|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-353 |
2.92e-178 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 498.08 E-value: 2.92e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQ 87
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVGC 247
Cdd:COG3842 165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 248 EVirLDGPDAMVRVGGIDYRLSAGNARL--GPAKLAVRPGSISISQPGGQG-VAGRVLHCAYLGGHVEYEVETEIGTLFI 324
Cdd:COG3842 245 TV--LGDEGGGVRTGGRTLEVPADAGLAagGPVTVAIRPEDIRLSPEGPENgLPGTVEDVVFLGSHVRYRVRLGDGQELV 322
|
330 340 350
....*....|....*....|....*....|.
gi 1028514096 325 ID--HMAETGLPPASDVTLGFRNRGIALIQA 353
Cdd:COG3842 323 VRvpNRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-350 |
2.59e-154 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 437.20 E-value: 2.59e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVF 86
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGE--ANV 244
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 245 VGCEVIrldgpDAMVRVGGIDYRLSAGNARL--GPAKLAVRPGSISISQPGGQGVAGRVLHCAYLGGHVEYEVETEiGTL 322
Cdd:COG3839 242 LPGTVE-----GGGVRLGGVRLPLPAALAAAagGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLG-GQE 315
|
330 340
....*....|....*....|....*...
gi 1028514096 323 FIIDHMAETGLPPASDVTLGFRNRGIAL 350
Cdd:COG3839 316 LVARVPGDTRLRPGDTVRLAFDPERLHL 343
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-345 |
2.16e-137 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 394.13 E-value: 2.16e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV-TMLPANERDVSMVF 86
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVG 246
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 247 CEVIrldgpDAMVRVGGIDYRLSAGNARlGPAKLAVRPGSISIS--QPGGQGVAGRVLHCAYLGGHVEYEVETEIGTLFI 324
Cdd:COG1118 242 GRVI-----GGQLEADGLTLPVAEPLPD-GPAVAGVRPHDIEVSrePEGENTFPATVARVSELGPEVRVELKLEDGEGQP 315
|
330 340
....*....|....*....|....*..
gi 1028514096 325 I------DHMAETGLPPASDVTLGFRN 345
Cdd:COG1118 316 LeaevtkEAWAELGLAPGDPVYLRPRP 342
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-315 |
1.84e-133 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 384.46 E-value: 1.84e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQS 88
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVGCe 248
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA- 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 249 viRLDGpdAMVRVGGidYRLSAGNARL-----GPAKLAVRPGSISISQPGGQGVAGRVLHCAYLGGHveYEV 315
Cdd:PRK11432 246 --TLSG--DYVDIYG--YRLPRPAAFAfnlpdGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQ--YEV 309
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-332 |
2.13e-127 |
|
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: 368.98 E-value: 2.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALF 92
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 PHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:TIGR03265 89 PNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 173 LRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVGCEVirl 252
Cdd:TIGR03265 169 VREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTR--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 253 dGPDAMVRVGGIDYRLSAGNARLGPA-KLAVRPGSISISQPGGQ--GVAGRVLHCAYLGG--HVEYEVETEIGTLFIIDH 327
Cdd:TIGR03265 246 -GGGSRARVGGLTLACAPGLAQPGASvRLAVRPEDIRVSPAGNAanLLLARVEDMEFLGAfyRLRLRLEGLPGQALVADV 324
|
....*
gi 1028514096 328 MAETG 332
Cdd:TIGR03265 325 SASEV 329
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-240 |
9.15e-127 |
|
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: 362.71 E-value: 9.15e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQS 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMG 240
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-320 |
4.43e-125 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 363.88 E-value: 4.43e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQS 88
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVGCE 248
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 249 VI-RLDGPDAMVRVGGI------DYRLSAGnARLgpaKLAVRPGSISISQ----PGGQGVAGRVLHCAYLGGHVEYEVET 317
Cdd:PRK09452 255 VIeRLDEQRVRANVEGRecniyvNFAVEPG-QKL---HVLLRPEDLRVEEinddEHAEGLIGYVRERNYKGMTLDSVVEL 330
|
...
