|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-357 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 570.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 241 FLTADiVEPGEVTTKvqihrGQAIVVSAnTIGAKVGDPCVVGIRPEHIRFGEKDaiqEGGV--TLSVVEQLGNECLMYFN 318
Cdd:COG3839 241 LLPGT-VEGGGVRLG-----GVRLPLPA-ALAAAAGGEVTLGIRPEHLRLADEG---DGGLeaTVEVVEPLGSETLVHVR 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 491647138 319 TPqsAEPVVIRTEGQTNIRAGDKRCIEFPADYCHLFDRD 357
Cdd:COG3839 311 LG--GQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-363 |
0e+00 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 553.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 241 FLTADIVEPGEVTTKVQIHRGQAIVVSANTIGAKVGDPCVVGIRPEHIRFGEK-DAIQEGgvTLSVVEQLGNECLMYFNT 319
Cdd:PRK11000 241 FLPVKVTATAIEQVQVELPNRQQVWLPVEGRGVQVGANMSLGIRPEHLLPSDIaDVTLEG--EVQVVEQLGNETQIHIQI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 491647138 320 PQSAEPVVIRTEGQTNIRAGDKRCIEFPADYCHLFDRDGKAFKR 363
Cdd:PRK11000 319 PAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRR 362
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-359 |
3.86e-174 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 488.58 E-value: 3.86e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTF-GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 240 NFLTADIVEPGevtTKVQIHRGQAIVVSANTiGAKVGDPCVVGIRPEHIRfgekDAIQEGGVTLSV--VEQLGNECLMYf 317
Cdd:PRK11650 241 NLLDGRVSADG---AAFELAGGIALPLGGGY-RQYAGRKLTLGIRPEHIA----LSSAEGGVPLTVdtVELLGADNLAH- 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 491647138 318 nTPQSAEPVVIRTEGQTNIRAGDKRCIEFPADYCHLFDRDGK 359
Cdd:PRK11650 312 -GRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTG 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-356 |
2.93e-151 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 430.67 E-value: 2.93e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGspKMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 241 FLTADIVEPGEVTTKVQihrGQAIVVSANTiGAKVGDPCVVGIRPEHIRFGEKDAIQEGGVTLSVVEQLGNECLMYFNTP 320
Cdd:COG3842 241 LLPGTVLGDEGGGVRTG---GRTLEVPADA-GLAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 491647138 321 QSAEPVVIRTEGQT-NIRAGDKRCIEFPADYCHLFDR 356
Cdd:COG3842 317 DGQELVVRVPNRAAlPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
8.37e-133 |
|
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: 378.52 E-value: 8.37e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491647138 164 LDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
5.86e-114 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 331.51 E-value: 5.86e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 164 LDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-290 |
1.58e-109 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 324.41 E-value: 1.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN-DLPPPERGIGMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 QSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSpkMNF 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC--VNV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491647138 242 LTADIVEPgevttkvQIHRGQaivVSANTIGAKVGDPCVVGIRPEHIRF 290
Cdd:COG1118 240 LRGRVIGG-------QLEADG---LTLPVAEPLPDGPAVAGVRPHDIEV 278
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
1.80e-109 |
|
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: 319.08 E-value: 1.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491647138 164 LDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-354 |
1.11e-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: 317.36 E-value: 1.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALYP 88
Cdd:TIGR03265 10 IRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 89 HMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:TIGR03265 90 NLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSpkMNFLTADIVE 248
Cdd:TIGR03265 170 REHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--VNWLPGTRGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 249 PGEVttkvqihRGQAIVVSANTIGAKVGDPCVVGIRPEHIRFGEKDAiQEGGVTLSV--VEQLGNECLMYFNTP----QS 322
Cdd:TIGR03265 248 GSRA-------RVGGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGN-AANLLLARVedMEFLGAFYRLRLRLEglpgQA 319
|
330 340 350
....*....|....*....|....*....|...
gi 491647138 323 AEPVVIRTEGQ-TNIRAGDKRCIEFPADYCHLF 354
Cdd:TIGR03265 320 LVADVSASEVErLGIRAGQPIWIELPAERLRAF 352
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-318 |
3.21e-106 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 316.89 E-value: 3.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYA 85
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK09452 97 LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGspKMNFLTAD 245
Cdd:PRK09452 177 YKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFDAT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 246 IVEP-GEVTTKVQIhRGQAIVVSANtIGAKVGDPCVVGIRPEHIRFGEKDAIQEG-------------GVTL-SVVEQLG 310
Cdd:PRK09452 255 VIERlDEQRVRANV-EGRECNIYVN-FAVEPGQKLHVLLRPEDLRVEEINDDEHAegligyvrernykGMTLdSVVELEN 332
|
330
....*....|.
gi 491647138 311 NECLM---YFN 318
Cdd:PRK09452 333 GKMVMvseFFN 343
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-300 |
3.77e-97 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 293.06 E-value: 3.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 2 AEVILNKVNKTFGK----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND-----LPP 72
Cdd:NF040933 1 VTVRVENVTKIFKKgkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 73 PERGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 153 KVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 233 FIGspKMNFLTADIVEPGEVTTKvqihrGQAIVVSANTIGAkvgDPCVVGIRPEHIRFGEKDAIQEGG 300
Cdd:NF040933 241 LIG--DINLLEGKVEEEGLVDGN-----DLKIPLPNPKLEA---GEVIIGIRPEDIDISESDMRLPPG 298
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-236 |
1.84e-94 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 281.92 E-value: 1.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNkVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMV 80
Cdd:cd03296 1 MSIEVRN-VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAK----TVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGS 236
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-294 |
2.78e-93 |
|
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: 282.07 E-value: 2.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 35 VGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 115 REVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 195 VEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKM-NFLTADIVEPGEVTTKVQIHRgQAIVVSANTIGA 273
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVfEATVIERKSEQVVLAGVEGRR-CDIYTDVPVEKD 240
|
250 260
....*....|....*....|.
gi 491647138 274 KvgdPCVVGIRPEHIRFGEKD 294
Cdd:TIGR01187 241 Q---PLHVVLRPEKIVIEEED 258
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-292 |
6.55e-89 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 271.98 E-value: 6.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 164 LDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKMnF-- 241
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANI-Fpa 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 242 -LTADIVEPGEvttkVQIHRGQAIVVSANTigakvGDpCVVGIRPEHIRFGE 292
Cdd:PRK11432 246 tLSGDYVDIYG----YRLPRPAAFAFNLPD-----GE-CTVGVRPEAITLSE 287
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
1.47e-88 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 267.05 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 164 LDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
1.11e-84 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 257.71 E-value: 1.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTF----GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPPPERG 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDA--GRV 212
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-288 |
3.22e-84 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 259.62 E-value: 3.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALYPHMTVYDNMAFG 99
Cdd:NF040840 17 RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARL 179
Cdd:NF040840 97 LKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 180 HERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKMNFLTADIVEPGEVttkvqIH 259
Cdd:NF040840 177 HREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGGEGTI-----LD 251
|
250 260
....*....|....*....|....*....
gi 491647138 260 RGQAIVVSAntiGAKVGDPCvVGIRPEHI 288
Cdd:NF040840 252 TGNIKIELP---EEKKGKVR-IGIRPEDI 276
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-235 |
9.29e-84 |
|
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: 254.57 E-value: 9.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALYPHMTVYDNMAFG 99
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARL 179
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 180 HERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIG 235
Cdd:cd03299 176 RKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-253 |
2.55e-81 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 250.78 E-value: 2.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVT-KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQ 82
Cdd:COG1125 4 FENVTKRYPDGTVAvDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLD--TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGS---- 236
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAdrgl 243
|
250
....*....|....*...
gi 491647138 237 PKMNFLTA-DIVEPGEVT 253
Cdd:COG1125 244 RRLSLLRVeDLMLPEPPT 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-293 |
1.92e-80 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 250.91 E-value: 1.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALYPHM 90
Cdd:PRK11607 27 KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFGLK---LAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:PRK11607 107 TVEQNIAFGLKqdkLPKAE---IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 168 LRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSpkMNFLTADIV 247
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEGVLK 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 491647138 248 EPGEVTTKVQiHRGQAIVVSANTiGAKVGD--PCVVGIRPEHIRFGEK 293
Cdd:PRK11607 262 ERQEDGLVID-SPGLVHPLKVDA-DASVVDnvPVHVALRPEKIMLCEE 307
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-246 |
2.02e-80 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 250.39 E-value: 2.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYA 85
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKL----AKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGspKMNF 241
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--EVNR 242
|
....*
gi 491647138 242 LTADI 246
Cdd:PRK10851 243 LQGTI 247
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
1.07e-78 |
|
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: 241.22 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFG----KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndLPPPERGIGM 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---VTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDA--GRV 212
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-238 |
3.04e-77 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 238.35 E-value: 3.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVH-VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQ 82
Cdd:cd03295 3 FENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLD--TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:cd03295 83 QIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPK 238
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
7.35e-76 |
|
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: 232.46 E-value: 7.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDL----PPPERGIGM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFGlklakaeaktvdekvrevaaalqldtllarkpkaLSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-216 |
2.20e-71 |
|
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: 222.17 E-value: 2.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINkGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND------LPPPERGIGMVFQSYALYPHMTVYD 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 NMAFGLKLAKAEAKTVdeKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRM 174
Cdd:cd03297 95 NLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491647138 175 EIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-235 |
1.24e-69 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 218.09 E-value: 1.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 5 ILNKVNKTFGkvHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSY 84
Cdd:COG3840 3 RLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFG----LKLAKAEAKtvdeKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG3840 81 NLFPHLTVAQNIGLGlrpgLKLTAEQRA----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIG 235
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
6.85e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 216.06 E-value: 6.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVI-LNKVNKTFG----KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER 75
Cdd:COG1136 1 MSPLLeLRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 76 G------IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQvEAMTLATKIVVLDAGRVE 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-288 |
9.67e-69 |
|
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: 220.36 E-value: 9.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDF--------------VVFvGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND------LPPPERGIGMV 80
Cdd:COG4148 4 EVDFRLRRGGFtldvdftlpgrgvtALF-GPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDekVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG4148 83 FQEARLFPHLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGfiGSPKMN 240
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 491647138 241 FLTADIVEPGEV--TTKVQIHrGQAIVVSAntIGAKVGDPCVVGIRPEHI 288
Cdd:COG4148 239 VLEATVAAHDPDygLTRLALG-GGRLWVPR--LDLPPGTRVRVRIRARDV 285
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
5.95e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.78 E-value: 5.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPPPE-------RG 76
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGE---DLTDSKkdinklrRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 IGMVFQSYALYPHMTVYDNMAFG----LKLAKAEAktvdekvREVAAALqLDT--LLARK---PKALSGGQRQRVAIGRA 147
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLApikvKKMSKAEA-------EERAMEL-LERvgLADKAdayPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 148 IVREPKVFLFDEPLSNLDAS-----LRVqMRmEIArlheRLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELY 222
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPElvgevLDV-MR-DLA----KEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
....*
gi 491647138 223 NHPAN 227
Cdd:COG1126 225 ENPQH 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-212 |
3.58e-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: 208.88 E-value: 3.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFG----KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG----- 76
Cdd:cd03255 3 LKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 -IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:cd03255 83 hIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 156 LFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMtLATKIVVLDAGRV 212
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-234 |
1.78e-64 |
|
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: 206.34 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 7 NKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE------RGIGMV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 161 LSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFI 234
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-234 |
1.51e-63 |
|
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: 202.90 E-value: 1.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGMVFQS 83
Cdd:COG1127 11 LTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGL----KLAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:COG1127 91 GALFDSLTVFENVAFPLrehtDLSEAE---IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 160 PLSNLD-ASLRVQMRMeIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPaNTFVAGFI 234
Cdd:COG1127 168 PTAGLDpITSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-227 |
1.26e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 200.70 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 8 KVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGI----GMVFQS 83
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFG----LKLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:PRK09493 86 FYLFPHLTALENVMFGplrvRGASKEEAE---KQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 160 PLSNLDASLrvqmRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPAN 227
Cdd:PRK09493 163 PTSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-221 |
1.53e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 197.59 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMVFQSY 84
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:COG1131 83 ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 165 DASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:COG1131 163 DPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-225 |
2.60e-61 |
|
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: 196.78 E-value: 2.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQsyalYP--- 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ----NPddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 89 --HMTVYDNMAFGLK---LAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:COG1122 88 lfAPTVEEDVAFGPEnlgLPREE---IRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 164 LDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:COG1122 165 LDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-211 |
2.55e-59 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 191.14 E-value: 2.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IGMVFQsyalYP-HM----TV 92
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQ----NPdDQffgpTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQM 172
Cdd:cd03225 94 EEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRREL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 491647138 173 RMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:cd03225 174 LELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-212 |
3.22e-59 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.03 E-value: 3.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVH-VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGM 79
Cdd:COG2884 4 FENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 160 PLSNLDAslrvQMRMEIARLHERL---GATMIYVTHDQ--VEAMtlATKIVVLDAGRV 212
Cdd:COG2884 164 PTGNLDP----ETSWEIMELLEEInrrGTTVLIATHDLelVDRM--PKRVLELEDGRL 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
2.38e-58 |
|
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: 189.25 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGMV 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGL----KLAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLrehtRLSEEE---IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 157 FDEPLSNLD-ASLRVQMRMeIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPaNTFVAGF 233
Cdd:cd03261 160 YDEPTAGLDpIASGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
2.91e-58 |
|
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: 197.43 E-value: 2.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVIL--NKVNKTF-----GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP 73
Cdd:COG1123 256 AAEPLLevRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 74 E-----RGIGMVFQ--SYALYPHMTVYDNMAFGLKLAK-AEAKTVDEKVREVAAALQLDT-LLARKPKALSGGQRQRVAI 144
Cdd:COG1123 336 SlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 145 GRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHD--QVEAMtlATKIVVLDAGRVEQVGSPLELY 222
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVF 493
|
...
gi 491647138 223 NHP 225
Cdd:COG1123 494 ANP 496
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-212 |
3.21e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 188.10 E-value: 3.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPhMTVYDNMAFG 99
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQEPALWG-GTVRDNLPFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKtvDEKVREVAAALQLDT-LLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIAR 178
Cdd:COG4619 98 FQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLRE 175
|
170 180 190
....*....|....*....|....*....|....
gi 491647138 179 LHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG4619 176 YLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
3.37e-58 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 189.24 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGK----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPPPERG--- 76
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKafr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 --IGMVFQSY--ALYPHMTVYDNMAFGLKLAKAeaKTVDEKVREVAAALQLD-TLLARKPKALSGGQRQRVAIGRAIVRE 151
Cdd:COG1124 79 rrVQMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 152 PKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDqVEAMT-LATKIVVLDAGRVEQVGSPLELYNHPAN 227
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-278 |
1.03e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.06 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTF----GKVHVTKEVDLHINKGDfvVF--VGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE----- 74
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 RGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVaaaLQLDTLLARK---PKALSGGQRQRVAIGRAIVRE 151
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAEL---LELVGLSDKAdayPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 152 PKVFLFDEPLSNLDAS-----LRVqmrmeIARLHERLGATMIYVTHDqveaM----TLATKIVVLDAGRVEQVGSPLELY 222
Cdd:COG1135 159 PKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVF 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 223 NHPANTFVAGFIGSpkmnflTADIVEPGEVTTKVQIHRGQAIVVSANTIGAKVGDP 278
Cdd:COG1135 230 ANPQSELTRRFLPT------VLNDELPEELLARLREAAGGGRLVRLTFVGESADEP 279
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
3.36e-57 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 185.81 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN----DLPPPERGIGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFGL----KLAKAEAktvDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPikvkGMSKAEA---EERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 156 LFDEPLSNLDAslrvQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03262 158 LFDEPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
2.21e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 185.07 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGK----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDlPPPERG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 IgmVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDA--GRV 212
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRI 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
3.52e-56 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 183.55 E-value: 3.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFG----KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE----- 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 RGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 155 FLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHdQVEAM-TLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-214 |
1.61e-55 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 181.94 E-value: 1.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTF----GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG-----IGM 79
Cdd:cd03257 7 LSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSY--ALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQL---DTLLARKPKALSGGQRQRVAIGRAIVREPKV 154
Cdd:cd03257 87 VFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 155 FLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGR-VEQ 214
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-212 |
1.17e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.25 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTF-GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGM 79
Cdd:COG3638 5 LRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFG----LKLAKAEAKTVDEKVREVAAALqLDTL-----LARKPKALSGGQRQRVAIGRAIVR 150
Cdd:COG3638 85 IFQQFNLVPRLSVLTNVLAGrlgrTSTWRSLLGLFPPEDRERALEA-LERVgladkAYQRADQLSGGQQQRVAIARALVQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 151 EPKVFLFDEPLSNLD--ASLRVqmrME-IARLHERLGATMIYVTHdQVE-AMTLATKIVVLDAGRV 212
Cdd:COG3638 164 EPKLILADEPVASLDpkTARQV---MDlLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
6-216 |
1.91e-53 |
|
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: 176.21 E-value: 1.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVnkTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYA 85
Cdd:TIGR01277 3 LDKV--RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:TIGR01277 81 LFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-226 |
1.12e-52 |
|
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: 178.38 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 36 GPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND------LPPPERGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKT 109
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKRARPSERR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 110 VDEKvrEVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIY 189
Cdd:TIGR02142 110 ISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILY 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 491647138 190 VTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:TIGR02142 188 VSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-226 |
2.53e-52 |
|
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: 181.64 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDIT---SGDLKIDGKVCNDLPPPERG--IGMVFQS--YAL 86
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQDpmTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 87 YPhMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA 166
Cdd:COG1123 97 NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 167 SLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:COG1123 176 TTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-212 |
3.76e-52 |
|
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: 172.68 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGkvHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQS 83
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFG----LKLAKAEaktvDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:cd03298 79 NNLFAHLTVEQNVGLGlspgLKLTAED----RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-218 |
8.49e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 171.98 E-value: 8.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDI-----TSGDLKIDGK-VCNDLPPPE---RGIGM 79
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKdIYDLDVDVLelrRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPhMTVYDNMAFGLKLA-KAEAKTVDEKVREVAAALQLDTLLARKPKA--LSGGQRQRVAIGRAIVREPKVFL 156
Cdd:cd03260 86 VFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 157 FDEPLSNLDASLRvqMRME--IARLHERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:cd03260 165 LDEPTSALDPIST--AKIEelIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-237 |
2.55e-51 |
|
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: 171.77 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IGMVFQS 83
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFG----LKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:COG1120 84 PPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 160 PLSNLDasLRVQMR-ME-IARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLE---------LYNHPANT 228
Cdd:COG1120 164 PTSHLD--LAHQLEvLElLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelleeVYGVEARV 241
|
....*....
