRMLAGLEEVN--KGRILIGGKdvttmqPKDRDI-----AMVFQNYALYPHMTVADNMGFA-- 101
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGF------PKKQETfarisGYCEQNDIHSPQVTVRESLIYSaf 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2525772010 102 LKIAG-TPKDEIRKRVEKAAEILDLTEYLDR-----KPKALSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAK 169
Cdd:PLN03140 980 LRLPKeVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-197 |
2.53e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKSTTLrmLAGLEEVNKGRILIGGKdvttmqpkdrdiamvfqnyALYPHMTVA-DNMGFA 101
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISFLP-------------------KFSRNKLIFiDQLQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 102 LKIAgtpkdeirkrvekaaeILDLTeyLDRKPKALSGGQRQRVAMGRAIVREPK--VFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:cd03238 72 IDVG----------------LGYLT--LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170
....*....|....*...
gi 2525772010 180 ALqRQLGVTTLYVTHDQT 197
Cdd:cd03238 134 GL-IDLGNTVILIEHNLD 150
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
33-64 |
1.10e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|...
gi 2525772010 33 FLVLVGPSGCGKSTTLRML-AGLEEVNKGRILI 64
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFV 39
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
248-286 |
2.27e-03 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 35.50 E-value: 2.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2525772010 248 VINGQAKIGDDTIDLPREAVAkltaeDNGQIIVGFRPED 286
Cdd:pfam17850 7 VEDGRVRIGGLALPLPELAGA-----EGSEVVAYVRPHD 40
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
28-64 |
6.80e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 6.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2525772010 28 IKDGE-FLVLVGPSGCGKSTTLRMLagLEEVNKGRILI 64
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRL--LERLPDDVKVA 74
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-206 |
8.30e-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: 37.24 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 23 DLNLDIKDGEFLVLVGPSGCGKST----TL------RMLAGLEEVNKGRI-LIGGKDVTTMQPKDRDIAMVFQNYALYPH 91
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSlafdTIyaegqrRYVESLSAYARQFLgQMDKPDVDSIEGLSPAIAIDQKTTSRNPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2525772010 92 MTVADNMG----FALKIAgtpKDEIRKRVEKAAEI-LD-LTeyLDRKPKALSGGQRQRVAMGRAI------VrepkVFLM 159
Cdd:cd03270 93 STVGTVTEiydyLRLLFA---RVGIRERLGFLVDVgLGyLT--LSRSAPTLSGGEAQRIRLATQIgsgltgV----LYVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2525772010 160 DEPLSNLDAKlrvQTRTQIAALQ--RQLGVTTLYVTHDQtEALTMGDRI 206
Cdd:cd03270 164 DEPSIGLHPR---DNDRLIETLKrlRDLGNTVLVVEHDE-DTIRAADHV 208
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
19-48 |
8.34e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 37.76 E-value: 8.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2525772010 19 PSVDDLNL--------DIKDGefLVLV-GPSGCGKSTTL 48
Cdd:COG2805 106 PTLEELGLppvlkelaELPRG--LVLVtGPTGSGKSTTL 142
|
|
| |