gi 1028514096 318 EIG 320
Cdd:PRK09452 331 ENG 333
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-221 |
5.50e-117 |
|
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: 337.18 E-value: 5.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQS 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-221 |
9.16e-110 |
|
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: 319.20 E-value: 9.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQS 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-241 |
9.70e-109 |
|
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: 317.36 E-value: 9.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQ 87
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQ----SSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGE 241
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-308 |
2.73e-105 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 312.93 E-value: 2.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVF 86
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGE----- 241
Cdd:PRK11650 163 SNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpamnl 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 242 -ANVVGCEVIRLDGPDAMVRVGGIDYRLSAGnarlGPAKLAVRPGSISISqPGGQGVAGRVLHCAYLG 308
Cdd:PRK11650 243 lDGRVSADGAAFELAGGIALPLGGGYRQYAG----RKLTLGIRPEHIALS-SAEGGVPLTVDTVELLG 305
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-325 |
1.08e-101 |
|
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: 302.88 E-value: 1.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 39 LLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREK 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 119 AEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHD 198
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 199 QDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVGCEVIRLDGpDAMVRVGGIDYRLSAGNARLGPA 278
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKS-EQVVLAGVEGRRCDIYTDVPVEK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 279 K----LAVRPGSISISQ----PGGQGVAGRVLHCAYLGGHVEYEVETEIGTLFII 325
Cdd:TIGR01187 240 DqplhVVLRPEKIVIEEedeaNSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLV 294
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
13-245 |
1.46e-101 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 299.02 E-value: 1.46e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALF 92
Cdd:TIGR00968 5 NISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 PHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 173 LRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVV 245
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-215 |
4.69e-101 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 298.54 E-value: 4.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 3 SVKPGSVTFKNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPan 78
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 eRDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:COG1116 80 -PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDG 215
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-290 |
5.70e-97 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 291.60 E-value: 5.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQ 87
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRK----AEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEAN 243
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVN 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 244 vvgceviRLDGpdaMVR-----VGGIDYRLSAGNARLGPAKLAVRPGSISIS 290
Cdd:PRK10851 242 -------RLQG---TIRggqfhVGAHRWPLGYTPAYQGPVDLFLRPWEVDIS 283
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-241 |
3.07e-96 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 288.14 E-value: 3.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVF 86
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL--AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDE 164
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 165 PLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGE 241
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
8-350 |
1.07e-94 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 286.12 E-value: 1.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFT----AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT-----MLPAN 78
Cdd:NF040933 2 TVRVENVTKIFKKGKkevvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVAspgkiIVPPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 ERDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:NF040933 82 DRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADF 238
Cdd:NF040933 162 VLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 239 MGEANVVGCEVIRldgpDAMVRVGGIDYRLSAGNARLGPAKLAVRPGSISIS-----QPGGQGVAG--RVLHCAYLGGHV 311
Cdd:NF040933 242 IGDINLLEGKVEE----EGLVDGNDLKIPLPNPKLEAGEVIIGIRPEDIDISesdmrLPPGFVEVGkgRVKVSSYAGGVF 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 1028514096 312 EYEVETEIGTLFIIDHMAETGLPPASDVTLGFRNRGIAL 350
Cdd:NF040933 318 RVVVSPIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKI 356
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-212 |
1.67e-93 |
|
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: 277.82 E-value: 1.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG----AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPaneRDVSM 84
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDE 164
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1028514096 165 PLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVM 212
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-240 |
3.34e-93 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 282.69 E-value: 3.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQ 87
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMG 240
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
12-291 |
4.70e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 271.18 E-value: 4.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTaIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYAL 91
Cdd:NF040840 5 ENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 92 FPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:NF040840 84 FPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 172 RLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVV-GceVI 250
Cdd:NF040840 164 QTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIeG--VA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1028514096 251 RLDGPDAMVRVGGIdyRLSAGNARLGPAKLAVRPGSISISQ 291
Cdd:NF040840 242 EKGGEGTILDTGNI--KIELPEEKKGKVRIGIRPEDITIST 280
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-240 |
2.09e-88 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 265.70 E-value: 2.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN----ERDVSM 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYGL-QSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMG 240
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-322 |
8.44e-88 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 269.01 E-value: 8.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYAL 91
Cdd:PRK11607 23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 92 FPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:PRK11607 103 FPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 172 RLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVGCeVIR 251
Cdd:PRK11607 183 KLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG-VLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 252 LDGPDAMV-RVGGIDYRL----SAGNARLGPAKLAVRPGSI----SISQPGGQGVAGRVLHCAYLGGHVEYEVETEIGTL 322
Cdd:PRK11607 262 ERQEDGLViDSPGLVHPLkvdaDASVVDNVPVHVALRPEKImlceEPPADGCNFAVGEVIHIAYLGDLSIYHVRLKSGQM 341
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-241 |
1.53e-87 |
|
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: 263.78 E-value: 1.53e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGA-FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMV 85
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL--AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGE 241
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-238 |
3.50e-86 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 265.04 E-value: 3.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE------RDVSMVFQ 87
Cdd:COG4175 33 ILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:COG4175 113 HFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADF 238
Cdd:COG4175 193 ALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADF 263
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-238 |
2.45e-85 |
|
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: 259.11 E-value: 2.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE------RDVSMVFQ 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADF 238
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-239 |
2.21e-84 |
|
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: 255.29 E-value: 2.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD-----VS 83
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMTALDNVAYGL-QSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPaSAFIADFM 239
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-217 |
1.20e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 250.35 E-value: 1.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG----AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD--- 81
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 ---VSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQdEALAVSDRIIVMKDGEI 217
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-217 |
5.89e-82 |
|
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: 248.56 E-value: 5.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGA----FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD--- 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 ---VSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAvSDRIIVMKDGEI 217
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-244 |
9.81e-82 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 248.40 E-value: 9.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTaIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALF 92
Cdd:cd03299 5 NLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 PHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 173 LRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANV 244
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-241 |
3.50e-78 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 239.27 E-value: 3.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTFGAFTAipDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSY 89
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 90 ALFPHMTALDNVAYGLqSSGLR-KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:COG3840 81 NLFPHLTVAQNIGLGL-RPGLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGE 241
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-233 |
5.41e-77 |
|
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: 245.58 E-value: 5.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF-----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE---- 79
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQ--SYALFPHMTALDNVAYGLQSSG-LRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASA 233
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-216 |
7.62e-77 |
|
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: 234.00 E-value: 7.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT----MLPANERDVSM 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYGLqssglrkaearekaeeglklvglagmghrlpaelSGGQQQRVAVARALVLEPQVLLLDE 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 165 PLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-239 |
1.41e-74 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 230.36 E-value: 1.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDV----SM 84
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYG-LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFM 239
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-230 |
1.68e-74 |
|