gi 491647138 229 FVAGFIGSP 237
Cdd:COG1120 242 IEDPVTGRP 250
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-221 |
2.07e-50 |
|
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: 169.27 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMVFQSY 84
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 165 DASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:COG4555 164 DVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
17-223 |
2.40e-50 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 168.61 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALYPHMTVYDNM 96
Cdd:PRK10771 13 HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 AFG----LKLAKAEAKTVDEKVREVAaalqLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQM 172
Cdd:PRK10771 93 GLGlnpgLKLNAAQREKLHAIARQMG----IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 173 RMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
2.69e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 169.47 E-value: 2.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLkIDGKVcnDLPPPERGIGMVFQS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA--PLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLA-KAEAktvdekvREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQwRDAA-------LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 163 NLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-224 |
3.95e-50 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 168.13 E-value: 3.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFG-KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGM 79
Cdd:cd03256 3 VENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFGlKLA-----KAEAKTVDEKVREVAAAL----QLDTLLARKPKALSGGQRQRVAIGRAIVR 150
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSG-RLGrrstwRSLFGLFPKEEKQRALAAlervGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 151 EPKVFLFDEPLSNLD-ASLRVQMRMeIARLHERLGATMIYVTHdQVE-AMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:cd03256 162 QPKLILADEPVASLDpASSRQVMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-209 |
4.87e-50 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 166.89 E-value: 4.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAG-LEDI--TSGDLKIDGKVCNDLPPPERGIGMVFQSYALYPHMTVYDNM 96
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 AFGL--KLAKAEAKTvdekvrEVAAALQ---LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQ 171
Cdd:COG4136 98 AFALppTIGRAQRRA------RVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 491647138 172 MRMEI-ARLHERlGATMIYVTHDqVEAMTLATKIVVLDA 209
Cdd:COG4136 172 FREFVfEQIRQR-GIPALLVTHD-EEDAPAAGRVLDLGN 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-211 |
8.36e-50 |
|
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: 166.65 E-value: 8.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEviLNKVNKTF-GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE----- 74
Cdd:TIGR02673 1 MIE--FHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 RGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKV 154
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 155 FLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-225 |
2.56e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 167.24 E-value: 2.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGK-----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN-----DLPPP 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 74 ERGIGMVFQsyalYPHM-----TVYDNMAFG---LKLAKAEAKtvdEKVREVAAALQLD-TLLARKPKALSGGQRQRVAI 144
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGpknLGLSEEEAE---ERVKEALELVGLDeEYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 145 GRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
.
gi 491647138 225 P 225
Cdd:TIGR04521 234 V 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-234 |
2.63e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.34 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--------RGI 77
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairllrQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDNMAFG----LKLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPK 153
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLIEApckvLGLSKEQAR---EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 154 VFLFDEPLSNLDASLRVQMrMEIARLHERLGATMIYVTHdQVE-AMTLATKIVVLDAGRVEQVGSpLELYNHPANTFVAG 232
Cdd:COG4161 162 VLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTH-EVEfARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAH 238
|
..
gi 491647138 233 FI 234
Cdd:COG4161 239 YL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-214 |
5.08e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 162.88 E-value: 5.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--------RGI 77
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSdkairelrRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDNMAFG----LKLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPK 153
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLIEApcrvLGLSKDQAL---ARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 154 VFLFDEPLSNLDASLRVQMRMEIARLHErLGATMIYVTHDQVEAMTLATKIVVLDAGR-VEQ 214
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHiVEQ 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-224 |
1.85e-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: 171.56 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDNMA 97
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIRENIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLKLAKaeaktvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA 166
Cdd:COG2274 571 LGDPDAT------DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 167 SLRVQMrmeIARLHERL-GATMIYVTHDqVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:COG2274 645 ETEAII---LENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-221 |
2.42e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 169.19 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDNMA 97
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGlklaKAEAkTvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA 166
Cdd:COG1132 436 YG----RPDA-T-DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 167 S--LRVQMRMEiaRLHErlGATMIYVTHdqveamTLAT-----KIVVLDAGRVEQVGSPLEL 221
Cdd:COG1132 510 EteALIQEALE--RLMK--GRTTIVIAH------RLSTirnadRILVLDDGRIVEQGTHEEL 561
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
3.93e-47 |
|
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: 158.33 E-value: 3.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG-IGMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMafglklakaeaktvdekvrevaaalqldtllarkpkALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 163 NLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-214 |
5.79e-47 |
|
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: 159.91 E-value: 5.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTF----GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPP-PE------ 74
Cdd:COG4181 11 LRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFAlDEdararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 --RGIGMVFQSYALYPHMTVYDNMAFGLKLA-KAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVRE 151
Cdd:COG4181 88 raRHVGFVFQSFQLLPTLTALENVMLPLELAgRRDAR---ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 152 PKVFLFDEPLSNLDASLRVQMrME-IARLHERLGATMIYVTHDQveamTLATK---IVVLDAGRVEQ 214
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQI-IDlLFELNRERGTTLVLVTHDP----ALAARcdrVLRLRAGRLVE 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-211 |
9.40e-47 |
|
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: 156.64 E-value: 9.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQs 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 yalyphmtvydnmafglklakaeaktvdekvrevaaalqldtllarkpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491647138 164 LDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:cd00267 111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-226 |
1.27e-46 |
|
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: 159.14 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMVFQSYA 85
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNM----------AFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:cd03219 86 LFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 156 LFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
11-236 |
2.14e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.20 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK------------VCNDLPPPER--- 75
Cdd:COG4598 16 KSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgelVPADRRQLQRirt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 76 GIGMVFQSYALYPHMTVYDNMAFG----LKLAKAEAktvdekvREVAAALqLDTL-LARK----PKALSGGQRQRVAIGR 146
Cdd:COG4598 96 RLGMVFQSFNLWSHMTVLENVIEApvhvLGRPKAEA-------IERAEAL-LAKVgLADKrdayPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 147 AIVREPKVFLFDEPLSNLDAS-----LRVqMRmeiaRLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPElvgevLKV-MR----DLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*
gi 491647138 222 YNHPANTFVAGFIGS 236
Cdd:COG4598 242 FGNPKSERLRQFLSS 256
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-221 |
2.43e-46 |
|
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: 158.01 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDlPPPERGIgmVFQSYALYPHMTVYDNMAFG 99
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKTVDEK--VREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIA 177
Cdd:TIGR01184 79 VDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491647138 178 RLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-224 |
2.73e-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: 166.09 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALyPHMTVYDN 95
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQNPYL-FAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 mafgLKLAKAEAKtvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:COG4988 431 ----LRLGRPDAS--DEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 165 DASLRVQMRMEIARLHErlGATMIYVTHDQvEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:COG4988 505 DAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
1.15e-45 |
|
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: 156.69 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVilNKVNKTFGK-VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCN----DLPPPE 74
Cdd:TIGR02315 1 MLEV--ENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTdITKlrgkKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 RGIGMVFQSYALYPHMTVYDN-------------MAFGL--KLAKAEAKTVDEKVREVAAALQldtllarKPKALSGGQR 139
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENvlhgrlgykptwrSLLGRfsEEDKERALSALERVGLADKAYQ-------RADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 140 QRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPL 219
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
....*
gi 491647138 220 ELYNH 224
Cdd:TIGR02315 232 ELDDE 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-221 |
1.65e-45 |
|
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: 164.17 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDN 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 mafgLKLAKAEAKtvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:COG4987 429 ----LRLARPDAT--DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 165 DASLRVQMrmeIARLHERL-GATMIYVTHDQVeAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:COG4987 503 DAATEQAL---LADLLEALaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-233 |
8.48e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 159.04 E-value: 8.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTFGkvhvTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE------RG 76
Cdd:PRK10070 32 EQILEKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGF 233
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-212 |
6.92e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.55 E-value: 6.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDlPPPERGIgmVFQSYALYPHMTVYDNMA 97
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIA 177
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 491647138 178 RLHERLGATMIYVTHDQVEAMTLATKIVVL--DAGRV 212
Cdd:PRK11248 173 KLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRV 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
8.84e-44 |
|
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: 148.56 E-value: 8.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN--DLPPPERGIGMVFQSYALYPHMTVYDNMA 97
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 98 FGLKLAKAEAKTVDEKVREVAAALQL----DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-211 |
9.26e-44 |
|
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: 149.46 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDN 95
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF-SGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MafglklakaeaktvdekvrevaaalqldtllarkpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRME 175
Cdd:cd03228 96 I-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 491647138 176 IARLHErlGATMIYVTHDqVEAMTLATKIVVLDAGR 211
Cdd:cd03228 139 LRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-226 |
1.13e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 153.67 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTF----GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED---ITSGDLKIDGKVCNDLPPPE------R 75
Cdd:COG0444 7 LKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 76 GIGMVFQ-SY-ALYPHMTVYDNMAFGLKL-AKAEAKTVDEKVREVAAALQLDT---LLARKPKALSGGQRQRVAIGRAIV 149
Cdd:COG0444 87 EIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQ-MRMeIARLHERLGATMIYVTHD--QVEAMtlATKIVVLDAGR-VEQvGSPLELYNHP 225
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGRiVEE-GPVEELFENP 242
|
.
gi 491647138 226 A 226
Cdd:COG0444 243 R 243
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-224 |
1.75e-43 |
|
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: 151.81 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG-KVCND--LPPPERGIGMVFQSyalyPH- 89
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEenLWEIRKKVGMVFQN----PDn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 ----MTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:TIGR04520 89 qfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDQVEAmTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:TIGR04520 169 PKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-194 |
1.98e-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: 146.99 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcNDLPPPER--------GI 77
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ--ETPPLNSKkaskfrreKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF 157
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 491647138 158 DEPLSNLDASLRvQMRMEIARLHERLGATMIYVTHDQ 194
Cdd:TIGR03608 159 DEPTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-226 |
4.55e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 149.88 E-value: 4.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGMVFQ-SY 84
Cdd:COG4608 26 RTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 A-LYPHMTVYDNMAFGLKLAK-AEAKTVDEKVREVAAALQLDTLLARK-PKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:COG4608 106 AsLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHD--QVEAMtlATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:COG4608 186 SALDVSIQAQVLNLLEDLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
9.78e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.39 E-value: 9.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPPPERGIGMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPH--MTVYDNMAFGL-------KLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVRE 151
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRygrrglfRRPSRADR---EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 152 PKVFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQvGSPLELYNHPA 226
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-236 |
1.18e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.18 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTF----GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RG 76
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVaaaLQLDTLLARK---PKALSGGQRQRVAIGRAIVREPK 153
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTEL---LELVGLSDKAdryPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 154 VFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTH--DQVEAmtLATKIVVLDAGR-VEQvGSPLELYNHPANTFV 230
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRlVEQ-GTVSEVFSHPKHPLT 237
|
....*.
gi 491647138 231 AGFIGS 236
Cdd:PRK11153 238 REFIQS 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-212 |
1.22e-41 |
|
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: 145.24 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 8 KVNKTF-GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDL-----PPPERGIGMVF 81
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 QSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKvreVAAALQLDTLLARK---PKALSGGQRQRVAIGRAIVREPKVFLFD 158
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKR---VPAALELVGLSHKHralPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 159 EPLSNLDASlrvqMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03292 162 EPTGNLDPD----TTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
9-236 |
1.93e-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: 146.13 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--------LPPPER----- 75
Cdd:TIGR03005 6 VTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplVPADEKhlrqm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 76 --GIGMVFQSYALYPHMTVYDNMA------FGLKLAKAEAKTVdEKVREVAAALQLDTLlarkPKALSGGQRQRVAIGRA 147
Cdd:TIGR03005 86 rnKIGMVFQSFNLFPHKTVLDNVTeapvlvLGMARAEAEKRAM-ELLDMVGLADKADHM----PAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 148 IVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPAN 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 491647138 228 TFVAGFIGS 236
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
1.24e-40 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 142.64 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGK--VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMV 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAF--GLK-LAKAEAKTVDEKVREVaaaLQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF 157
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLKgLPKSEIKEEVELLLRV---LGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 158 DEPLSNLDASLRVQMRMEIarLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
4.07e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.58 E-value: 4.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIdGKVCNDLPPPERG---- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLSQqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 -------IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAK-TVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAI 148
Cdd:PRK11264 80 irqlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 149 VREPKVFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-221 |
5.07e-40 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 141.42 E-value: 5.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMVFQ 82
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNmafgLKLAkAEAKTVDEKVREVAAALQ----LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFD 158
Cdd:cd03224 83 GRRIFPELTVEEN----LLLG-AYARRRAKRKARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 159 EPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-211 |
9.81e-40 |
|
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: 139.92 E-value: 9.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG-IGMVFQSYALYPH 89
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAFGLKLAKAEAKtvDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlr 169
Cdd:COG4133 90 LTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491647138 170 vqmrmEIARLHERL------GATMIYVTHDQVEAmtLATKIVVLDAGR 211
Cdd:COG4133 166 -----GVALLAELIaahlarGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-212 |
1.10e-39 |
|
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: 140.04 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYA 85
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAaalqLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491647138 166 ASLRVQMRmEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03268 159 PDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-223 |
1.31e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 141.67 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--LPPPERGIGMVFQSyalyPH-----MTV 92
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQN----PDnqfigATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQM 172
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 173 RMEIARLHERLGATMIYVTHDQVEAmTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
9-226 |
1.55e-39 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 143.86 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTkeVDLHI-NKGDFVVFvGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND------LPPPERGIGMVF 81
Cdd:PRK11144 6 FKQQLGDLCLT--VNLTLpAQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 QSYALYPHMTVYDNMAFGLKlakaeaKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK11144 83 QDARLFPHYKVRGNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
2.47e-38 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 136.55 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVfVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG-IGMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 163 NLDASLRVQMRMEIARLHErlGATMIYVTH--DQVEAMtlATKIVVLDAGRVEQVG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-227 |
5.91e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.09 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLR-------LIAGLEdiTSGDLKIDGKvcN----DLPPPE--RGIGM 79
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGE--DiydpDVDVVElrRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPhMTVYDNMAFGLKLAKAEAKTV-DEKVREV--AAAL------QLDtllaRKPKALSGGQRQRVAIGRAIVR 150
Cdd:COG1117 97 VFQKPNPFP-KSIYDNVAYGLRLHGIKSKSElDEIVEESlrKAALwdevkdRLK----KSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 151 EPKVFLFDEPLSNLD--ASLRVqmrmE--IARLHERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:COG1117 172 EPEVLLMDEPTSALDpiSTAKI----EelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
.