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: 229.91 E-value: 1.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMV 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQS--YALFpHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
16-245 |
4.35e-74 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 233.59 E-value: 4.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 16 KTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT------MLPANERDVSMVFQSY 89
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqspveLREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 90 ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNL 169
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 170 DARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVV 245
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLS 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-217 |
7.95e-74 |
|
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: 227.41 E-value: 7.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN----ERDVSM 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYGL-QSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-226 |
9.26e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.02 E-value: 9.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD-VSMVFQ 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-324 |
9.44e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.50 E-value: 9.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE----- 79
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFM 239
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 240 GeanvvgcEVIRLDGPDAMVR------VGGIDYRLS-AGNARLGP--AKLAVRPG-SISIsqpggqgvagrvlhcayLGG 309
Cdd:COG1135 242 P-------TVLNDELPEELLArlreaaGGGRLVRLTfVGESADEPllSELARRFGvDVNI-----------------LSG 297
|
330
....*....|....*
gi 1028514096 310 HVEYEVETEIGTLFI 324
Cdd:COG1135 298 GIEEIQGTPVGRLIV 312
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-226 |
1.12e-71 |
|
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: 222.76 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVS 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMTALDNVAYGL-QSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-230 |
3.70e-70 |
|
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: 218.99 E-value: 3.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG----AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE----- 79
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
13-290 |
6.43e-68 |
|
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: 217.28 E-value: 6.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAipDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD---QD---VTMLPANERDVSMVF 86
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDsarGIFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSSglRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANVVG 246
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1028514096 247 CEVIRLDGPDAM--VRVGGIDYRLSAGNARLG-PAKLAVRPGSISIS 290
Cdd:COG4148 242 ATVAAHDPDYGLtrLALGGGRLWVPRLDLPPGtRVRVRIRARDVSLA 288
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-222 |
9.50e-68 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 212.22 E-value: 9.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDV 82
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGA 222
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-216 |
2.85e-67 |
|
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: 210.79 E-value: 2.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTF--GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVF 86
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QsyalFP-HM----TALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLL 161
Cdd:cd03225 82 Q----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-226 |
6.92e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 211.07 E-value: 6.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDV 82
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGL--QSSGLR------KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgRTSTWRsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-221 |
1.16e-66 |
|
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: 209.67 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT-----MLPANE 79
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSY--ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL---AGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-240 |
1.36e-65 |
|
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: 207.73 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKtfgAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM--LPAN 78
Cdd:COG1124 1 MLEVRNLSVSYGQGGR---RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 ERDVSMVFQSY--ALFPHMTALDNVAYGLQSSGLRKAEARekAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVL 155
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFI 235
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....*
gi 1028514096 236 ADFMG 240
Cdd:COG1124 236 RELLA 240
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-212 |
9.00e-65 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 205.87 E-value: 9.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlPANERDVsmVFQSYALFPHMTALDNVA 102
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--VFQKDALLPWLNVLDNVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIR 182
Cdd:COG4525 99 FGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178
|
170 180 190
....*....|....*....|....*....|
gi 1028514096 183 ELQQRLGFTAVYVTHDQDEALAVSDRIIVM 212
Cdd:COG4525 179 DVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-226 |
6.87e-64 |
|
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: 203.35 E-value: 6.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVF 86
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYG----LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-212 |
2.00e-63 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 200.79 E-value: 2.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP---TSGRILIGDQDVTMLPANERDVSM 84
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYGLqSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDE 164
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1028514096 165 PLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSdRIIVM 212
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDL 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-227 |
3.51e-63 |
|
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: 202.30 E-value: 3.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGA-----FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE---- 79
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQ--SYALFpHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVL 155
Cdd:TIGR04521 81 rKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-221 |
8.53e-63 |
|
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: 199.44 E-value: 8.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGAFTAipDLSLTIePGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD------QDVTMLPANERDVSMVFQ 87
Cdd:cd03297 6 IEKRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQssGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:cd03297 83 QYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
1.01e-62 |
|
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: 200.08 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKpgsvtfkNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP-ANE 79
Cdd:COG4555 1 MIEVE-------NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPrEAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-226 |
1.19e-62 |
|
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: 199.33 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEH-----PTSGRILIGDQDVTMLPANE----RD 81
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPhMTALDNVAYGLQSSGLR-KAEAREKAEEGLKLVGLAG-MGHRLPA-ELSGGQQQRVAVARALVLEPQ 158
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDeVKDRLHAlGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLgfTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-229 |
3.73e-61 |
|
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: 195.86 E-value: 3.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTFGA-FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVS 83
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMTALDNVAYG-------LQS-SGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVL 155
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGrlgrrstWRSlFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-217 |
5.02e-61 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 194.65 E-value: 5.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQ 87
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPhMTALDNVAYGLQSSGLRkaEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERK--FDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-239 |
5.15e-61 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 195.62 E-value: 5.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQ--DVTMLPANE------ 79
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKairllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDN-VAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGApRELYEAPASAFIADF 238
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239
|
.
gi 1028514096 239 M 239
Cdd:COG4161 240 L 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
7.83e-61 |
|
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: 194.96 E-value: 7.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLp 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 77 aNE--------RDVSMVFQSYALFPHMTALDNVAYGLQSSGLRkaEAREKAEEGLKLVGLagmGHRL---PAELSGGQQQ 145
Cdd:COG4181 80 -DEdararlraRHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGL---GHRLdhyPAQLSGGEQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 146 RVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
8.84e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 203.21 E-value: 8.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNvrktfGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPT---SGRILIGDQDVTMLPA 77
Cdd:COG1123 4 LLEVRDLSVRYPG-----GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 78 NER--DVSMVFQS--YALFPhMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARAL 153
Cdd:COG1123 79 ALRgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPAS 232
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-225 |
1.02e-60 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 195.26 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:COG0411 8 RGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVA--------YGLQSSGLR-------KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARAL 153
Cdd:COG0411 88 PRLFPELTVLENVLvaaharlgRGLLAALLRlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
1.20e-60 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 195.40 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM------ 74
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 75 --LPANERDV-------SMVFQSYALFPHMTALDNVAYG-LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQ 144
Cdd:COG4598 81 elVPADRRQLqrirtrlGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 145 QRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPR 224
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*
gi 1028514096 225 ELYEAPASAFIADFM 239
Cdd:COG4598 240 EVFGNPKSERLRQFL 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-225 |
1.75e-60 |
|
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: 194.19 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSG----------LRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:cd03219 84 PRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-239 |
5.06e-60 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 193.31 E-value: 5.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQ--DVTMLPANE------ 79
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKairelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDN-VAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQ 158
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGApRELYEAPASAFIADF 238
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNY 239
|
.
gi 1028514096 239 M 239
Cdd:PRK11124 240 L 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-231 |
1.43e-58 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 192.25 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 15 RKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVSMVFQ-S 88
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YA-LFPHMTALDNVAYGLQSSGL-RKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:COG4608 105 YAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqdeaLAV----SDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:COG4608 185 VSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-231 |
4.70e-58 |
|
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: 190.65 E-value: 4.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP---TSGRILIGDQDVTMLPANE----- 79
Cdd:COG0444 5 RNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElrkir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQ-SY-ALFPHMTALDNVAYGLQS-SGLRKAEAREKAEEGLKLVGLAGMGHRL---PAELSGGQQQRVAVARA 152
Cdd:COG0444 85 gREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:COG0444 165 LALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-229 |
7.33e-58 |
|
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: 187.51 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFG-AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVSM 84
Cdd:TIGR02315 4 VENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYG-------LQSS-GLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLE 156
Cdd:TIGR02315 84 IFQHYNLIERLTVLENVLHGrlgykptWRSLlGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 157 PQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-217 |
4.24e-57 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 186.04 E-value: 4.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDqdvTMLPANERDVSMVFQS 88
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLqssglrKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-221 |
4.59e-57 |
|
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: 184.62 E-value: 4.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALFPHMTALDNVAYGL 105
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 qSSGLR-KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIREL 184
Cdd:cd03298 96 -SPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1028514096 185 QQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-237 |
4.48e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 186.16 E-value: 4.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE----- 79
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP----ASAFI 235
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREFI 241
|
..
gi 1028514096 236 AD 237
Cdd:PRK11153 242 QS 243
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-227 |
1.94e-55 |
|
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: 182.24 E-value: 1.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDvTMLPANERD----VSMVFQSyalfPH---- 94
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLWEirkkVGMVFQN----PDnqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 -MTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARL 173
Cdd:TIGR04520 92 gATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 174 RRRVRTEIRELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:TIGR04520 172 RKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-230 |
2.35e-55 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 181.49 E-value: 2.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD----------QDVTMLPAN 78
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 ERDVSMVFQSYALFPHMTALDNVAYG-LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-216 |
2.39e-55 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 180.14 E-value: 2.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDV 82
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
9-230 |
2.47e-55 |
|
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: 181.57 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILI-GDQDVTM-------LPANER 80
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHMpgrngplVPADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 -------DVSMVFQSYALFPHMTALDNVAYG-LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARA 152
Cdd:TIGR03005 81 hlrqmrnKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQP 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-221 |
5.38e-55 |
|
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: 179.97 E-value: 5.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 24 IPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlPANERDVsmVFQSYALFPHMTALDNVAY 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 104 GLQS--SGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEI 181
Cdd:TIGR01184 78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1028514096 182 RELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-217 |
7.95e-55 |
|
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: 177.20 E-value: 7.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-ERDVSMVFQSYA 90
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 91 LFPHMTALDNVayglqssglrkaearekaeeglklvglagmghrlpaELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:cd03230 84 LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1028514096 171 ARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03230 128 PESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-233 |
1.12e-54 |
|
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: 187.20 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 15 RKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLeHPTSGRILIGDQDVTMLPANE-----RDVSMVFQS- 88
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YA-LFPHMTALDNVAYGL--QSSGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDE 164
Cdd:COG4172 372 FGsLSPRMTVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 165 PLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqdeaLAV----SDRIIVMKDGEIAQSGAPRELYEAPASA 233
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHD----LAVvralAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-238 |
1.89e-54 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 183.70 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE------RDVSMVFQSYALF 92
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 PHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 173 LRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADF 238
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-226 |
2.25e-54 |
|
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: 177.70 E-value: 2.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG--AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV-TMLPANERDVSMV 85
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQRLgfTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-226 |
3.10e-54 |
|
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: 177.56 E-value: 3.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-ERDVSMVFQSYA 90
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 91 LFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 171 ARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-225 |
2.05e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.05 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlpANERDVSMVFQS 88
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR---RARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YAL---FPhMTALDNVAYGLQSS----GLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLL 161
Cdd:COG1121 84 AEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAqSGAPRE 225
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEE 224
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
12-238 |
2.71e-53 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 175.95 E-value: 2.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-----EHPTSGRILIGDQDVTmlpANERDVS--- 83
Cdd:TIGR00972 5 ENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIY---DKKIDVVelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 ----MVFQSYALFPhMTALDNVAYGLQSSGLR-KAEAREKAEEGLKLVGL----AGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:TIGR00972 82 rrvgMVFQKPNPFP-MSIYDNIAYGPRLHGIKdKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlgFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAF 234
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....