gi 491647138 227 N 227
Cdd:COG1117 246 D 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-212 |
1.07e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.69 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE---RGIGMVFQSYA 85
Cdd:COG1129 10 ISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKaeAKTVD-----EKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG1129 90 LVPNLSVAENIFLGREPRR--GGLIDwramrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 161 LSNLDASlrvqmrmEIARLHERL------GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG1129 168 TASLTER-------EVERLFRIIrrlkaqGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-204 |
1.86e-37 |
|
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: 134.40 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTF--GK--VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG------IG 78
Cdd:TIGR02211 7 LGKRYqeGKldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnkkLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 79 MVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFD 158
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 159 EPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDqveaMTLATKI 204
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-212 |
3.88e-37 |
|
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: 132.17 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IGMVFQs 83
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 yalyphmtvydnmafglklakaeaktvdekvreVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:cd03214 81 ---------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 164 LDasLRVQMR-ME-IARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03214 128 LD--IAHQIElLElLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-221 |
3.95e-37 |
|
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: 133.89 E-value: 3.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHmT 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMAFGLKLAKaeaktvDEKVREVAAALQLDTLLARKPKA-----------LSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:cd03254 93 IMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 161 LSNLDASLRVQMRMEIARLHErlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-234 |
1.62e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.17 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILN--KVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVC----------- 67
Cdd:PRK10619 1 MSENKLNviDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 68 ----NDLPPPERGIGMVFQSYALYPHMTVYDNMAFG----LKLAKAEAKtvDEKVREVAAALQLDTLLARKPKALSGGQR 139
Cdd:PRK10619 81 vadkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiqvLGLSKQEAR--ERAVKYLAKVGIDERAQGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 140 QRVAIGRAIVREPKVFLFDEPLSNLDASLrvqmRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
250
....*....|....*...
gi 491647138 217 SPLELYNHPANTFVAGFI 234
Cdd:PRK10619 235 APEQLFGNPQSPRLQQFL 252
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-221 |
2.91e-36 |
|
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: 131.97 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG----KVcnDLPPPERGIGMVFQSYALYpHMTVY 93
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirEV--TLDSLRRAIGVVPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGlklaKAEAKtvDEKVREVAAALQLDTLLARKPKA-----------LSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:cd03253 93 YNIRYG----RPDAT--DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 163 NLDaslrVQMRMEIARLHERL--GATMIYVTHDQVEAMTlATKIVVLDAGRVEQVGSPLEL 221
Cdd:cd03253 167 ALD----THTEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-222 |
3.13e-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: 131.89 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 16 VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPhMTVY 93
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGLKLAKAEaktVDEKVREVAAAL--------QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:cd03249 95 ENIRYGKPDATDE---EVEEAAKKANIHdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 166 AS--LRVQMRMEIArlheRLGATMIYVTHdqveamTLAT-----KIVVLDAGRVEQVGSPLELY 222
Cdd:cd03249 172 AEseKLVQEALDRA----MKGRTTIVIAH------RLSTirnadLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
6.90e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 131.50 E-value: 6.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDIT-----SGDLKIDGK--VCNDLPPPE--RGIGMVFQS 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRniYSPDVDPIEvrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAK--AEAKTVDEKVREV--AAAL--QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWAlkKAALwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 158 DEPLSNLDASLRVQMRMEIARLHERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPAN----TFVAGF 233
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHelteKYVTGA 251
|
..
gi 491647138 234 IG 235
Cdd:PRK14267 252 LG 253
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-212 |
1.12e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 129.63 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTV 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKLAKaeaktvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:cd03245 95 RDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 162 SNLDaslrvqMRMEiARLHERL-----GATMIYVTHDQVeAMTLATKIVVLDAGRV 212
Cdd:cd03245 169 SAMD------MNSE-ERLKERLrqllgDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-225 |
1.12e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 136.74 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTL----LRLIAglediTSGDLKIDGKVCNDLPPPE-----RGIGMVF 81
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRAlrplrRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 QS-YA-LYPHMTVYDNMAFGLKLAKAE--AKTVDEKVREVAAALQLD-TLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQ--VEAMtlATKIVVLDAGR-VEQvGSPLELYNHP 225
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGKvVEQ-GPTEQVFDAP 517
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-224 |
1.26e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSyalyPH-----MTV 92
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLklakaEAKTV--DEKVREVAAALQL---DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:PRK13635 100 QDDVAFGL-----ENIGVprEEMVERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 168 LRVQMRMEIARLHERLGATMIYVTHDQVEAMTlATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-221 |
1.36e-35 |
|
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: 129.80 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG-KVCNDLPPPERGIGMVFQSYALYPH 89
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLR 169
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 170 VQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-226 |
1.38e-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: 130.10 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMVFQSYALYPHM 90
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFGLKLAKAEAKTvdEKVREVAAAL--QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLdASL 168
Cdd:COG0410 94 TVEENLLLGAYARRDRAEV--RADLERVYELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL-APL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 169 RVQMRME-IARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:COG0410 171 IVEEIFEiIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-208 |
2.74e-35 |
|
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: 128.42 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlpPPERG---IGMVFQ 82
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKErkrIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYAL---YPhMTVYDNMAFGL-------KLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREP 152
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGLyghkglfRRLSKADK---AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 153 KVFLFDEPLSNLDaslrVQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLD 208
Cdd:cd03235 152 DLLLLDEPFAGVD----PKTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-226 |
3.09e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 3.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGMVFQSY--ALYPHM 90
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFGLK----LAKAEAKtvdEKVREVAAALQLD-TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK10419 107 TVREIIREPLRhllsLDKAERL---ARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV--EQVGSPLELYNHPA 226
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSPA 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-223 |
3.57e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.55 E-value: 3.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND----LPPPERGIGMVFQ--SYALYPHmTVY 93
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvkLSDIRKKVGLVFQypEYQLFEE-TIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGLKLAKAEAKTVDEKVREVAAALQLD--TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQ 171
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 172 MRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-193 |
2.06e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 126.85 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVH--VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG------IGMVFQSYA 85
Cdd:PRK11629 18 GSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK11629 98 LLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180
....*....|....*....|....*...
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHD 193
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHD 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-222 |
2.45e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.93 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvcnDLPPPE------RGIGMVFQSyalyPH---- 89
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG----DLLTEEnvwdirHKIGMVFQN----PDnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 -MTVYDNMAFGLKLAKAEAKTVDEKVREvaaALQLDTLLA---RKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK13650 96 gATVEDDVAFGLENKGIPHEEMKERVNE---ALELVGMQDfkeREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDqVEAMTLATKIVVLDAGRVEQVGSPLELY 222
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-212 |
2.51e-34 |
|
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: 124.46 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE---RGIGMVFQsya 85
Cdd:cd03216 6 ITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMVYQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 lyphmtvydnmafglklakaeaktvdekvrevaaalqldtllarkpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491647138 166 ASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03216 115 PAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-212 |
2.85e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 133.84 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDNMA 97
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDNIA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLKLAKaeaktvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA 166
Cdd:TIGR03375 561 LGAPYAD------DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491647138 167 SLRVQMrmeIARLHERL-GATMIYVTHdQVEAMTLATKIVVLDAGRV 212
Cdd:TIGR03375 635 RSEERF---KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
4.32e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.44 E-value: 4.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKI------DGKVCNDLPPPERGIGMVFQsyalYP-HM-- 90
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPeHQlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 --TVYDNMAFG---LKLAKAEAKtvdEKVREVAAALQLD-TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK13634 100 eeTVEKDICFGpmnFGVSEEDAK---QKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 165 DASLRVQMrMEI-ARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:PRK13634 177 DPKGRKEM-MEMfYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-216 |
5.78e-34 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.17 E-value: 5.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGK----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG-KVCNDLPPPERGIGMV 80
Cdd:cd03266 4 ADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAF-----GLKLAKAEAKtvdekVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:cd03266 84 SDSTGLYDRLTARENLEYfaglyGLKGDELTAR-----LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 156 LFDEPLSNLDAsLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03266 159 LLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-222 |
8.49e-34 |
|
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: 125.42 E-value: 8.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--LPPPERGIGMVFQSYALYpHMTVYDN 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGlklaKAEAKtvDEKVREVAAALQLDTLLARKPKA-----------LSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:cd03251 96 IAYG----RPGAT--REEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 165 DASLRVQMRMEIARLHErlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELY 222
Cdd:cd03251 170 DTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-221 |
1.98e-33 |
|
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: 131.62 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHmTVYDN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFG----LKLAKAEAKTV--DEKVRevAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAslR 169
Cdd:TIGR03797 547 IAGGapltLDEAWEAARMAglAEDIR--AMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDN--R 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 170 VQmRMEIARLhERLGATMIYVTHDQVEAMTlATKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR03797 623 TQ-AIVSESL-ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-226 |
1.33e-32 |
|
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: 122.99 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGMVFQ-SY-ALYPHM 90
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFGLK----LAKAEAKtvdEKVREVAAALQLDTLLARK-PKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:TIGR02769 106 TVRQIIGEPLRhltsLDESEQK---ARIAELLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV--EQVGSPLELYNHPA 226
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFKHPA 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-212 |
1.97e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.50 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGK-----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IG 78
Cdd:COG1101 4 LKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 79 MVFQSYAL--YPHMTVYDNMA--------FGLKLAKAEAKTvdEKVREVAAAL------QLDTllarKPKALSGGQRQRV 142
Cdd:COG1101 84 RVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKRR--ELFRELLATLglglenRLDT----KVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 143 AIGRAIVREPKVFLFDEPLSNLD--ASLRVqmrMEI-ARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDpkTAALV---LELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-212 |
2.08e-32 |
|
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: 120.82 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPPPER--GIGMVFQS--YALYPHmTVY 93
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERrkSIGYVMQDvdYQLFTD-SVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGLKLAKAEAktvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaslRVQMR 173
Cdd:cd03226 91 EELLLGLKELDAGN----EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491647138 174 mEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03226 164 -RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-212 |
2.17e-32 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 121.48 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMVFQ 82
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQldTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:TIGR03410 83 GREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 163 NLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-217 |
2.70e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 126.68 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCnDLPPP----ERGIGMVF 81
Cdd:COG3845 8 LRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPrdaiALGIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 QSYALYPHMTVYDNMAFGL---KLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFD 158
Cdd:COG3845 87 QHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 159 EPLSNLDASlrvqmrmEIARLHERL------GATMIYVTHDQVEAMTLATKIVVLDAGRVeqVGS 217
Cdd:COG3845 167 EPTAVLTPQ-------EADELFEILrrlaaeGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-212 |
4.35e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 120.36 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-----RGIGMVFQSYALYPHMTVYDNM 96
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 AFGLKLAKAEAKTVDekvREVAAALQLDTLLARK---PKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLrvqmR 173
Cdd:PRK10908 101 AIPLIIAGASGDDIR---RRVSAALDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL----S 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491647138 174 MEIARLHE---RLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK10908 174 EGILRLFEefnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-238 |
5.42e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.14 E-value: 5.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLP-------PPERGig 78
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEERG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 79 mvfqsyaLYPHMTVYDNMAF--GLK-LAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:COG4152 82 -------LYPKMKVGEQLVYlaRLKgLSKAEAK---RRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 156 LFDEPLSNLD---ASLrvqMRMEIARLHERlGATMIYVTH--DQVEAmtLATKIVVLDAGRVEQVGSPLELYN-HPANTF 229
Cdd:COG4152 152 ILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRqFGRNTL 225
|
....*....
gi 491647138 230 VAGFIGSPK 238
Cdd:COG4152 226 RLEADGDAG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-212 |
3.76e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.64 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppeRgIGMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------R-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLK--------LAKAEAKTVDE------------------------KVREVAAALQLDT-LLARKPK 132
Cdd:COG0488 72 LDDDLTVLDTVLDGDAelraleaeLEELEAKLAEPdedlerlaelqeefealggweaeaRAEEILSGLGFPEeDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 133 ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAslrvqmrmE-IARLHERLGA---TMIYVTHD-----QVeamtlATK 203
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------EsIEWLEEFLKNypgTVLVVSHDryfldRV-----ATR 218
|
....*....
gi 491647138 204 IVVLDAGRV 212
Cdd:COG0488 219 ILELDRGKL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
4.16e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 123.55 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHmT 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMAFGLKLAKAEAktVDEKVREVAAA-------LQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:TIGR02857 412 IAENIRLARPDASDAE--IREALERAGLDefvaalpQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491647138 165 DASLRVQMRMEIARLHErlGATMIYVTHDqVEAMTLATKIVVL 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-225 |
5.06e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.07 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 35 VGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDL--PPPE------RGIGMVFQS-YA-LYPHMTVYDNMAFGL---- 100
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQ---DLlkADPEaqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLlint 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 101 KLAKAEAKtvdEKVREVAAALQLDTLLA-RKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARL 179
Cdd:PRK11308 124 SLSAAERR---EKALAMMAKVGLRPEHYdRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 180 HERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK11308 201 QQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-225 |
1.30e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.04 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER-----GIGMVFQS--YALYPHMTVYD 94
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 NMAFGL-----KLAKAEAKtvdEKVREVAAALQL-DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:PRK15079 120 IIAEPLrtyhpKLSRQEVK---DRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-221 |
1.66e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.11 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQS 83
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGL------KLAKAEaktvDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF 157
Cdd:COG4604 84 NHINSRLTVRELVAFGRfpyskgRLTAED----REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 158 DEPLSNLDASLRVQMrMEIAR-LHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:COG4604 160 DEPLNNLDMKHSVQM-MKLLRrLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-216 |
3.18e-30 |
|
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: 121.39 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IGMVFQSYALYPHmT 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMA-FGlklakaEAKtvDEKVreVAAA---------LQL----DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF 157
Cdd:COG4618 422 IAENIArFG------DAD--PEKV--VAAAklagvhemiLRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 158 DEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQvEAMTLATKIVVLDAGRVEQVG 216
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-212 |
3.46e-30 |
|
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: 115.95 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSG-DLKIDGK----------------V 66
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkriglV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 67 CNDL----PPPERGIGMV----FQSYALYPHMTvyDNMAfglklakaeaktvdEKVREVAAALQLDTLLARKPKALSGGQ 138
Cdd:COG1119 84 SPALqlrfPRDETVLDVVlsgfFDSIGLYREPT--DEQR--------------ERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 139 RQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-197 |
6.14e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 115.65 E-value: 6.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGdLKIDGKVC--------NDLPPPE--RGIG 78
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPVEvrRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 79 MVFQSYALYPHmTVYDNMAFGLKLAKAEA---KTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGARINGYKGdmdELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491647138 156 LFDEPLSNLD--ASLRVQMRMEiaRLHERLgaTMIYVTHDQVEA 197
Cdd:PRK14243 174 LMDEPCSALDpiSTLRIEELMH--ELKEQY--TIIIVTHNMQQA 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
1.19e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.62 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL-----EDITSGDLKIDGKVCNDLPPPE- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 -RGIGMVFQSYALYPHMTVYDNMAFGLKLAK--AEAKTVDEKVREVAAALQL-----DTLLARKPKaLSGGQRQRVAIGR 146
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevkDRLDAPAGK-LSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 147 AIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-234 |
1.35e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 114.76 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN--------DLPPPERGIGMVFQSYALYPH 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAF-----GLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK14246 105 LSIYDNIAYplkshGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 165 DASLRVQMRMEIARLHERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFI 234
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-226 |
3.13e-29 |
|
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: 113.02 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLD--ASLRVQmRMeIARLHER-LGatmIYVT-HDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:cd03218 161 FAGVDpiAVQDIQ-KI-IKILKDRgIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-207 |
3.36e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.89 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQS 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHmTVYDNMAFGLKLAKaeaKTVDEKvrEVAAALQL----DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRN---QQPDPA--IFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEaMTLATKIVVL 207
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-226 |
4.26e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 117.86 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKS----TLLRLIAGLEDITSGDLKIDGKVCNDLPPPE----RG--IGMVFQ- 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 -SYALYPHMTVYDNMAFGLKL------AKAEAKTVD--EKVREVAAAlqldTLLARKPKALSGGQRQRVAIGRAIVREPK 153
Cdd:COG4172 101 pMTSLNPLHTIGKQIAEVLRLhrglsgAAARARALEllERVGIPDPE----RRLDAYPHQLSGGQRQRVMIAMALANEPD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 154 VFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQ--VEAMtlATKIVVLDAGR-VEQvGSPLELYNHPA 226
Cdd:COG4172 177 LLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGEiVEQ-GPTAELFAAPQ 249
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-212 |
5.93e-29 |
|
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: 110.38 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IGMVFQSYALYPHmTVYDN 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MafglklakaeaktvdekvrevaaalqldtllarkpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRME 175
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 491647138 176 IARLHERlGATMIYVTHdQVEAMTLATKIVVLDAGRV 212
Cdd:cd03246 139 IAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-223 |
1.41e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.71 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCndlPPPERGIGMVfq 82
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS---ALLELGAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 syalyPHMTVYDNMAFG---LKLAKAEaktVDEKVREVA--AALQ--LDTllarkP-KALSGGQRQRVAIGRAIVREPKV 154
Cdd:COG1134 101 -----PELTGRENIYLNgrlLGLSRKE---IDEKFDEIVefAELGdfIDQ-----PvKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 155 FLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHD--QVEamTLATKIVVLDAGRVEQVGSP---LELYN 223
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPeevIAAYE 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-216 |
1.99e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.06 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLP-------PPERGig 78
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 79 mvfqsyaLYPHMTVYDNMAF-----GLKlaKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPK 153
Cdd:cd03269 81 -------LYPKMKVIDQLVYlaqlkGLK--KEEAR---RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 154 VFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTH--DQVEAMtlATKIVVLDAGRVEQVG 216
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHqmELVEEL--CDRVLLLNKGRAVLYG 210
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-221 |
2.15e-28 |
|
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: 116.46 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDNMA 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGlklaKAEAKtvDEKVREVAAALQLDTLLARKPKA-----------LSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD- 165
Cdd:COG5265 454 YG----RPDAS--EEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDs 527
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 166 -------ASLRvqmrmEIARlherlGATMIYVTH------DqveamtlATKIVVLDAGR-VEQvGSPLEL 221
Cdd:COG5265 528 rteraiqAALR-----EVAR-----GRTTLVIAHrlstivD-------ADEILVLEAGRiVER-GTHAEL 579
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-207 |
3.38e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.86 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlpppeRGIGMVFQSYALYPHM-- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFGL--------KLAKAEAKTVDEKVrevaAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:NF040873 73 TVRDLVAMGRwarrglwrRLTRDDRAAVDDAL----ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491647138 163 NLDASLRVQMRMEIARLHERlGATMIYVTHDqVEAMTLATKIVVL 207
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-216 |
3.78e-28 |
|
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: 109.93 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCndlPPPERGIGMVfqsyalyPHMTVY 93
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLLGLGGGFN-------PELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMr 173
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491647138 174 meIARLHERL--GATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03220 182 --QRRLRELLkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-227 |
5.97e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.25 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVIL--NKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDI-----TSGDLKIDGKvcnDLPPP 73
Cdd:PRK14239 1 MTEPILqvSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGH---NIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 74 E-------RGIGMVFQSYALYPhMTVYDNMAFGLKLAKAEAKTV-DEKVRE--VAAAL--QLDTLLARKPKALSGGQRQR 141
Cdd:PRK14239 78 RtdtvdlrKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKslKGASIwdEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 142 VAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
....*.
gi 491647138 222 YNHPAN 227
Cdd:PRK14239 235 FMNPKH 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-212 |
8.04e-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: 108.02 E-value: 8.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED--ITSGDLKIDGKvcnDLPPPE--RGIGMVFQSYALYPHMTVYDN 95
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGR---PLDKRSfrKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFglklakaeaktvdekvrevAAALqldtllarkpKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMrME 175
Cdd:cd03213 103 LMF-------------------AAKL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV-MS 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 491647138 176 IARLHERLGATMIYVTHD-QVEAMTLATKIVVLDAGRV 212
Cdd:cd03213 153 LLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-221 |
8.50e-28 |
|
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: 114.13 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKI----DGKVCNDLPPPERG-----IGMVFQSY 84
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGrakryIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNM--AFGLKLAK--AEAKTV---------DEKVREVaaalqldtlLARKPKALSGGQRQRVAIGRAIVRE 151
Cdd:TIGR03269 375 DLYPHRTVLDNLteAIGLELPDelARMKAVitlkmvgfdEEKAEEI---------LDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 152 PKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
8.58e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.35 E-value: 8.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GI 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDN-MAFgLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 157 FDEPLSNLD--ASLRVQmRMeIARLHER-LGatmIYVTHDQVEAmTLatKIV----VLDAGRVEQVGSPLELYNHP 225
Cdd:COG1137 160 LDEPFAGVDpiAVADIQ-KI-IRHLKERgIG---VLITDHNVRE-TL--GICdrayIISEGKVLAEGTPEEILNNP 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-222 |
1.39e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK--VCNDLPPPERGIGMVFQSY-ALYPHMTVYDNMAF 98
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 99 GLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIAR 178
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491647138 179 LHERLGATMIYVTHDQVEAMTlATKIVVLDAGRVEQVGSPLELY 222
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-216 |
1.46e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 113.60 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG--IGMVFQSYALYPHmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMA-FGLKLAkaeaktvDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:TIGR01842 408 VAENIArFGENAD-------PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
6.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSG-----DLKIDGkvcNDLPPPERGIGMVFQSyalyPH----- 89
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynNQAITD---DNFEKLRKHIGIVFQN----PDnqfvg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAFGLKlakAEAKTVDEKVREVAAALQLDTLLAR---KPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA 166
Cdd:PRK13648 99 SIVKYDVAFGLE---NHAVPYDEMHRRVSEALKQVDMLERadyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 167 SLRVQMRMEIARLHERLGATMIYVTHDQVEAMTlATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-218 |
7.46e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.51 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNdlPPPERGI----GMVFQSyalyPH--- 89
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVrskvGLVFQD----PDdqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 --MTVYDNMAFG---LKLAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK13647 93 fsSTVWDDVAFGpvnMGLDKDE---VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491647138 165 DASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-228 |
8.25e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.43 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDItSGDLKIDGKV-------------CNDLpppERGIGMVFQSY 84
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerrvnLNRL---RRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPhMTVYDNMAFGLKLAKAEAKT-VDEKVREVAAALQL-DTLLARKPKA---LSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGWRPKLeIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 160 PLSNLD--ASLRVQMRMEIARLHERLgaTMIYVTHD--QVEAMTLATKIVVLDAGRVEQV---GSPLELYNHPANT 228
Cdd:PRK14258 177 PCFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNlhQVSRLSDFTAFFKGNENRIGQLvefGLTKKIFNSPHDS 250
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-224 |
1.28e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN------DLPPPERGIGMVFQsyalYPHM---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 -TVYDNMAFG---LKLAKAEA-KTVDEKVREVAAAlqlDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK13649 101 eTVLKDVAFGpqnFGVSQEEAeALAREKLALVGIS---ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 166 ASLRVQMRMEIARLHErLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:PRK13649 178 PKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-225 |
1.30e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.77 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvcNDLPPPERG--------IGMVFQSYALYPHMTV 92
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPAMSRSrlytvrkrMSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKlakaEAKTVDEKVREVAAALQLDTLLAR-----KPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA- 166
Cdd:PRK11831 102 FDNVAYPLR----EHTQLPAPLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPi 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 167 SLRVQMRMeIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK11831 178 TMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
2.29e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.35 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE---RGI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDNMAFGLKLakAEAKTVDEKVREVAAAL-QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRV--EQVGSPL 219
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDAL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-218 |
4.29e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 7 NKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSY 84
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 AL-YPhMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVR------EPKVFLF 157
Cdd:PRK13548 86 SLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 158 DEPLSNLDasLRVQMR-MEIAR-LHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:PRK13548 165 DEPTSALD--LAHQHHvLRLARqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-226 |
5.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.45 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND---LPPPERGIGMVFQS-YALYPHMTVYDN 95
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGIVFQNpETQFVGRTVEED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFG---LKLAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQM 172
Cdd:PRK13644 99 LAFGpenLCLPPIE---IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491647138 173 RMEIARLHERlGATMIYVTHDqVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:PRK13644 176 LERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-211 |
7.16e-26 |
|
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: 102.93 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvcndlppperGIGMVFQSyALYPHMTVYDNMAFG 99
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE-PWIQNGTIRENILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKaeaktvdEKVREV--AAALQLD---------TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:cd03250 90 KPFDE-------ERYEKVikACALEPDleilpdgdlTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTHdQVEAMTLATKIVVLDAGR 211
Cdd:cd03250 163 GRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-222 |
1.02e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG---KVCNDLPPPERGIGMVFQSyalyPH----- 89
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLR 169
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491647138 170 VQMRMEIARLHERLGATMIYVTHDQVEAMTlATKIVVLDAGRVEQVGSPLELY 222
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-223 |
1.03e-25 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 103.39 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 24 LHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNdlpPPERGIGMVFQSYAL---YPhMTVYDNMAFGL 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQRHEFawdFP-ISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 101 --------KLAKAEAKTVDEKVREVaaalQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD---ASLR 169
Cdd:TIGR03771 77 tghigwlrRPCVADFAAVRDALRRV----GLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491647138 170 VQMRMEIArlheRLGATMIYVTHDQVEAMTLATKIVVLDaGRVEQVGSPLELYN 223
Cdd:TIGR03771 153 TELFIELA----GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-193 |
1.31e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.93 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 2 AEVIL--NKVNKTFG----KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER 75
Cdd:PRK10584 3 AENIVevHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 76 G------IGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIV 149
Cdd:PRK10584 83 AklrakhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHD 193
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-229 |
1.59e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.87 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKST----LLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQ--SY 84
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFGLKLAKAE--AKTVDEKVREVAAALQLD-TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTF 229
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
1.68e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKidgkvcndlpppeRGIGMVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-------------LGETVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YA-----LYPHMTVYDNMAfglklakAEAKTVDEK-VREVAAALQLDTLLARKP-KALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:COG0488 383 FDqhqeeLDPDKTVLDELR-------DGAPGGTEQeVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 157 FDEPLSNLD-ASLRVqmrmeiarLHERLGA---TMIYVTHDQ--VEamTLATKIVVLDAGRVE 213
Cdd:COG0488 456 LDEPTNHLDiETLEA--------LEEALDDfpgTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-255 |
1.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL---EDITSGDLKIDGKVCND--LPPPERGIGMVFQSY-ALYP 88
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktVWDIREKVGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 89 HMTVYDNMAFGLK---LAKAEAKTVdekVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK13640 99 GATVGDDVAFGLEnraVPRPEMIKI---VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 166 ASLRVQMRMEIARLHERLGATMIYVTHDQVEAmTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAG----FIGSPKMNF 241
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGldipFVYKLKNKL 254
|
250
....*....|....
gi 491647138 242 LTADIVEPGEVTTK 255
Cdd:PRK13640 255 KEKGISVPQEINTE 268
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
2.44e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.17 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVI-LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL--EDITSGD--------LKIDGKVCND 69
Cdd:PRK09984 1 MQTIIrVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShiellgrtVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 70 LPPPERGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTV------DEKVREVAAALQLDT--LLARKPKALSGGQRQR 141
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCfswftrEQKQRALQALTRVGMvhFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 142 VAIGRAIVREPKVFLFDEPLSNLDA-SLRVQMRMeIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPeSARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-228 |
3.53e-25 |
|
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: 102.06 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED----ITSGDLKIDGKVCNDLPPPERGIGMVFQS--YALYPHMTVYDN 95
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLKLAKAEAKTVDEKVREVAAALQLD---TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQM 172
Cdd:TIGR02770 85 AIETLRSLGKLSKQARALILEALEAVGLPdpeEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 173 RMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANT 228
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-220 |
3.56e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.50 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 12 TFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPH 89
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAFGLkLAKAEAKTVDEK-VREVAAALQLDTLLARKPKALSGGQRQRVAIGRAI------VREPKVFLF-DEPL 161
Cdd:COG4559 90 FTVEEVVALGR-APHGSSAAQDRQiVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 162 SNLDasLRVQMR-MEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLE 220
Cdd:COG4559 169 SALD--LAHQHAvLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-264 |
4.54e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN------DLPPPERGIGMVFQsyalYPHM---- 90
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPESqlfe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 -TVYDNMAFG---LKLAKAEA-KTVDEKVREVAAALQLdtlLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK13643 100 eTVLKDVAFGpqnFGIPKEKAeKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 166 ASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHpANTFVAGFIGSPKMNFLTAD 245
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-VDFLKAHELGVPKATHFADQ 254
|
250 260
....*....|....*....|
gi 491647138 246 IVEPGEVT-TKVQIHRGQAI 264
Cdd:PRK13643 255 LQKTGAVTfEKLPITRAELV 274
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-224 |
8.08e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.39 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTFGK-----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL-----EDITSGDLKIDG--KVCNDL 70
Cdd:PRK13645 6 DIILDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPAnlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 71 PPPERGIGMVFQ--SYALYPHmTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQL-DTLLARKPKALSGGQRQRVAIGRA 147
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 148 IVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-224 |
9.06e-25 |
|
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: 105.57 E-value: 9.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--LPPPERGIGMVFQSYALYPHmTVYDNMAFG 99
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVALVSQDVVLFND-TIANNIAYG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 lklakAEAKTVDEKVREVAAA-----------LQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:TIGR02203 430 -----RTEQADRAEIERALAAayaqdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 169 RVQMRMEIARLHErlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:TIGR02203 505 ERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-212 |
9.63e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.96 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGI------GMVFQSYALY 87
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 88 PHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 168 LRVQMRMEIARLHERlGATMIYVTHD-QVEAMtlATKIVVLDAGRV 212
Cdd:PRK10535 179 SGEEVMAILHQLRDR-GHTVIIVTHDpQVAAQ--AERVIEIRDGEI 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-221 |
9.96e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED--ITSGDLKIDGKVCNDLPPPER---GIGMVFQSYALYPHMTVYD 94
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 nmaFgLKLAKAE-------AKTVDEKVREVAAALQLDTLLARKP--KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:COG0396 97 ---F-LRTALNArrgeelsAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 166 A-SLRVqMRMEIARLHERlGATMIYVTH-----DQVEamtlATKIVVLDAGRVEQVGSPlEL 221
Cdd:COG0396 173 IdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-193 |
1.64e-24 |
|
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: 104.75 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYpHMTVYDN 95
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 mafgLKLAKAEAKtvDEKVREVAAALQLDTLLARKP-----------KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:TIGR02868 429 ----LRLARPDAT--DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180 190
....*....|....*....|....*....|
gi 491647138 165 DASLRVQM-RMEIARLHERlgaTMIYVTHD 193
Cdd:TIGR02868 503 DAETADELlEDLLAALSGR---TVVLITHH 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-212 |
1.86e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 100.10 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpPPERG------IGMVF- 81
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRkkflrrIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 ------------QSYALYPHMtvYDnmafglkLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIV 149
Cdd:cd03267 102 qktqlwwdlpviDSFYLLAAI--YD-------LPPARFK---KRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-178 |
1.92e-24 |
|
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: 100.04 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 8 KVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED---ITSGDLKIDGKvcndlpPPERG-----IGM 79
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ------PRKPDqfqkcVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMAFG--LKLAKAEAKTVDEKVREVAAALQL-DTLLA-RKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDLaLTRIGgNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180
....*....|....*....|....*.
gi 491647138 156 LFDEPLSNLDASLR---VQMRMEIAR 178
Cdd:cd03234 166 ILDEPTSGLDSFTAlnlVSTLSQLAR 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-221 |
1.94e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHM 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFG----LKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA 166
Cdd:PRK10253 97 TVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 167 SLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-192 |
2.23e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLkidgkvcnDLPPPERgigMVF---QSY--------AL-Y 87
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPYlplgtlreALlY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 88 PHmtvydnmafglklakAEAKTVDEKVREVAAALQLDTLLAR------KPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:COG4178 449 PA---------------TAEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|..
gi 491647138 162 SNLDASLRVQMrmeIARLHERL-GATMIYVTH 192
Cdd:COG4178 514 SALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
10-223 |
2.60e-24 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 104.64 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 10 NKTFG----KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQS 83
Cdd:TIGR03796 482 NITFGysplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVAMVDQD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYpHMTVYDNMA--------FGLKLAKAEAKTVDEKVREVAaalQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:TIGR03796 562 IFLF-EGTVRDNLTlwdptipdADLVRACKDAAIHDVITSRPG---GYDAELAEGGANLSGGQRQRLEIARALVRNPSIL 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 156 LFDEPLSNLDASLRvqmRMEIARLHERlGATMIYVTHdqveamTLAT-----KIVVLDAGRVEQVGSPLELYN 223
Cdd:TIGR03796 638 ILDEATSALDPETE---KIIDDNLRRR-GCTCIIVAH------RLSTirdcdEIIVLERGKVVQRGTHEELWA 700
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-221 |
2.74e-24 |
|
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: 99.87 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvcNDLPPPE-----RGIGMVFQSYALYpHMTV 92
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADpawlrRQVGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGlklakAEAKTVdEKVREVAAA-------LQL----DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:cd03252 93 RDNIALA-----DPGMSM-ERVIEAAKLagahdfiSELpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 162 SNLD-ASLRVQMRmeiaRLHERL-GATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:cd03252 167 SALDyESEHAIMR----NMHDICaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
4.32e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN--DLPPPERGIGMVFQS---YALYP 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 89 hmTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:PRK13652 95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-225 |
6.03e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.65 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlPPPE-------RGIGMVFQSYALY 87
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-----PLVQydhhylhRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 88 PHmTVYDNMAFGLKlakaeaKTVDEKVREVAAALQLDTLLARKPKA-----------LSGGQRQRVAIGRAIVREPKVFL 156
Cdd:TIGR00958 568 SG-SVRENIAYGLT------DTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 157 FDEPLSNLDAslrvQMRMEIARLHERLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:TIGR00958 641 LDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-192 |
7.52e-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: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPP-PERGIGMVFQSYALYPHMTVYDNMAFGL 100
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 101 KLAKAEAKTVDEKVREVAAALQLDTLLArkpkALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlRVQMRMEIARLH 180
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAVGLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAH 173
|
170
....*....|..