gi 1028514096 235 IADF 238
Cdd:TIGR00972 239 TEDY 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-221 |
6.72e-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: 173.89 E-value: 6.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 28 SLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALFPHMTALDNVAYGLQS 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 108 SGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQR 187
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 1028514096 188 LGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-217 |
1.91e-52 |
|
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: 172.59 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGA-FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDV 82
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-231 |
5.43e-52 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 174.05 E-value: 5.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFT-----AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM------LPA 77
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 78 NERDVSMVFQsyalFP-HM----TALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVAR 151
Cdd:PRK13634 83 LRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-215 |
9.53e-52 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 172.19 E-value: 9.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlPANERDVsmVFQSYALFPHMTALDNVA 102
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIR 182
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLL 172
|
170 180 190
....*....|....*....|....*....|...
gi 1028514096 183 ELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDG 215
Cdd:PRK11248 173 KLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-233 |
2.72e-51 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 170.15 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 28 SLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQSYALFPHMTALDNVAYGLqS 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL-N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 108 SGLR-KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQ 186
Cdd:PRK10771 98 PGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1028514096 187 RLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY--EAPASA 233
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLsgKASASA 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-216 |
5.48e-51 |
|
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: 167.04 E-value: 5.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT--MLPANERDVSMVFQ 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAklPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 syalfphmtaldnvayglqssglrkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-229 |
2.32e-50 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 178.49 E-value: 2.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGAFT--AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:COG2274 472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFpHMTALDNVAYGLQSSGLrkaearEKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVAR 151
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLGDPDATD------EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHDqDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-167 |
3.04e-50 |
|
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: 164.74 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHMTALDNVAY 103
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 104 GLQSSGLRKAEAREKAEEGLKLVGLAGMGHRL----PAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-221 |
3.72e-50 |
|
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: 165.69 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERdvsmvfqsyal 91
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 92 fphmtaLDNVAYGLQSsglrkaearekaeegLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:cd03214 72 ------ARKIAYVPQA---------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1028514096 172 RLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03214 131 AHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
23-217 |
8.70e-50 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 166.05 E-value: 8.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD------VSMVFQSYALFPHMT 96
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrrelIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 97 ALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRR 176
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1028514096 177 VRTEIRELQQRlGFTAVYVTHdQDEALAVSDRIIVMKDGEI 217
Cdd:NF038007 180 VLQQLKYINQK-GTTIIMVTH-SDEASTYGNRIINMKDGKL 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-221 |
2.03e-49 |
|
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: 164.63 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPaneRDVSMVFQSYA 90
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 91 L---FPhMTALDNVAYGL--QSSGLR--KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:cd03235 79 IdrdFP-ISVRDVVLMGLygHKGLFRrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMkDGEIAQSG 221
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-322 |
9.64e-49 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 167.60 E-value: 9.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAipDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD---QDV---TMLPANERDVSMVF 86
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSrkgIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSSglRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIAdFMGEANVVG 246
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQGSLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 247 CEVIRLDGPDAM--VRVGGIDYRLSAGNARLG-PAKLAVRPGSISISQPGGQGVAGR-VLHCAYLG------GHVEYEVE 316
Cdd:TIGR02142 239 GVVAEHDQHYGLtaLRLGGGHLWVPENLGPTGaRLRLRVPARDVSLALQKPEATSIRnILPARVVEiedsdiGRVGVVLE 318
|
....*.
gi 1028514096 317 TEIGTL 322
Cdd:TIGR02142 319 SGGKTL 324
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-218 |
1.94e-48 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 162.50 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVSMVFQSYALFPHMTALDN 100
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlrRRIGYIFQAHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 VAYGLQ-SSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRT 179
Cdd:TIGR02982 103 VQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVE 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1028514096 180 EIRELQQRLGFTAVYVTHDqDEALAVSDRIIVMKDGEIA 218
Cdd:TIGR02982 183 LMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-218 |
2.23e-48 |
|
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: 162.52 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF--GAFTAI--PDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER------D 81
Cdd:TIGR02211 5 ENLGKRYqeGKLDTRvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLagmGHRL---PAELSGGQQQRVAVARALVLEPQ 158
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGL---EHRInhrPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqDEALAVSDRIIVMKDGEIA 218
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD-LELAKKLDRVLEMKDGQLF 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-228 |
2.52e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 161.72 E-value: 2.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPAN----ERDVSMVFQSY-ALFPHMTA 97
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETvwdvRRQVGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 98 LDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRV 177
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 178 RTEIRELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-227 |
2.58e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 161.75 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD 81
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 ----VSMVFQ--SYALFPHMTALDnVAYGLQSSGLRKAEAREKAEEGLKLVGLA--GMGHRLPAELSGGQQQRVAVARAL 153
Cdd:PRK13637 81 irkkVGLVFQypEYQLFEETIEKD-IAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-239 |
4.18e-47 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 160.52 E-value: 4.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDV---------- 82
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 -----SMVFQSYALFPHMTALDNVAYG-LQSSGLRKAEAREKAEEGLKLVGLAGMGH-RLPAELSGGQQQRVAVARALVL 155
Cdd:PRK10619 90 lrtrlTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFI 235
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
....
gi 1028514096 236 ADFM 239
Cdd:PRK10619 249 QQFL 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-226 |
5.80e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 167.65 E-value: 5.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKNVrkTF---GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN 78
Cdd:COG1132 333 LPPVRGEIEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 E--RDVSMVFQSYALFpHMTALDNVAYGlqssglrKAEA-REKAEEGLKLVGLAGMGHRLP-----------AELSGGQQ 144
Cdd:COG1132 411 SlrRQIGVVPQDTFLF-SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 145 QRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTH------DqdealavSDRIIVMKDGEIA 218
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHrlstirN-------ADRILVLDDGRIV 553
|
....*...