gi 491647138 181 ERLGATMIYVTH 192
Cdd:TIGR01189 174 LARGGIVLLTTH 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
8.37e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN----DLPPPERGIGMVFQS-----YAlyPhm 90
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddqlFA--P-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFG---LKLAKAEaktVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:PRK13639 95 TVEEDVAFGplnLGLSKEE---VEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 168 LRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-225 |
9.26e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.62 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVhVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITsGDLKIDGKVCNDLPPPE--RGIGMVFQSYALyPHMT 91
Cdd:PRK11174 362 GKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMAfglkLAKAEAKtvDEKVREVAAALQLDTLLARKPKAL-----------SGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:PRK11174 439 LRDNVL----LGNPDAS--DEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 161 LSNLDA-SLRVQMRmeiARLHERLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK11174 513 TASLDAhSEQLVMQ---ALNAASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-218 |
1.45e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 12 TFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYAL--- 86
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 87 -----------YPHMTVYDNMafglklakaeAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:PRK09536 92 fdvrqvvemgrTPHRSRFDTW----------TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 156 LFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-245 |
1.56e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 98.32 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHV--TKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN--DLPPPERGIGMVFQ--SYAL 86
Cdd:PRK15112 21 FRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 87 YPHMTVYDNMAFGLKL-----AKAEAKTVDEKVREVAAalqLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK15112 101 NPRQRISQILDFPLRLntdlePEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGFIGSPKMNF 241
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFGEA 257
|
....
gi 491647138 242 LTAD 245
Cdd:PRK15112 258 LTAD 261
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-224 |
1.74e-23 |
|
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: 96.44 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED--ITSGDLKIDGKVCNDLPPPER---GIGMVFQSYALYP 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 89 hmtvydnmafGLKLAkaeaktvdEKVREVAaalqldtllarkpKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDA-S 167
Cdd:cd03217 91 ----------GVKNA--------DFLRYVN-------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 168 LRVqMRMEIARLHERlGATMIYVTH-----DQVEamtlATKIVVLDAGRVEQVGSP---LELYNH 224
Cdd:cd03217 140 LRL-VAEVINKLREE-GKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSGDKelaLEIEKK 198
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-221 |
2.77e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 101.74 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP--ERGIGMVFQSYALYPHmTVYDN 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAfglkLAKAEAKtvDEKVR---EVAAALQL--------DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:TIGR01846 551 IA----LCNPGAP--FEHVIhaaKLAGAHDFiselpqgyNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSAL 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 165 D----ASLRVQMRmEIARlherlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR01846 625 DyeseALIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-212 |
2.79e-23 |
|
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: 96.77 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP--ERGIGMVFQSYALYPHmTVYDN 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLklakaeAKTVDEKVREVAA-----------ALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:cd03248 108 IAYGL------QSCSFECVKEAAQkahahsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491647138 165 DASLRVQMRMEIARLHERlgATMIYVTHdQVEAMTLATKIVVLDAGRV 212
Cdd:cd03248 182 DAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-226 |
2.84e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.77 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL----------EDITSGDlKIDGKVCNDLPPPE------ 74
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGD-KKNNHELITNPYSKkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 ---RGIGMVFQ--SYALYPHmTVYDNMAFG---LKLAKAEAKtvdEKVREVAAALQLD-TLLARKPKALSGGQRQRVAIG 145
Cdd:PRK13631 113 elrRRVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAK---KLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 146 RAIVREPKVFLFDEPLSNLDASLRVQMrMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
.
gi 491647138 226 A 226
Cdd:PRK13631 268 H 268
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-220 |
2.88e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGigmvfQSYALYP--HM 90
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----RRLALLPqhHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 T-----VYDNMAFGL--------KLAKAEAKTVDEKVrevaAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF 157
Cdd:PRK11231 87 TpegitVRELVAYGRspwlslwgRLSAEDNARVNQAM----EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 158 DEPLSNLDASLRVQMrMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLE 220
Cdd:PRK11231 163 DEPTTYLDINHQVEL-MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-225 |
3.72e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN------DLPPPERGIGMVFQsyalYPHM---- 90
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 -TVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARK-PKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 169 RVQMrMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK13641 181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-221 |
1.62e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHmTVYD 94
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 NmafgLKLAKAEAKtvDEKVREVAAALQLDTLLARKP----------KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK11160 433 N----LLLAAPNAS--DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 165 DASLRVQMrMEIARLHERlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PRK11160 507 DAETERQI-LELLAEHAQ-NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-225 |
1.70e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 5 ILNKVNKtfgKVHVTKEVDLHINKGDFVVFVGPSGCGKST----LLRLIAGLE-DITSGDLKIDGKVCNDLPPPERGIGM 79
Cdd:PRK10261 329 LLNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQGgEIIFNGQRIDTLSPGKLQALRRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQS-YA-LYPHMTVYDNM-----AFGLKLAKAEAKTVDEKVREVAaaLQLDTLLaRKPKALSGGQRQRVAIGRAIVREP 152
Cdd:PRK10261 406 IFQDpYAsLDPRQTVGDSImeplrVHGLLPGKAAAARVAWLLERVG--LLPEHAW-RYPHEFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 153 KVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-223 |
2.16e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.58 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDNMAFGLKLAK-AEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-223 |
2.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG-KVCND-----LPPPERGIGMVFQsyalYPHMTVY 93
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKtkdkyIRPVRKRIGMVFQ----FPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DN-----MAFGLKLAKAEAktvdEKVREVAAALQLD-----TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:PRK13646 100 EDtvereIIFGPKNFKMNL----DEVKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 164 LDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-212 |
2.66e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP---ERGIGMVFQSYA 85
Cdd:PRK15439 17 ISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLArkpkALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK15439 97 LFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 166 ----ASLRVQMRMEIArlherLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK15439 173 paetERLFSRIRELLA-----QGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
3.65e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 2 AEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlPPPERG----- 76
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE-----PVPSRArharq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 77 -IGMVFQSYALYPHMTVYDNMA-----FGLKLAKAEAKTvdEKVREVAaalQLDTLLARKPKALSGGQRQRVAIGRAIVR 150
Cdd:PRK13537 81 rVGVVPQFDNLDPDFTVRENLLvfgryFGLSAAAARALV--PPLLEFA---KLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 151 EPKVFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-222 |
5.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN----DLPPPERGIGMVFQS--YALYPhM 90
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLRESVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRV 170
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 171 QMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELY 222
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
5.98e-22 |
|
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: 92.88 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVI-LNKVNKTF------GK-VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKI---DGKVcnD 69
Cdd:COG4778 1 MTTLLeVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWV--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 70 L---PPPE------RGIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKA-LSGGQR 139
Cdd:COG4778 79 LaqaSPREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPAtFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 140 QRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQvEAM-TLATKIVVLDAGR 211
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVReAVADRVVDVTPFS 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-192 |
9.64e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERgIGMVFQSYALYPHMTVYDNMAFGLK 101
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 102 LAKAEaktvDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlRVQMRMEIARLHE 181
Cdd:PRK13539 100 FLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELIRAHL 174
|
170
....*....|.
gi 491647138 182 RLGATMIYVTH 192
Cdd:PRK13539 175 AQGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-212 |
1.77e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.61 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 16 VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlPPPER-----GIGMVF-QSYALYPH 89
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKRRkefarRIGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNmafgLKLAKA----EAKTVDEKVREVAAALQLDTLL---ARKpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:COG4586 111 LPAIDS----FRLLKAiyriPDAEYKKRLDELVELLDLGELLdtpVRQ---LSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 163 NLDASLRVQMRMEIARLHERLGATMIYVTHD--QVEAmtLATKIVVLDAGRV 212
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-234 |
3.39e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.19 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSyalyPHM---TV 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYLPQE----PYIfsgSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKlAKAEAKTVDEKVR--EVAAALQ-----LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIWAACEiaEIKDDIEnmplgYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 166 ASLRVQMRMEIARLHERlgaTMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNhpANTFVAGFI 234
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLD--RNGFYASLI 706
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
3.40e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP---ERGIGMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKA--EAKTVD-EKVREVAAALQLDTLLARKPKA----LSGGQRQRVAIGRAIVREPK 153
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKvcGVNIIDwREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 154 VFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAG 210
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-208 |
4.34e-21 |
|
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: 91.32 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPpergigmvfQSYALYPhMTVYDnmafgLKLAKA 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ---------YIKADYE-GTVRD-----LLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 106 EAKTVDEKVR-EVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLG 184
Cdd:cd03237 87 KDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|....
gi 491647138 185 ATMIYVTHDQVEAMTLATKIVVLD 208
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-221 |
4.51e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.64 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTF-GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--LPPPERGIGM 79
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYpHMTVYDNmafgLKLAKAEAktVDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAI 148
Cdd:PRK13657 414 VFQDAGLF-NRSIEDN----IRVGRPDA--TDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 149 VREPKVFLFDEPLSNLDASLRVQMRMEIARLheRLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-278 |
1.89e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvcndLPPPER------GIGM 79
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-----VPVPARarlaraRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYALYPHMTVYDNMA-----FGLKLAKAEAktVDEKVREVAaalQLDTLLARKPKALSGGQRQRVAIGRAIVREPKV 154
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLvfgryFGMSTREIEA--VIPSLLEFA---RLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 155 FLFDEPLSNLDASLR----VQMRMEIARlherlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHpantfv 230
Cdd:PRK13536 194 LILDEPTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE------ 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 491647138 231 agFIGSPKMNFLTADivePGEVTTKVQIHrGQAIVVSANTIGAKVGDP 278
Cdd:PRK13536 263 --HIGCQVIEIYGGD---PHELSSLVKPY-ARRIEVSGETLFCYAPDP 304
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-212 |
2.12e-20 |
|
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: 87.49 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMV---FQSYALYPHMTVY 93
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGLklakaeaktvdekvrevaaalqldtllarkpkALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaslrVQMR 173
Cdd:cd03215 97 ENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491647138 174 MEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03215 141 AEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
2.95e-20 |
|
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: 85.96 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlppperGIGMVFQs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------KIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 yalyphmtvydnmafglklakaeaktvdekvrevaaalqldtllarkpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491647138 164 LDaslrVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:cd03221 101 LD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-240 |
4.15e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.17 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKS----TLLRLIAGlEDITSGDLKIDGKVCNDLPPPE------RGIGMVFQS 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKElnklraEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 --YALYPHMTVYDNMAFGLKL----AKAEAktVDEKVRevaaalQLDTLL---ARK-----PKALSGGQRQRVAIGRAIV 149
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMEVLMLhkgmSKAEA--FEESVR------MLDAVKmpeARKrmkmyPHEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTF 229
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
250
....*....|..
gi 491647138 230 VAGFIGS-PKMN 240
Cdd:PRK09473 258 SIGLLNAvPRLD 269
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-238 |
4.52e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.00 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 34 FVGPSGCGKSTLLRLIAGLEDITSG-----DLKIDGKVC---NDLPPPERGIGMVFQSYALYPhMTVYDNMAFGLK---- 101
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRahkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 102 LAKAEAKTVDE-KVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLH 180
Cdd:PRK14271 131 VPRKEFRGVAQaRLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 181 ERLgaTMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANT----FVAGFIGSPK 238
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSGDVK 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-211 |
6.03e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKV---CNDLPPPERGIGMVFQ 82
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAALAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMAFGL---KLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:PRK11288 87 ELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 160 PLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
8.53e-20 |
|
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: 86.78 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKST----LLRLIagleDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHmT 91
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMAFGLKLAKAEAKTVDEKV--REVAAAL--QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:cd03244 94 IRSNLDPFGEYSDEELWQALERVglKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 168 LRVQMRmEIARlHERLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:cd03244 174 TDALIQ-KTIR-EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-233 |
1.03e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 91.23 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKeVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMVFQSY 84
Cdd:TIGR01257 934 LVKIFEPSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFglkLAKAEAKTVDEKVREVAAALQlDTLLARK----PKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:TIGR01257 1013 ILFHHLTVAEHILF---YAQLKGRSWEEAQLEMEAMLE-DTGLHHKrneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 161 LSNLDASLRVQMRMEIarLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELynhpANTFVAGF 233
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-223 |
2.08e-19 |
|
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: 89.48 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDI--TSGDL----------------KIDGKVC 67
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpSKVGEPC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 68 ----NDLPPPE---------------RGIGMVFQ-SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLL 127
Cdd:TIGR03269 83 pvcgGTLEPEEvdfwnlsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 128 ARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD---ASLRVQMRMEIARlheRLGATMIYVTHDQVEAMTLATKI 204
Cdd:TIGR03269 163 THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAVK---ASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 491647138 205 VVLDAGRVEQVGSPLELYN 223
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVA 258
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-212 |
2.42e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDiTSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHMTVYDNMAFG 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKlAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVR-------EPKVFLFDEPLSNLD-----AS 167
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDvaqqaAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491647138 168 LRVqmrmeIARLHErLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG4138 173 DRL-----LRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-221 |
3.36e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLL-----RLIAGLEdiTSGDLKIDGKVCnDLPPPERGIGMVFQSYALYPHMT 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMAFG--LKLAKAEAKTVD-EKVREVAAALQL----DTLL--ARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:TIGR00955 116 VREHLMFQahLRMPRRVTKKEKrERVDEVLQALGLrkcaNTRIgvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 163 NLD---ASLRVQMRMEIArlheRLGATMIYVTHD-QVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR00955 196 GLDsfmAYSVVQVLKGLA----QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
1.03e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.52 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTFGK-----VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSG-------DLKIDGK----- 65
Cdd:PRK13651 2 QIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkDEKNKKKtkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 66 ---VCNDLPPPE-----------RGIGMVFQ--SYALYpHMTVYDNMAFG---LKLAKAEAKtvdEKVREVAAALQLD-T 125
Cdd:PRK13651 82 kvlEKLVIQKTRfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGpvsMGVSKEEAK---KRAAKYIELVGLDeS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 126 LLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIV 205
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*...
gi 491647138 206 VLDAGRVEQVGSPLELYN 223
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILS 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-193 |
1.39e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.17 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppergigmvfqSY------ALYPhMTVYDNmafg 99
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI----------------SYkpqyikPDYD-GTVEDL---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 lkLAKAEAKTVDEKVR-EVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIAR 178
Cdd:PRK13409 421 --LRSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170
....*....|....*
gi 491647138 179 LHERLGATMIYVTHD 193
Cdd:PRK13409 499 IAEEREATALVVDHD 513
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-212 |
2.71e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE---RGIGMV---FQSYALYPHM 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 TVYDNMA---------FGLKLAKAEAKTVDEKVREvaaaLQLDTLLARKP-KALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:COG1129 346 SIRENITlasldrlsrGGLLDRRRERALAEEYIKR----LRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 161 LSNLDaslrVQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG1129 422 TRGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
21-223 |
3.22e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 86.10 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP--ERGIGMVFQSYALYpHMTVYDNMAF 98
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTREslRKSIATVFQDAGLF-NRSIRENIRL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 99 GLKLAkaeaktVDEKVREVAAALQ-----------LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:TIGR01192 432 GREGA------TDEEVYEAAKAAAahdfilkrsngYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 168 LRVQMRMEIARLheRLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:TIGR01192 506 TEARVKNAIDAL--RKNRTTFIIAH-RLSTVRNADLVLFLDQGRLIEKGSFQELIQ 558
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-229 |
4.68e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKS----TLLRLIagleDITSGDLKIDGKVC----------NDLPPPE----R 75
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL----EQAGGLVQCDKMLLrrrsrqvielSEQSAAQmrhvR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 76 G--IGMVFQS--YALYPHMTVYDNMAFGLKL--------AKAEAKTVDEKVREVAAalqlDTLLARKPKALSGGQRQRVA 143
Cdd:PRK10261 103 GadMAMIFQEpmTSLNPVFTVGEQIAESIRLhqgasreeAMVEAKRMLDQVRIPEA----QTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 144 IGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
....*.
gi 491647138 224 HPANTF 229
Cdd:PRK10261 259 APQHPY 264
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-193 |
5.74e-18 |
|
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: 85.22 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppergigmvfqSY------ALYPhMTVYDNmafg 99
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI----------------SYkpqyisPDYD-GTVEEF---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 lkLAKAEAKTVDEKV--REVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIA 177
Cdd:COG1245 422 --LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|....*.
gi 491647138 178 RLHERLGATMIYVTHD 193
Cdd:COG1245 500 RFAENRGKTAMVVDHD 515
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-225 |
5.75e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 13 FGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE---RGIGMVFQSYALYPH 89
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNM-------------AFGLKLA---KAEAKTVDEkvrevaAALQLDTL----LA-RKPKALSGGQRQRVAIGRAI 148
Cdd:PRK11300 95 MTVIENLlvaqhqqlktglfSGLLKTPafrRAESEALDR------AATWLERVglleHAnRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 149 VREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-224 |
8.32e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--LPPPERGIGMVFQSYALYpHMTVYDNMA 97
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FglklAKAEAKTVD--EKVREVAAALQ--------LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD-A 166
Cdd:PRK11176 439 Y----ARTEQYSREqiEEAARMAYAMDfinkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDtE 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 167 SLR-VQMRMEIARlHERlgaTMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:PRK11176 515 SERaIQAALDELQ-KNR---TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
1.11e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 84.62 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAG---LED---ITSGDLKIdGKVCNDLPPPE 74
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriIYEQDLIV-ARLQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 RGigmvfqsyalyphmTVYDNMAFGL---------------------------KLAKAEAK-------TVDEKVREVAAA 120
Cdd:PRK11147 80 EG--------------TVYDFVAEGIeeqaeylkryhdishlvetdpseknlnELAKLQEQldhhnlwQLENRINEVLAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 121 LQL--DTLLArkpkALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlrvqmrmEIARLHERL---GATMIYVTHDQV 195
Cdd:PRK11147 146 LGLdpDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGFLktfQGSIIFISHDRS 214
|
250
....*....|....*..
gi 491647138 196 EAMTLATKIVVLDAGRV 212
Cdd:PRK11147 215 FIRNMATRIVDLDRGKL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
2.13e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVN--KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL--EDITSGDLKIDGK--VCNDLPPPE 74
Cdd:PRK13549 1 MMEYLLEMKNitKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEelQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 75 R-GIGMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVA---AALQLDTLLARKPKALSGGQRQRVAIGRAIVR 150
Cdd:PRK13549 81 RaGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQkllAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 151 EPKVFLFDEPLSNLDASlRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:PRK13549 161 QARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
2.24e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDiTSGDLKIDGKVCNDLPPPE----RG---------IGM-VFQSYALYPHmt 91
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLHQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 vydnmafglklAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRV-------AIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK03695 96 -----------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 165 DASLRVQMRMEIARLhERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLE 220
Cdd:PRK03695 165 DVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-214 |
2.56e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP--ERGIGMVFQSYALYPHmTVYDN 95
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLKLAKAEAKTVDEKVR--EVAAALQ--LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLR-- 169
Cdd:PRK10790 435 VTLGRDISEEQVWQALETVQlaELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEqa 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 170 VQMRMEIARLHerlgATMIYVTHdQVEAMTLATKIVVLDAGR-VEQ 214
Cdd:PRK10790 515 IQQALAAVREH----TTLVVIAH-RLSTIVEADTILVLHRGQaVEQ 555
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-211 |
2.69e-17 |
|
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: 82.95 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL--EDITSGDLKIDG---KVCNDLPPPERGIGMV 80
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGsplKASNIRDTERAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYALYPHMTVYDNMAFGLKLAKAEAKTVDE----KVREVAAALQLDTL-LARKPKALSGGQRQRVAIGRAIVREPKVF 155
Cdd:TIGR02633 84 HQELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 156 LFDEPLSNLDASlRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:TIGR02633 164 ILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-216 |
2.83e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKI---DGKVCN--DLPPPERGI------GM 79
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDlyALSEAERRRllrtewGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQSYA--LYPHMTVYDN-----MAFGLK---LAKAEAKTVDEKVrEVAAAlQLDTLlarkPKALSGGQRQRVAIGRAIV 149
Cdd:PRK11701 94 VHQHPRdgLRMQVSAGGNigerlMAVGARhygDIRATAGDWLERV-EIDAA-RIDDL----PTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 150 REPKVFLFDEPLSNLDASlrVQMRM--EIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVS--VQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-194 |
3.32e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEditsgdLKIDGKVCNDLPPPErgigmvfqsyaLYPHMTVYDNm 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------KGTPVAGCVDVPDNQ-----------FGREASLIDA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 aFGLKLAKAEAKtvdekvrEVAAALQLDT--LLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRM 174
Cdd:COG2401 106 -IGRKGDFKDAV-------ELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|
gi 491647138 175 EIARLHERLGATMIYVTHDQ 194
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-216 |
3.52e-17 |
|
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: 78.51 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 17 HVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERG-IGMVFQSYALYpHMTVYDN 95
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQRPYLF-DTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAfglklakaeaktvdekvrevaaalqldtllarkpKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMR-- 173
Cdd:cd03247 95 LG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLsl 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491647138 174 -MEIARlherlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03247 141 iFEVLK-----DKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-192 |
4.32e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.96 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIdgkvcndlpPPERGIGMVFQ-SYalyphmtvydnMAF 98
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY-----------LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 99 GLklakaeaktvdekVREVAAalqldtllarKP--KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaslrVQMRMEI 176
Cdd:cd03223 78 GT-------------LREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRL 130
|
170
....*....|....*.
gi 491647138 177 ARLHERLGATMIYVTH 192
Cdd:cd03223 131 YQLLKELGITVISVGH 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-217 |
4.44e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 83.29 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKidgkvcndlppPERGIGMVFQSyALYPHMTVYDNMAF- 98
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFf 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 99 ----GLKLAKAEaktvdeKVREVAAALQ-----LDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL- 168
Cdd:PTZ00243 745 deedAARLADAV------RVSQLEADLAqlgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 169 -RVQMRMEIARLHerlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGS 217
Cdd:PTZ00243 819 eRVVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-192 |
6.84e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMVFQSYALYPHMTVYDNMAFgl 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 101 klakAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlRVQMRMEIARLH 180
Cdd:cd03231 97 ----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA-GVARFAEAMAGH 171
|
170
....*....|..
gi 491647138 181 ERLGATMIYVTH 192
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-229 |
8.59e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKS----TLLRLIAGLEDI-TSGDLKIDGKVCNDLPPPE----RG--IGMVFQS--Y 84
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTlrgvRGnkIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFGLKL--------AKAEAKTVDEKVREVAAAlqldTLLARKPKALSGGQRQRVAIGRAIVREPKVFL 156
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLhrgmrreaARGEILNCLDRVGIRQAA----KRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 157 FDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTF 229
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
1.00e-16 |
|
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: 82.30 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppergiGMVFQSyALYPHMTVYDNMAFGLK 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 102 LAKAEAKTVDEkvrevAAALQLD---------TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQM 172
Cdd:TIGR00957 725 LNEKYYQQVLE-----ACALLPDleilpsgdrTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 173 RMEIARLHERL-GATMIYVTHDqVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR00957 800 FEHVIGPEGVLkNKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-216 |
2.69e-16 |
|
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: 77.95 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND-----LPPPERGI--- 77
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyqLSEAERRRlmr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 ---GMVFQSYALYPHMTVYDNMAFGLKLAKAEAKTVDeKVREVA----AALQLD-TLLARKPKALSGGQRQRVAIGRAIV 149
Cdd:TIGR02323 86 tewGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYG-NIRATAqdwlEEVEIDpTRIDDLPRAFSGGMQQRLQIARNLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-225 |
2.83e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.14 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE-RG-IGMVFQSYALYPHmTVYDN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLKLAKAEaktvdeKVREVA--AALQLDTLlaRKPKA-----------LSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:PRK10789 409 IALGRPDATQQ------EIEHVArlASVHDDIL--RLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 163 NLDASLRVQMRMEIARLHErlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGE--GRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-286 |
3.38e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGL---EDITSGDLKIDGKVCNdlpPPERGIGMVFQSYALYPHMTVYDNMAFG--L 100
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRiqgNNFTGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCslL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 101 KLAKAEAKTVDEKVRE-VAAALQL----DTLLARK-PKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRM 174
Cdd:PLN03211 168 RLPKSLTKQEKILVAEsVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 175 EIARLHERlGATMIYVTHD-QVEAMTLATKIVVLDAGRVEQVGSplelyNHPANTFV--AGFIGSPKMNF------LTAD 245
Cdd:PLN03211 248 TLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGK-----GSDAMAYFesVGFSPSFPMNPadflldLANG 321
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 491647138 246 IVEPGEVTTKVQIHRGQAIVVSANTIGA-KVGDPCVVGIRPE 286
Cdd:PLN03211 322 VCQTDGVSEREKPNVKQSLVASYNTLLApKVKAAIEMSHFPQ 363
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-193 |
3.96e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlppperGIGMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------RIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHM--TVYDNMAFGLKLAKAEAKTVDEKVrevaaalQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK09544 76 LYLDTTLplTVNRFLRLRPGTKKEDILPALKRV-------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|..
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGATMIYVTHD 193
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-209 |
4.77e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.00 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlppPERGIGMVFQSYALY--------PHMTV 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-------PIRRQRDEYHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKLAkaeAKTVDEKVREVAAALQLD---TLLARkpkALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlr 169
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEALWEALAQVGLAgfeDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 170 vqmrmEIARLHERL------GATMIYVTHDQVEAMTLATKIVVLDA 209
Cdd:PRK13538 164 -----GVARLEALLaqhaeqGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
5.21e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVILNKVNKTFGKVHVT-KEVD---LHINKGDFVVFVGPSGCGKSTLLRLIAGLED----ITSGDLKIDGKVCNDLPP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPfRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 73 PER------GIGMVFQS--YALYPHMTVYDNMAFGLKLAKAEAKtvdeKVREvAAALQLDTL---------LARKPKALS 135
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNK----KTRR-QRAIDLLNQvgipdpasrLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 136 GGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQV 215
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250
....*....|
gi 491647138 216 GSPLELYNHP 225
Cdd:PRK11022 236 GKAHDIFRAP 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-221 |
9.90e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 9.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 35 VGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPP--ERGIGMVFQSYALYPHMTVYDNMAFG-------LKLAKA 105
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVAIGrypwhgaLGRFGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 106 EAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGA 185
Cdd:PRK10575 123 ADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGL 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 491647138 186 TMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PRK10575 200 TVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-207 |
1.52e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlpPPERGIGMVFQSY-----ALYPHMTVYDNM 96
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGDRSRFMAYlghlpGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 AFGLKLAKAEAK-TVDEKVREVAAALQLDTLLarkpKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS-LRVQMRM 174
Cdd:PRK13543 104 HFLCGLHGRRAKqMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgITLVNRM 179
|
170 180 190
....*....|....*....|....*....|...
gi 491647138 175 EIARLHERlGATMIyVTHDQVEAMTLATKIVVL 207
Cdd:PRK13543 180 ISAHLRGG-GAALV-TTHGAYAAPPVRTRMLTL 210
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
22-212 |
1.59e-15 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 78.08 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDlppPERG-----IGMVFQSYALYPHMTVYDNm 96
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSA---DSRDdyrdlFSAIFADFHLFDDLIGPDE- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 afGLKLAKAEAKTVDEKVrEVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEI 176
Cdd:TIGR01194 437 --GEHASLDNAQQYLQRL-EIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEEL 513
|
170 180 190
....*....|....*....|....*....|....*.
gi 491647138 177 ARLHERLGATMIYVTHDQvEAMTLATKIVVLDAGRV 212
Cdd:TIGR01194 514 LPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-212 |
2.31e-15 |
|
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: 73.84 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGledITSGDLKIDGKVC-NDLPPPErgIGMVFQSYALY-- 87
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHyNGIPYKE--FAEKYPGEIIYvs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 88 ------PHMTVYDNMAFGLKLAKaeaktvDEKVREVaaalqldtllarkpkalSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:cd03233 90 eedvhfPTLTVRETLDFALRCKG------NEFVRGI-----------------SGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 162 SNLDASLRVQMRMEIARLHERLGAT-MIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-222 |
2.50e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN----DLPPPERGIGMVFQSyalyPHMTVY 93
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 -----DNMAFGLK-LAKAEaktvDEKVREVAAALQL-DTLLAR-KP-KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK13638 92 ytdidSDIAFSLRnLGVPE----AEITRRVDEALTLvDAQHFRhQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 165 DASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELY 222
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-211 |
2.53e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.28 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTF-GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLeditsgDLKIDGKVcndLPPPERGIGMVFQSY 84
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEA---RPQPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 85 ALYPHMTVYDNMAFGLklakAEAKTVDEKVREVAAAL-----QLDTLLARKPK--------------------------- 132
Cdd:TIGR03719 78 QLDPTKTVRENVEEGV----AEIKDALDRFNEISAKYaepdaDFDKLAAEQAElqeiidaadawdldsqleiamdalrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 133 -------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlrvqmrmEIA----RLHERLGaTMIYVTHDQVEAMTLA 201
Cdd:TIGR03719 154 pwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAwlerHLQEYPG-TVVAVTHDRYFLDNVA 225
|
250
....*....|
gi 491647138 202 TKIVVLDAGR 211
Cdd:TIGR03719 226 GWILELDRGR 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-208 |
3.42e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 57 SGDLKIDG-KVCN-DLPPPERGIGMVFQSYALYpHMTVYDNMAFGLKLAKAEA-------KTVDEKVREVAAalQLDTLL 127
Cdd:PTZ00265 1276 SGKILLDGvDICDyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDvkrackfAAIDEFIESLPN--KYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 128 ARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHdQVEAMTLATKIVVL 207
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVF 1431
|
.
gi 491647138 208 D 208
Cdd:PTZ00265 1432 N 1432
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-215 |
6.69e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 7 NKVNKTFGKVhvtKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcnDLPPP------ERGIGMV 80
Cdd:PRK09700 270 NVTSRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRspldavKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSY---ALYPHMTVYDNMAFGLKLAKAEAK----TVDEKVREVAAALQLDtLLARKPKA-------LSGGQRQRVAIGR 146
Cdd:PRK09700 344 TESRrdnGFFPNFSIAQNMAISRSLKDGGYKgamgLFHEVDEQRTAENQRE-LLALKCHSvnqniteLSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 147 AIVREPKVFLFDEPLSNLDaslrVQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRVEQV 215
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-222 |
7.44e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGleditsgdlkidgkvcnDLPPPERGIGMVFQSYALYPHM------TVYD 94
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVswifnaTVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 NMAFGLKLAKAE-AKTVDekvrevAAALQLD---------TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PLN03232 698 NILFGSDFESERyWRAID------VTALQHDldllpgrdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 165 DASLRVQMRMEIARlHERLGATMIYVThDQVEAMTLATKIVVLDAGRVEQVGSPLELY 222
Cdd:PLN03232 772 DAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-207 |
7.82e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.22 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 16 VHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKI-DGKVCND--LPPPERGIGMVFQ---------- 82
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDinLKWWRSKIGVVSQdpllfsnsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 ---SYALYP--------------HMTVYDNM----------------------AFGLKLAKAEAKTVDEK---------- 113
Cdd:PTZ00265 478 nniKYSLYSlkdlealsnyynedGNDSQENKnkrnscrakcagdlndmsnttdSNELIEMRKNYQTIKDSevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 114 VREVAAAL--QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVT 191
Cdd:PTZ00265 558 IHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250
....*....|....*.
gi 491647138 192 HdQVEAMTLATKIVVL 207
Cdd:PTZ00265 638 H-RLSTIRYANTIFVL 652
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-195 |
8.68e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.29 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMVFQSYALYPHMTVYDNMAF 98
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 99 GLKLAKAeAKTVDEKVRevaaALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaSLRVQMRMEIAR 178
Cdd:PRK13540 98 DIHFSPG-AVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSLLTIITKIQ 171
|
170
....*....|....*..
gi 491647138 179 LHERLGATMIYVTHDQV 195
Cdd:PRK13540 172 EHRAKGGAVLLTSHQDL 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-193 |
1.62e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppERGigmVFQSY--ALYPHMTVYDNMAFGlkla 103
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL-------EVA---YFDQHraELDPEKTVMDNLAEG---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 104 KAEAkTVDEKVREVAAALQlDTLL----ARKP-KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaslrvqmrMEIAR 178
Cdd:PRK11147 408 KQEV-MVNGRPRHVLGYLQ-DFLFhpkrAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD--------VETLE 477
|
170
....*....|....*....