gi 1028514096 219 QSGAPREL 226
Cdd:COG1132 554 EQGTHEEL 561
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-230 |
6.15e-47 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 159.82 E-value: 6.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRML-------AGLEhpTSGRILIGDQ-------DVTMLpa 77
Cdd:COG1117 15 RNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEdiydpdvDVVEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 78 nERDVSMVFQSYALFPhMTALDNVAYGLQSSGLR-KAEAREKAEEGLKLVGLAG-MGHRL--PA-ELSGGQQQRVAVARA 152
Cdd:COG1117 91 -RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALWDeVKDRLkkSAlGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlgFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-214 |
6.86e-47 |
|
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: 158.03 E-value: 6.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-ERDVSMVFQ 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEARekAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAvsDRIIVMKD 214
Cdd:COG4133 161 ALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAA--ARVLDLGD 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-227 |
8.16e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 160.28 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPAN----ERDVSMVFQSY-ALFPHMTALDN 100
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENvwdiRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 VAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTE 180
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1028514096 181 IRELQQRLGFTAVYVTHDQDEaLAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-210 |
8.65e-46 |
|
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: 155.08 E-value: 8.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTML---PANE--RD-VSMV 85
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnskKASKfrREkLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQdEALAVSDRII 210
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-226 |
1.56e-45 |
|
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: 154.90 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQssGLRKAEAREKAEEGLKLV-GLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:cd03224 84 RRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-217 |
1.75e-45 |
|
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: 154.36 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPANERDVSMVFQS 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1028514096 169 LDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-221 |
1.90e-45 |
|
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: 154.83 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKTFgafTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-E 79
Cdd:cd03266 1 MITADALTKRFRDVKKTV---QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELqQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-231 |
2.24e-45 |
|
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: 155.01 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQSY 89
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 90 ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNL 169
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 170 DARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:cd03218 165 DPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-216 |
7.49e-45 |
|
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: 151.38 E-value: 7.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVrkTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:cd03228 1 IEFKNV--SFsypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFpHMTALDNVayglqssglrkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLL 162
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHDqDEALAVSDRIIVMKDGE 216
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-226 |
8.85e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 155.27 E-value: 8.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-------ER 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 dvsmvfqsyALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVL 160
Cdd:COG4152 81 ---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 161 LLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-230 |
1.21e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 153.26 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 169 LDARLRRRVRTEIRELQQR-LGftaVYVT-HDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:COG1137 167 VDPIAVADIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-219 |
1.88e-44 |
|
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: 153.81 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 22 TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP-----ANERDVSMVFQ-SYALF-PH 94
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqrrAFRRDVQLVFQdSPSAVnPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 MTALDNVAYGLQS-SGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:TIGR02769 105 MTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1028514096 173 LRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQ 219
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-226 |
1.99e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 159.41 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPANERD-----VS 83
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDaqaagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMTALDNVAYGLQSSG---LRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVL 160
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 161 LLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-229 |
2.12e-44 |
|
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: 160.31 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 6 PGSVTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:COG4988 334 PPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFpHMTALDNVAYGlqssglrKAEA-REKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVA 150
Cdd:COG4988 414 AWVPQNPYLF-AGTIRENLRLG-------RPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHDqDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-228 |
4.40e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 152.98 E-value: 4.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFT-----AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--- 79
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 ---RDVSMVFQsyalFPHM-----TALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLA-GMGHRLPAELSGGQQQRVAVA 150
Cdd:PRK13649 82 qirKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-221 |
4.68e-43 |
|
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: 148.11 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVtLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD-VSMVFQSYA 90
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 91 LFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:cd03264 83 VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 171 ARLRRRVrteiRELQQRLGFTAVYV--THDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03264 163 PEERIRF----RNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-230 |
5.48e-43 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 149.60 E-value: 5.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF---------GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER-- 80
Cdd:COG4167 8 RNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRck 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 DVSMVFQ--SYALFPHMTA---LD-----NvayglqsSGLRKAEAREKAEEGLKLVGLAGmGHRL--PAELSGGQQQRVA 148
Cdd:COG4167 88 HIRMIFQdpNTSLNPRLNIgqiLEeplrlN-------TDLTAEEREERIFATLRLVGLLP-EHANfyPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 149 VARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
..
gi 1028514096 229 AP 230
Cdd:COG4167 240 NP 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-218 |
8.02e-43 |
|
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: 146.03 E-value: 8.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTML-P--ANERDVSMV 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPrdARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQsyalfphmtaldnvayglqssglrkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-225 |
1.98e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 147.95 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE----RDVsmVFQ 87
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYAL-FPhMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALV-------LEPQV 159
Cdd:COG4559 83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-217 |
2.29e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 148.30 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP-----ANERDVSMVFQ 87
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SY--ALFPHMTALDNVAYGLQS-SGLRKAEAREKAEEGLKLVGLA-GMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:PRK10419 97 DSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-231 |
2.52e-42 |
|
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: 154.92 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 5 KPGSVTFKNVRKTF--GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--R 80
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 DVSMVFQSYALFpHMTALDNVAYGlqssglrKAEA-REKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVA 148
Cdd:COG4987 410 RIAVVPQRPHLF-DTTLRENLRLA-------RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 149 VARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHDQdEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLA 558
|
...
gi 1028514096 229 APA 231
Cdd:COG4987 559 QNG 561
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-225 |
2.88e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 147.61 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSY 89
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 90 AL-FPhMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALV------LEPQVLLL 162
Cdd:PRK13548 86 SLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-226 |
3.19e-42 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 147.15 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKpgsvtfkNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE- 79
Cdd:COG4604 1 MIEIK-------NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQSYALFPHMTALDNVAYGL--QSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLE 156
Cdd:COG4604 74 aKRLAILRQENHINSRLTVRELVAFGRfpYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 157 PQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-231 |
4.46e-42 |
|
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: 146.28 E-value: 4.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQSYALFPHM 95
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 96 TALDNvaygLQSsGLRKAEAREKAEEGLKLVG-----LAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:COG0410 94 TVEEN----LLL-GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 171 ARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:COG0410 169 PLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-231 |
7.52e-42 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 149.25 E-value: 7.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGaftaipDLSLTIE---PGTLVT-LLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQ---DVTM---LPANERDV 82
Cdd:PRK11144 5 NFKQQLG------DLCLTVNltlPAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLqssglrkaeAREKAEEGLKLVGLAGMGH---RLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK11144 79 GYVFQDARLFPHYKVRGNLRYGM---------AKSMVAQFDKIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-219 |
8.87e-42 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 145.73 E-value: 8.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPA------NERDVSMVFQSYALFPHMTALD 99
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRT 179
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1028514096 180 EIRELQQRLGFTAVYVTHDQDEALAVSdRIIVMKDGEIAQ 219
Cdd:PRK11629 187 LLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-231 |
1.16e-41 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 152.53 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFknvRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTT----LRMLAGLEHPTSGRILIGDQDVTMLPANE---- 79
Cdd:COG4172 13 SVAF---GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 --RDVSMVFQ--SYALFPHMTALDNVAYGLQ-SSGLRKAEAREKAEEGLKLVGLAGMGHRL---PAELSGGQQQRVAVAR 151
Cdd:COG4172 90 rgNRIAMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqdeaLAV----SDRIIVMKDGEIAQSGAPRELY 227
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIVEQGPTAELF 245
|
....
gi 1028514096 228 EAPA 231
Cdd:COG4172 246 AAPQ 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-229 |
2.61e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 150.95 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTML-P--ANERDVSMV 85
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsPrdAIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYGLQSSG---LRKAEAREKAEE-----GLKlVGLagmgHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRElseryGLD-VDP----DAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 158 QVLLLDEPLSNLdarlrrrvrT--EIRELQQRL------GFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:COG3845 161 RILILDEPTAVL---------TpqEADELFEILrrlaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-221 |
1.13e-40 |
|
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: 141.97 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFQS 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKAEarekAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 169 LDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-217 |
2.27e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 142.92 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFT-----AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER--DVSM 84
Cdd:COG1101 5 KNLSKTFNPGTvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYAL--FPHMTALDNVA--------YGLqSSGLRKAEaREKAEEGLKLVGLaGMGHRLPAE---LSGGQQQRVAVAR 151
Cdd:COG1101 85 VFQDPMMgtAPSMTIEENLAlayrrgkrRGL-RRGLTKKR-RELFRELLATLGL-GLENRLDTKvglLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-226 |
2.99e-40 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 142.15 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGriligdQDVTML-----PANERD-- 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLFgerrgGEDVWElr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 -----VSMVFQSYaLFPHMTALDNVAYGLQSS-GLRK---AEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARA 152
Cdd:COG1119 78 kriglVSPALQLR-FPRDETVLDVVLSGFFDSiGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-226 |
3.63e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.57 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPANERD----VSMVFQSY--ALFPhMT 96
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWvrskVGLVFQDPddQVFS-ST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 97 ALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRR 176
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1028514096 177 VRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:PRK13647 177 LMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-230 |
4.10e-40 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 141.64 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSG-LRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 168 NLDARLRRRVRTEIRELQQR-LGftaVYVT-HDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKERgIG---VLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-217 |
6.70e-40 |
|
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: 139.70 E-value: 6.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDvtmLPANER--DVSMVFQS--YALFPHmTALDNV 101
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERrkSIGYVMQDvdYQLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 102 AYGLQssglRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEI 181
Cdd:cd03226 94 LLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELI 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1028514096 182 RELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03226 170 RELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-226 |
3.13e-39 |
|
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: 138.90 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVrkTFG---AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT--MLPANERDVS 83
Cdd:cd03253 1 IEFENV--TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFpHMTALDNVAYG-LQSSGLRKAEAREKA------------------EEGLKlvglagmghrlpaeLSGGQQ 144
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGrPDATDEEVIEAAKAAqihdkimrfpdgydtivgERGLK--------------LSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 145 QRVAVARALVLEPQVLLLDEPLSNLDarlrrrVRTEiRELQQRL-----GFTAVYVTHDQDEaLAVSDRIIVMKDGEIAQ 219
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALD------THTE-REIQAALrdvskGRTTIVIAHRLST-IVNADKIIVLKDGRIVE 215
|
....*..
gi 1028514096 220 SGAPREL 226
Cdd:cd03253 216 RGTHEEL 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-230 |
9.76e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 140.48 E-value: 9.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVSMVFQS-YA-LFPHM 95
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 96 TALDNVAYGLQ-SSGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARL 173
Cdd:PRK11308 110 KVGQILEEPLLiNTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 174 RRRVRTEIRELQQRLGFTAVYVTHDqdeaLAV----SDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHD----LSVvehiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-215 |
1.47e-38 |
|
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: 137.18 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF------GA-FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILI--GDQDVTMLPANERDV 82
Cdd:COG4778 8 ENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 --------SMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAgmgHRL----PAELSGGQQQRVAVA 150
Cdd:COG4778 88 lalrrrtiGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLP---ERLwdlpPATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDG 215
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
8-230 |
2.78e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 138.04 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFT-----AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--- 79
Cdd:PRK13641 2 SIKFENVDYIYSPGTpmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 ---RDVSMVFQsyalFPHM-----TALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLA-GMGHRLPAELSGGQQQRVAVA 150
Cdd:PRK13641 82 klrKKVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVrTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-227 |
3.62e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.53 E-value: 3.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKpgSVTFKNVRKTFGAFT-AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDvTMLPANE 79
Cdd:PRK13633 4 MIKCK--NVSYKYESNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDV----SMVFQSyalfPhmtalDN----------VAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQ 145
Cdd:PRK13633 81 WDIrnkaGMVFQN----P-----DNqivativeedVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 146 RVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKE 230
|
..