gi 491647138 179 LHERLGA----TMIYVTHD 193
Cdd:PRK11147 478 LLEELLDsyqgTVLLVSHD 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
1.62e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCnDLPPPERGI--GMVF-----QSYALYPHMTVYD 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIraGIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 NMA---------FGLKL-AKAEAKTVDEKVRevaaALQLDTLLARKP-KALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:PRK11288 351 NINisarrhhlrAGCLInNRWEAENADRFIR----SLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 164 LDaslrVQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK11288 427 ID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-212 |
4.48e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER---GIGMV---FQSYALYPHMTVY 93
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLVPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFG------------LKLAKAEAKTvDEKVRE--VAAAlQLDTllarKPKALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:COG3845 355 ENLILGryrrppfsrggfLDRKAIRAFA-EELIEEfdVRTP-GPDT----PARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 160 PLSNLDASlrvqmrmEIARLHERL------GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:COG3845 429 PTRGLDVG-------AIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-223 |
5.98e-14 |
|
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: 73.41 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlpppergIGMVFQSYALYPHmTVYDNMA 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLklakaeakTVDE-KVREVAAALQLD---TLLARKPK--------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:TIGR01271 509 FGL--------SYDEyRYTSVIKACQLEediALFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 166 ASLRVQMrMEIARLHERLGATMIYVThDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:TIGR01271 581 VVTEKEI-FESCLCKLMSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQA 636
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-194 |
6.16e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.83 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 12 TFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLE--DITSGDLKIDGKVCNDLPPPER---GIGMVFQsyal 86
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQ---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 87 YP-HMTVYDNMAFgLKLA-----KAEAKT-VD-----EKVREVAAALQLD-TLLARK-PKALSGGQRQRVAIGRAIVREP 152
Cdd:CHL00131 92 YPiEIPGVSNADF-LRLAynskrKFQGLPeLDpleflEIINEKLKLVGMDpSFLSRNvNEGFSGGEKKRNEILQMALLDS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491647138 153 KVFLFDEPLSNLDASLRVQMRMEIARLhERLGATMIYVTHDQ 194
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQ 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-225 |
6.74e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED----ITSGDLKIDGKVCNDLPPPER------GIGMVFQ- 82
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 -SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQL---------DTLLARKPKALSGGQRQRVAIGRAIVREP 152
Cdd:COG4170 98 pSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELlhrvgikdhKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 153 KVFLFDEPLSNLDASLRVQmrmeIARLHERL----GATMIYVTHDqVEAMT-LATKIVVLDAGRVEQVGSPLELYNHP 225
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQ----IFRLLARLnqlqGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-210 |
6.78e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.05 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDitsgdlKIDGKVCNDLPPPERGIGMVFQSYALYP-----------H 89
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ------TLEGKVHWSNKNESEPSFEATRSRNRYSvayaaqkpwllN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAFGLKLAKAEAKTVDEkvrevAAALQLD---------TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEP 160
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTD-----ACSLQPDidllpfgdqTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491647138 161 LSNLDASLRVQMRME-IARLHERLGATMIYVTHdQVEAMTLATKIVVLDAG 210
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-218 |
6.87e-14 |
|
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: 69.75 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN--DLPPPERGIGMVFQSYALYPHmTVYDN 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MafglklaKAEAKTVDEKVREvaaALQLdtllARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL----DASLRVQ 171
Cdd:cd03369 102 L-------DPFDEYSDEEIYG---ALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491647138 172 MRMEIArlherlGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:cd03369 168 IREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-223 |
8.06e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 71.04 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvcndlpppergIGMVFQSYALYPHmTVYDNMA 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLklakaeakTVDE-KVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:cd03291 120 FGV--------SYDEyRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 166 ASLRVQMrMEIARLHERLGATMIYVThDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:cd03291 192 VFTEKEI-FESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-226 |
1.38e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKS-----TLLRLIAGLEDiTSGDLKIDGKVCNDLPPPERGIGMVFQS--YALYPHMTVYD 94
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 NmafGLKLAKAEAKTVDEKV-REVAAALQLD---TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASlrV 170
Cdd:PRK10418 101 H---ARETCLALGKPADDATlTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV--A 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 171 QMRM--EIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPA 226
Cdd:PRK10418 176 QARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-235 |
2.51e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVC--NDLPPPERgIGMVFQSYALYPHMTVYDNMAFG 99
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRR-VGYMSQAFSLYGELTVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLR---VQMRMEI 176
Cdd:NF033858 364 ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARdmfWRLLIEL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 177 ARlheRLGATmIYV-THDQVEAMtLATKIVVLDAGRVEQVGSPLELY-NHPANTFVAGFIG 235
Cdd:NF033858 444 SR---EDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAALVaARGAATLEEAFIA 499
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-193 |
2.68e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 68.93 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 29 GDFVVFVGPSGCGKSTLLRLIAGleditsgDLKID-GKVCNdlPPPERGIGMVFQSYALYPHMTVYDNMafGLKLAKAEA 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAG-------KLKPNlGKFDD--PPDWDEILDEFRGSELQNYFTKLLEG--DVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 108 ------KTVDEKVRE-------------VAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDasl 168
Cdd:cd03236 95 yvdlipKAVKGKVGEllkkkdergkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--- 171
|
170 180
....*....|....*....|....*...
gi 491647138 169 rVQMRMEIARLHERL---GATMIYVTHD 193
Cdd:cd03236 172 -IKQRLNAARLIRELaedDNYVLVVEHD 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-193 |
3.12e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.97 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 28 KGDFVVFVGPSGCGKSTLLRliagledITSGDLKID-GKVcnDLPPPERGIGMVFQSYALYPHMT-VYDNmafGLKLA-- 103
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALK-------ILSGELKPNlGDY--DEEPSWDEVLKRFRGTELQDYFKkLANG---EIKVAhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 104 -----------KAEA----KTVDE--KVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDa 166
Cdd:COG1245 166 pqyvdlipkvfKGTVrellEKVDErgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD- 244
|
170 180 190
....*....|....*....|....*....|
gi 491647138 167 slrVQMRMEIARLHERL---GATMIYVTHD 193
Cdd:COG1245 245 ---IYQRLNVARLIRELaeeGKYVLVVEHD 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
108-193 |
3.35e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 108 KTVDE--KVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaslrVQMRMEIARLHERL-- 183
Cdd:PRK13409 185 KKVDErgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD----IRQRLNVARLIRELae 260
|
90
....*....|
gi 491647138 184 GATMIYVTHD 193
Cdd:PRK13409 261 GKYVLVVEHD 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-223 |
7.13e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGleditsgdlkidgkvcnDLPPPERGIGMVFQSYALYPHM------TVYDN 95
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVPQVswifnaTVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLKLAKAE-AKTVDekvrevAAALQLD---------TLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PLN03130 699 ILFGSPFDPERyERAID------VTALQHDldllpggdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 166 ASLRVQMRMEIARlHERLGATMIYVThDQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:PLN03130 773 AHVGRQVFDKCIK-DELRGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-169 |
7.17e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 66.82 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 36 GPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPErgIGMVFQSYALYPHMTVYDNMAFGLKLAKAeAKTVDEKVR 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFENLKFWSEIYNS-AETLYAAIH 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491647138 116 evaaALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLR 169
Cdd:PRK13541 110 ----YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-211 |
1.54e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.60 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCN---DLPPPERGIGMVFQSYA 85
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKA----EAKTVDEkVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTKGmfvdQDKMYRD-TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 162 SNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-193 |
4.50e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 1 MAEVI--LNKVNKTFG-KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLeditsgDLKIDGKVcndLPPPERGI 77
Cdd:PRK11819 2 MAQYIytMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKEFEGEA---RPAPGIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 78 GMVFQSYALYPHMTVYDN-------------------MAFGL------KLAKAEAK-----------TVDEKVrEVAA-A 120
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENveegvaevkaaldrfneiyAAYAEpdadfdALAAEQGElqeiidaadawDLDSQL-EIAMdA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 121 LQL---DTllarKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAslrvqmrmE-IA----RLHERLGaTMIYVTH 192
Cdd:PRK11819 152 LRCppwDA----KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsVAwleqFLHDYPG-TVVAVTH 218
|
.
gi 491647138 193 D 193
Cdd:PRK11819 219 D 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-167 |
7.68e-12 |
|
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: 63.80 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLED--ITSGDLKIDGKvcndlPPPE---RGIGMVFQSYALYPHMTVYDNMAFGL 100
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR-----PLDKnfqRSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 101 KLakaeaktvdekvrevaaalqldtllarkpKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDAS 167
Cdd:cd03232 105 LL-----------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
1.19e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlppperGIGMVFQ- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA---------NIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPH-MTVYDNMAfglklAKAEAKTVDEKVREVaaalqLDTLL-----ARKP-KALSGGQRQRVAIGRAIVREPKVF 155
Cdd:PRK15064 391 HAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGT-----LGRLLfsqddIKKSvKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 156 LFDEPLSNLDaslrvqmrME-IARLH---ERLGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK15064 461 VMDEPTNHMD--------MEsIESLNmalEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-208 |
1.35e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.59 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLhINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvcndlpppergigmvfqsyalyphm 90
Cdd:cd03222 8 KRYGVFFLLVELGV-VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 91 tvydnmafglklakaeaktvdekvrevaaalqldTLLARKPK--ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASL 168
Cdd:cd03222 61 ----------------------------------ITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ 106
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLD 208
Cdd:cd03222 107 RLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-193 |
3.55e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 2 AEVILNKVNKTFGKVHVT-KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDlPPPERGIGMV 80
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTAlRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 81 FQSYAL---YP-------HMTVYDNMAFgLKLAKAEAKtvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVR 150
Cdd:PRK15056 84 PQSEEVdwsFPvlvedvvMMGRYGHMGW-LRRAKKRDR---QIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 151 EPKVFLFDEPLSNLDaslrVQMRMEIARLHERL---GATMIYVTHD 193
Cdd:PRK15056 160 QGQVILLDEPFTGVD----VKTEARIISLLRELrdeGKTMLVSTHN 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-221 |
3.83e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDG----------KVCND---L 70
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrrAVCPRiayM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 71 PppeRGIGMvfqsyALYPHMTVYDNMAF-----GlkLAKAEAktvDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIG 145
Cdd:NF033858 82 P---QGLGK-----NLYPTLSVFENLDFfgrlfG--QDAAER---RRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 146 RAIVREPKVFLFDEPLSNLDASLRVQMRMEIARL-HERLGATMIYVThdqveA-MTLATK---IVVLDAGRVEQVGSPLE 220
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVAT-----AyMEEAERfdwLVAMDAGRVLATGTPAE 223
|
.
gi 491647138 221 L 221
Cdd:NF033858 224 L 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-212 |
4.92e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPErGI--GMVFQSY-----ALYPHMTV 92
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLanGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMA---------FGLKL-AKAEAKTVDEKVRevaaALQLDTLLARKP-KALSGGQRQRVAIGRAIVREPKVFLFDEPL 161
Cdd:PRK10762 348 KENMSltalryfsrAGGSLkHADEQQAVSDFIR----LFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491647138 162 SNLDaslrVQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK10762 424 RGVD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-218 |
5.61e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGleDIT----------SGDLKIDGKVCNDLPPPE----RGIgMVFQS 83
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAPRlarlRAV-LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPhMTVYDNMAFGLKLAKAEAKTVDEKVREVA-AALQL---DTLLARKPKALSGGQRQRVAIGRAI---------VR 150
Cdd:PRK13547 93 QPAFA-FSAREIVLLGRYPHARRAGALTHRDGEIAwQALALagaTALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 151 EPKVFLFDEPLSNLDASLRVQMRMEIARLHE--RLGATMIyvTHDQVEAMTLATKIVVLDAGRVEQVGSP 218
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAI--VHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-216 |
1.48e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.99 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 4 VILNKVNKTFgkvHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppergiGMVFQS 83
Cdd:PRK13546 28 LIPKHKNKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-----------SVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 YALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSN 163
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491647138 164 LDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVG 216
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-192 |
1.64e-10 |
|
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: 62.46 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKvCNDLPPPER---GIGmVFQSYALYPhMTVYDNMA 97
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-GKLFYVPQRpymTLG-TLRDQIIYP-DSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLKlakaeaktvDEKVREVAAALQLDTLLARK---------PKALSGGQRQRVAIGRAIVREPKVFLFDEPLSnldaSL 168
Cdd:TIGR00954 547 RGLS---------DKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS----AV 613
|
170 180
....*....|....*....|....
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTH 192
Cdd:TIGR00954 614 SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-211 |
2.36e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGleDITSGDLKIDGKVC-NDLPPPErgIGMVFQSYALY------ 87
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITyDGITPEE--IKKHYRGDVVYnaetdv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 88 --PHMTVYDNMAFG--LKLAKAEAKTVDEKVRE------VAAALQLDTLLARKP-----KALSGGQRQRVAIGRAIVREP 152
Cdd:TIGR00956 149 hfPHLTVGETLDFAarCKTPQNRPDGVSREEYAkhiadvYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 153 KVFLFDEPLSNLDASlrvqMRMEIAR-LHE--RLGATMIYVTHDQV--EAMTLATKIVVLDAGR 211
Cdd:TIGR00956 229 KIQCWDNATRGLDSA----TALEFIRaLKTsaNILDTTPLVAIYQCsqDAYELFDKVIVLYEGY 288
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-215 |
3.38e-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: 61.35 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDfVVF-VGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndLPPPERG-----IGMVFQSYALYPHmtvydn 95
Cdd:COG4615 351 IDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDR------ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 mafglkLAKAEAKTVDEKVREVAAALQLDTLLARK-----PKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRv 170
Cdd:COG4615 421 ------LLGLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR- 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491647138 171 qmRM---EIarLHE--RLGATMIYVTHDQvEAMTLATKIVVLDAGRVEQV 215
Cdd:COG4615 494 --RVfytEL--LPElkARGKTVIAISHDD-RYFDLADRVLKMDYGKLVEL 538
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-221 |
6.24e-10 |
|
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: 61.11 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLppperGIGMVFQSYALYPHMTVYDNMA 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-----GLHDLRFKITIIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGLKLAKAEAKTvDEKVREVAAALQLDTLLARKP-----------KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD- 165
Cdd:TIGR00957 1376 LRMNLDPFSQYS-DEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDl 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491647138 166 -------ASLRVQMR-MEIARLHERLGATMIYvthdqveamtlaTKIVVLDAGRVEQVGSPLEL 221
Cdd:TIGR00957 1455 etdnliqSTIRTQFEdCTVLTIAHRLNTIMDY------------TRVIVLDKGEVAEFGAPSNL 1506
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-204 |
9.31e-10 |
|
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: 56.61 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 28 KGDFVVFVGPSGCGKSTLLRLIAGLeditsgdlkidgkvcndLPPPERGIgmvfqsyalyphmtVYDNMafglklakaea 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-----------------LGPPGGGV--------------IYIDG----------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 108 ktvdEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEI-----ARLHER 182
Cdd:smart00382 39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSE 114
|
170 180
....*....|....*....|..
gi 491647138 183 LGATMIYVTHDQVEAMTLATKI 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-165 |
1.21e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 7 NKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlppperGIGMVFQSY-A 85
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVDQSRdA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFG---LKLAKAEA-----------KTVDEKvrevaaalqldtllaRKPKALSGGQRQRVAIGRAIVRE 151
Cdd:TIGR03719 397 LDPNKTVWEEISGGldiIKLGKREIpsrayvgrfnfKGSDQQ---------------KKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....
gi 491647138 152 PKVFLFDEPLSNLD 165
Cdd:TIGR03719 462 GNVLLLDEPTNDLD 475
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-193 |
1.36e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE--RGIGMVFQSYALYPHMTVYDNMAFG 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQLLGPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKTVD--EKVRevaaaLQLDTLLARKpkaLSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIA 177
Cdd:PRK10522 422 PALVEKWLERLKmaHKLE-----LEDGRISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLL 493
|
170
....*....|....*.
gi 491647138 178 RLHERLGATMIYVTHD 193
Cdd:PRK10522 494 PLLQEMGKTIFAISHD 509
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-242 |
1.61e-09 |
|
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: 60.03 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGK-VCNDLPPPERGIGMVFQSYALYPHMTVYDNMAFGLKLAK 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 105 AEAKTVDEKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIARLhERLG 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREG 2120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 185 ATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTFVAGF-IGSPKMNFL 242
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLL 2179
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-166 |
3.20e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED---ITSGDLKIDGkvcndlpPP-----ERGIGMVFQSYALYPHMT 91
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNG-------RPldssfQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 VYDNMAFGLKLAKAEAKTVDEKVREVAAALQL-------DTLLARKPKALSGGQRQRVAIGRAIVREPKVFLF-DEPLSN 163
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLlemesyaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSG 932
|
...
gi 491647138 164 LDA 166
Cdd:TIGR00956 933 LDS 935
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-229 |
4.38e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 35 VGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvCN----DLPPPERGIGMVFQSYALYPHMTVYDNMAF------GL--KL 102
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDvakfGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFsehndaDLweAL 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 103 AKAEAKTVDEKvrevaAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDasLRVQMRMEIARLHER 182
Cdd:PLN03232 1346 ERAHIKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRTDSLIQRTIREEF 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491647138 183 LGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTF 229
Cdd:PLN03232 1419 KSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-288 |
4.51e-09 |
|
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: 51.82 E-value: 4.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491647138 235 GSPKMNFLTADIVEPGEVT----TKVQIHRGQAIVVsantiGAKVGDPCVVGIRPEHI 288
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVlgggVTLPLPEGQVLAL-----KLYVGKEVILGIRPEHI 53
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-223 |
5.09e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.79 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 9 VNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDiTSGDLKIDGKVCNDLPPPE--RGIGMVFQSYAL 86
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 87 YPHmTVYDNMAFGLKLAKAEAKTVDEKV--REVAAAL--QLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLS 162
Cdd:cd03289 89 FSG-TFRKNLDPYGKWSDEEIWKVAEEVglKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 163 NLDaSLRVQMRMEIARlHERLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:cd03289 168 HLD-PITYQVIRKTLK-QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-210 |
6.00e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 6 LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPP---PERGIGMVFQ 82
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 83 SYALYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAaalqlDTLLAR-----KPKALSG----GQRQRVAIGRAIVREPK 153
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEA-----DKLLARlnlrfSSDKLVGelsiGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491647138 154 VFLFDEPLSNL----DASL-RVqmrmeIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAG 210
Cdd:PRK10762 162 VIIMDEPTDALtdteTESLfRV-----IRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-234 |
1.48e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED----ITSGDLKIDGKVCNDLPPPER------GIGMVFQS 83
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 84 yalyPHMTVYDNMAFGLKLAKA----------------EAKTVDEKVREVAAALQLDtLLARKPKALSGGQRQRVAIGRA 147
Cdd:PRK15093 98 ----PQSCLDPSERVGRQLMQNipgwtykgrwwqrfgwRKRRAIELLHRVGIKDHKD-AMRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 148 IVREPKVFLFDEPLSNLDASLRVQMRMEIARLHERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPAN 227
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
....*..
gi 491647138 228 TFVAGFI 234
Cdd:PRK15093 253 PYTQALI 259
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
100-221 |
2.24e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 LKLAKAEAKTvdeKVREVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIaRL 179
Cdd:NF000106 114 LDLSRKDARA---RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RS 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491647138 180 HERLGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:NF000106 190 MVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-165 |
2.34e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED--ITSGDLKIDGKVCNDLPPPER---GIGMVFQsyalYPHMTV 92
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKLAKAEAKTVDEK-----------VREVAAALQL-DTLLARKPK-ALSGGQRQRVAIGRAIVREPKVFLFDE 159
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRGQepldrfdfqdlMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDE 171
|
....*.
gi 491647138 160 PLSNLD 165
Cdd:PRK09580 172 SDSGLD 177
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-229 |
3.53e-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: 54.14 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLP--PPERGIGMVFQSYALYPhmtvyDN 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLKlakAEAKTVDEKVREVAAALQLDTLLARKPKAL-----------SGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:cd03288 111 IRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491647138 165 D-ASLRVQMRMEIARLHERLGATMIYVTHDQVEamtlATKIVVLDAGRVEQVGSPLELYNHPANTF 229
Cdd:cd03288 188 DmATENILQKVVMTAFADRTVVTIAHRVSTILD----ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-208 |
4.43e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 23 DLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLkidgkvCNDLPPP-----ERGIGMVFQSYALYPH-MTVYDNM 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER------QSQFSHItrlsfEQLQKLVSDEWQRNNTdMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 97 AFGLKLAKAEAKTVDEKVR--EVAAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRM 174
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDPARceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190
....*....|....*....|....*....|....
gi 491647138 175 EIARLHERlGATMIYVTHDQVEAMTLATKIVVLD 208
Cdd:PRK10938 177 LLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLA 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-229 |
4.65e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCND--LPPPERGIGMVFQSYALYPHmTVYDN 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MAFGLKLAKAeaktvdekvrEVAAALQLDTLLAR--------KPKALSG------GQRQRVAIGRAIVREPKVF-LFDEP 160
Cdd:PTZ00243 1404 VDPFLEASSA----------EVWAALELVGLRERvasesegiDSRVLEGgsnysvGQRQLMCMARALLKKGSGFiLMDEA 1473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 161 LSNLDASLRVQMRmeiARLHERLGA-TMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYNHPANTF 229
Cdd:PTZ00243 1474 TANIDPALDRQIQ---ATVMSAFSAyTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-165 |
8.82e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 32 VVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPERGIGMVFQSYALyphmtvydnmafgLKLAKAEAKTVD 111
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPL-------------LYMMRCFPGVPE 604
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 112 EKVREVAAALQLDTLLARKPK-ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-165 |
9.33e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 35 VGPSGCGKSTLLRLIAG------LEDIT-------SGDLKIDGKvcndlpppeRGIGMVfqSYALypHM------TVYDN 95
Cdd:PRK10938 292 VGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrrgSGETIWDIK---------KHIGYV--SSSL--HLdyrvstSVRNV 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 96 MAFGLKLAKAEAKTVDEKVREVA----AALQLDTLLARKP-KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLD 165
Cdd:PRK10938 359 ILSGFFDSIGIYQAVSDRQQKLAqqwlDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-166 |
1.51e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLED--ITSGDLKIDGkvcndLPPPE----RGIGMVFQSYALYP 88
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG-----FPKKQetfaRISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 89 HMTVYDNMAFG--LKLAKAEAKtvDEK---VREVAAALQLDTL---LARKP--KALSGGQRQRVAIGRAIVREPKVFLFD 158
Cdd:PLN03140 967 QVTVRESLIYSafLRLPKEVSK--EEKmmfVDEVMELVELDNLkdaIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*...
gi 491647138 159 EPLSNLDA 166
Cdd:PLN03140 1045 EPTSGLDA 1052
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-216 |
1.55e-07 |
|
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: 50.78 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRliAGLEdiTSGDLKIdgkvcNDLPPpergigmvfqsyALYPHMTVYd 94
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARL-----ISFLP------------KFSRNKLIF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 95 nmafglklakaeaktVDekvrevaaalQLDTL---------LARKPKALSGGQRQRVAIGRAIVREPK--VFLFDEPLSN 163
Cdd:cd03238 65 ---------------ID----------QLQFLidvglgyltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491647138 164 LDASLRVQMRMEIARLHErLGATMIYVTHDqVEAMTLATKIVVLDAGRVEQVG 216
Cdd:cd03238 120 LHQQDINQLLEVIKGLID-LGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGG 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-165 |
2.51e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVI-LNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCndlpppergIGMVF 81
Cdd:PRK11819 323 KVIeAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK---------LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 82 QSY-ALYPHMTVYDNMAFGL---KLAKAEAKTvdekvREVAAAL-------QldtllaRKPKALSGGQRQRVAIGRAIVR 150
Cdd:PRK11819 394 QSRdALDPNKTVWEEISGGLdiiKVGNREIPS-----RAYVGRFnfkggdqQ------KKVGVLSGGERNRLHLAKTLKQ 462
|
170
....*....|....*
gi 491647138 151 EPKVFLFDEPLSNLD 165
Cdd:PRK11819 463 GGNVLLLDEPTNDLD 477
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-212 |
3.07e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPER-GIGMVF-----QSYALYPHMT-- 91
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 92 ------VYDNMAFGLKLAKaEAKTVdEKVRevaAALQLDTLLARKP-KALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:PRK15439 360 wnvcalTHNRRGFWIKPAR-ENAVL-ERYR---RALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491647138 165 DASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-212 |
5.02e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 3 EVILNKVNKTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVCNDLPPPE---RGIGM 79
Cdd:PRK10982 248 EVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 80 VFQ---SYALYPHMTV-YDNMAFGLKLAKAEAKTVDEKVREVAAALQLDTLLARKPK------ALSGGQRQRVAIGRAIV 149
Cdd:PRK10982 328 VTEerrSTGIYAYLDIgFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491647138 150 REPKVFLFDEPLSNLDASLRVQMRMEIARLHERlGATMIYVTHDQVEAMTLATKIVVLDAGRV 212
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-223 |
6.33e-07 |
|
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: 51.45 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 18 VTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDiTSGDLKIDGKVCND--LPPPERGIGMVFQSYALYPHmTVYDN 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvtLQTWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 96 MafglklaKAEAKTVDEKVREVAAALQLDTLLARKPK-----------ALSGGQRQRVAIGRAIVREPKVFLFDEPLSNL 164
Cdd:TIGR01271 1312 L-------DPYEQWSDEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 165 DASLRVQMRMEIArlHERLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLELYN 223
Cdd:TIGR01271 1385 DPVTLQIIRKTLK--QSFSNCTVILSEH-RVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-221 |
1.13e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 26 INKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGkvCN-------DLpppERGIGMVFQSYALYPHmTVYDNM-A 97
Cdd:PLN03130 1262 ISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDiskfglmDL---RKVLGIIPQAPVLFSG-TVRFNLdP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 98 FGL--------KLAKAEAKTVdekVREvaAALQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLR 169
Cdd:PLN03130 1336 FNEhndadlweSLERAHLKDV---IRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491647138 170 VQMRMEIArlHERLGATMIYVTHdQVEAMTLATKIVVLDAGRVEQVGSPLEL 221
Cdd:PLN03130 1411 ALIQKTIR--EEFKSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-211 |
1.36e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 11 KTFGKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITS--GDLKIDGKVCN--DLPPPE-RGIGMVFQSYA 85
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfkDIRDSEaLGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 86 LYPHMTVYDNMAFGLKLAKAEAKTVDEKVREVAAalqldtLLAR-----KPKALSG----GQRQRVAIGRAIVREPKVFL 156
Cdd:NF040905 89 LIPYLSIAENIFLGNERAKRGVIDWNETNRRARE------LLAKvgldeSPDTLVTdigvGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491647138 157 FDEPLSNLDASlrvqmrmEIARLHERL------GATMIYVTHDQVEAMTLATKIVVLDAGR 211
Cdd:NF040905 163 LDEPTAALNEE-------DSAALLDLLlelkaqGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-224 |
1.66e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 22 VDLHINKGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDLKIDGKVcndlpppergiGMVFQSYALYPHMTVYDNMAF-GL 100
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIENIELkGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 101 K--LAKAEAKTVDEKVREVAaalQLDTLLARKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDASLRVQMRMEIAR 178
Cdd:PRK13545 112 MmgLTKEKIKEIIPEIIEFA---DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491647138 179 LHERlGATMIYVTHDQVEAMTLATKIVVLDAGRVEQVGSPLELYNH 224
Cdd:PRK13545 189 FKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
281-354 |
3.38e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 44.53 E-value: 3.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491647138 281 VGIRPEHIRFGEKDAIQEGgvTLSVVEQLGNECLMYFNTPQSAEPVVIRT-EGQTNIRAGDKRCIEFPADYCHLF 354
Cdd:pfam08402 1 LAIRPEKIRLAAAANGLSG--TVTDVEYLGDHTRYHVELAGGEELVVRVPnAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-213 |
1.55e-05 |
|
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: 46.74 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 21 EVDLHINKGDFVVFVGPSGCGKSTLLRLIAGL-EDITSGDLKIDGKVCNDLPPP---ERGIGMVFQS---YALYPHMTVY 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 DNMAFGL-----KLAKAEAKTVDEKVREVAAALQLDTLLARKPKA-LSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDas 167
Cdd:TIGR02633 358 KNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD-- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491647138 168 lrVQMRMEIARLHERL---GATMIYVTHDQVEAMTLATKIVVLDAGRVE 213
Cdd:TIGR02633 436 --VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-207 |
8.97e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 8.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491647138 129 RKPKALSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDasLRVQMRMEIARLheRLGATMIYVTHDQVEAMTLATKIVVL 207
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLL--KWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
15-205 |
1.36e-04 |
|
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: 42.63 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTL----------LRLIAGLE-------------DITSgdlkIDGkvcndLP 71
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSayarqflgqmdkpDVDS----IEG-----LS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 72 PperGIGMVFQSYALYPHMTV------YDnmAFGLKLAKAEAKTVDEKVREVAaalqLDTL-LARKPKALSGGQRQRVAI 144
Cdd:cd03270 78 P---AIAIDQKTTSRNPRSTVgtvteiYD--YLRLLFARVGIRERLGFLVDVG----LGYLtLSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 145 GRAI------VrepkVFLFDEPLSNLDASLRVQMRMEIARLHErLGATMIYVTHDQvEAMTLATKIV 205
Cdd:cd03270 149 ATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDE-DTIRAADHVI 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
57-212 |
1.57e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 57 SGDLKIDGKVCNDLPPPE---RGIGMVFQS---YALYPHMTVYDNMA---------FGLKLAKAEAKTVDEKVREvaaaL 121
Cdd:PRK13549 317 EGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITlaaldrftgGSRIDDAAELKTILESIQR----L 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 122 QLDTLLARKPKA-LSGGQRQRVAIGRAIVREPKVFLFDEPLSNLDaslrVQMRMEIARLHERL---GATMIYVTHDQVEA 197
Cdd:PRK13549 393 KVKTASPELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPEV 468
|
170
....*....|....*
gi 491647138 198 MTLATKIVVLDAGRV 212
Cdd:PRK13549 469 LGLSDRVLVMHEGKL 483
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-193 |
1.77e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 31 FVVFVGPSGCGKSTLlrlIAGLEDITSGDLKIDGKVCNDLPPP-----ERG-IGMVFQS-----YALYPHMTVYDNMAFg 99
Cdd:cd03240 24 LTLIVGQNGAGKTTI---IEALKYALTGELPPNSKGGAHDPKLiregeVRAqVKLAFENangkkYTITRSLAILENVIF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 100 lklakaeaktvdekVREVaaalQLDTLLARKPKALSGGQRQ------RVAIGRAI-VREPKVFLfDEPLSNLDA-SLRVQ 171
Cdd:cd03240 100 --------------CHQG----ESNWPLLDMRGRCSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEeNIEES 160
|
170 180
....*....|....*....|..
gi 491647138 172 MRMEIARLHERLGATMIYVTHD 193
Cdd:cd03240 161 LAEIIEERKSQKNFQLIVITHD 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-225 |
2.20e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 90 MTVYDNMAF--GLKLAKAEAKTVDEKVREVAAALQ------LDTL-LARKPKALSGGQRQRVA----IGRAIVrePKVFL 156
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLGflidvgLDYLsLSRAAGTLSGGEAQRIRlatqIGSGLT--GVLYV 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491647138 157 FDEPLSNLDAslRVQMRM--EIARLHErLGATMIYVTHDQvEAMTLATKIVVL------DAGRVEQVGSPLELYNHP 225
Cdd:TIGR00630 514 LDEPSIGLHQ--RDNRRLinTLKRLRD-LGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEILANP 586
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-205 |
2.38e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 14 GKVHVTKEVDLHINKGDFVVFVGPSGCGKSTLLRLIAgleditsgdlkidgkvcndlpppergigmvfqsyalyphmtvy 93
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 94 dnMAFGLKlAKAEAKTVDEKVREVAAALQLDTLLARKpkALSGGQRQRVAI-----GRAIVREPkVFLFDEPLSNLDaSL 168
Cdd:cd03227 43 --LALGGA-QSATRRRSGVKAGCIVAAVSAELIFTRL--QLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLD-PR 115
|
170 180 190
....*....|....*....|....*....|....*..
gi 491647138 169 RVQMRMEIARLHERLGATMIYVTHDQvEAMTLATKIV 205
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
20-60 |
1.56e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 1.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 491647138 20 KEVDLHInkGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDL 60
Cdd:COG4637 14 RDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
15-45 |
2.22e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|.
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTL 45
Cdd:TIGR00630 8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-59 |
2.36e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|..
gi 491647138 28 KGDFVVFVGPSGCGKSTLLRLIAGLEDITSGD 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGE 115
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
15-45 |
3.34e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 3.34e-03
10 20 30
....*....|....*....|....*....|.
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTL 45
Cdd:COG0178 12 REHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-60 |
3.93e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 3.93e-03
10 20 30
....*....|....*....|....*....|...
gi 491647138 28 KGDFVVFVGPSGCGKSTLLRLIAGLEDITSGDL 60
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
31-54 |
8.82e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 8.82e-03
10 20
....*....|....*....|....*
gi 491647138 31 FVVFVGPSGCGKSTLLR-LIAGLED 54
Cdd:COG3267 45 FVVLTGEVGTGKTTLLRrLLERLPD 69
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-248 |
9.68e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 20 KEVDLHINKgDFVVFVGPSGCGKSTLLRLIAG-LEDITSGDLKI-DGKVCNDLPPPERGIGMVFQSY-----ALYPHMTV 92
Cdd:COG3593 15 KDLSIELSD-DLTVLVGENNSGKSSILEALRLlLGPSSSRKFDEeDFYLGDDPDLPEIEIELTFGSLlsrllRLLLKEED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 93 YDNMAFGLKLAKAEA----KTVDEKVREV------AAALQLDTLLARKPKALSG------------------GQRQRV-- 142
Cdd:COG3593 94 KEELEEALEELNEELkealKALNELLSEYlkelldGLDLELELSLDELEDLLKSlslriedgkelpldrlgsGFQRLIll 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647138 143 AIGRAIVR-----EPKVFLFDEPlsnlDASLRVQMRMEIARL---HERLGATMIYVTH-----DQVEamtlATKIVVLDA 209
Cdd:COG3593 174 ALLSALAElkrapANPILLIEEP----EAHLHPQAQRRLLKLlkeLSEKPNQVIITTHsphllSEVP----LENIRRLRR 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 491647138 210 GRVEQVGSPLELYNHPANTFVAGFIGSPKMNFLTAD---IVE 248
Cdd:COG3593 246 DSGGTTSTKLIDLDDEDLRKLLRYLGVTRSELLFARkviLVE 287
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
15-45 |
9.71e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|.
gi 491647138 15 KVHVTKEVDLHINKGDFVVFVGPSGCGKSTL 45
Cdd:PRK00349 12 REHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| |