gi 1028514096 226 LY 227
Cdd:PRK13633 231 IF 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-228 |
6.01e-38 |
|
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: 142.25 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF-----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGR--ILIGDQ--DVTMLPANERD- 81
Cdd:TIGR03269 283 RNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDGRGr 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 ----VSMVFQSYALFPHMTALDNV--AYGLQssgLRKAEAREKAEEGLKLVGLA-----GMGHRLPAELSGGQQQRVAVA 150
Cdd:TIGR03269 363 akryIGILHQEYDLYPHRTVLDNLteAIGLE---LPDELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-230 |
7.10e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 136.43 E-value: 7.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV-----TMLPANERDVSMVFQSYALFPHMTALDN 100
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 VAYGL-QSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRT 179
Cdd:PRK11831 105 VAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 180 EIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-230 |
7.44e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.81 E-value: 7.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-----EHPTSGRILIGDQDVTMLPANE--RD 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHMTALDNVAYGLQSSGL--RKAEAREKAEEGLKLVGL-AGMGHRLPA---ELSGGQQQRVAVARALVL 155
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLgfTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-225 |
8.29e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 142.94 E-value: 8.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE------RD 81
Cdd:PRK10535 8 KDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrEH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLL 161
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-230 |
9.30e-38 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.92 E-value: 9.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 3 SVKPGSVTFKNVRKTFgafTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER-- 80
Cdd:PRK15079 19 DIKDGKQWFWQPPKTL---KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWra 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 ---DVSMVFQS--YALFPHMTALDNVAYGLQS--SGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARA 152
Cdd:PRK15079 96 vrsDIQMIFQDplASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqdeaLAV----SDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD----LAVvkhiSDRVLVMYLGHAVELGTYDEVYH 251
|
..
gi 1028514096 229 AP 230
Cdd:PRK15079 252 NP 253
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-217 |
2.16e-37 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 133.87 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGA--FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:cd03245 1 GRIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFpHMTALDNVAYGLQSSG----LRKAEAR------EKAEEGLKL-VGLAGMGhrlpaeLSGGQQQRVAVAR 151
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAPLADderiLRAAELAgvtdfvNKHPNGLDLqIGERGRG------LSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELqqRLGFTAVYVTHDQdEALAVSDRIIVMKDGEI 217
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-230 |
2.75e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 135.31 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKNVRKTfgaftAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTS---GRILIGDQDV---TML 75
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-----ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLtakTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 76 PANERdVSMVFQSY-ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:PRK13640 81 DIREK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-228 |
3.19e-37 |
|
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: 133.82 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRktfgaFT--------AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE- 79
Cdd:cd03249 1 IEFKNVS-----FRypsrpdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQSYALFPhMTALDNVAYGLQS-------SGLRKAEARE---KAEEGLK-LVGLAGmghrlpAELSGGQQQRV 147
Cdd:cd03249 76 rSQIGLVSQEPVLFD-GTIAENIRYGKPDatdeeveEAAKKANIHDfimSLPDGYDtLVGERG------SQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 148 AVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELqqRLGFTAVYVTHD----QDealavSDRIIVMKDGEIAQSGAP 223
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRlstiRN-----ADLIAVLQNGQVVEQGTH 221
|
....*
gi 1028514096 224 RELYE 228
Cdd:cd03249 222 DELMA 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
4.57e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.35 E-value: 4.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKpgSVTFKnvrKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE- 79
Cdd:PRK13632 7 MIKVE--NVSFS---YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQSY-ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:PRK13632 82 rKKIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALaVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-256 |
8.70e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.55 E-value: 8.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV-TMLPANERDVSMVFQ 87
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPasafiadfmgeanvVGC 247
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE--------------IGC 232
|
....*....
gi 1028514096 248 EVIRLDGPD 256
Cdd:PRK13537 233 DVIEIYGPD 241
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-236 |
1.16e-36 |
|
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: 132.26 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSSGLRKaeaREKAEEGLKLVG-LAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:TIGR03410 84 REIFPRLTVEENLLTGLAALPRRS---RKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIA 236
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-227 |
3.30e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 132.12 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIG----DQDVTMLPANERDVSMVFQSY--ALFPHmT 96
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVGIVFQNPddQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 97 ALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRR 176
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 177 VRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-228 |
3.71e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.80 E-value: 3.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF---GAFTaIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPANERD---- 81
Cdd:PRK13648 8 IVFKNVSFQYqsdASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT--DDNFEKlrkh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQS-YALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVL 160
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 161 LLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAvSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-227 |
4.02e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 132.14 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM--LPANERDVSMVFQSY-ALFPHMTALDNVAY 103
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 104 GLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRE 183
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1028514096 184 LQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-239 |
6.55e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 130.94 E-value: 6.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL------EHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHMTA 97
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 98 LDNVAYGLQSSGLR-KAEAREKAEEGLKLVGLAGMGH-RL--PA-ELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:PRK14246 108 YDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYdRLnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 173 LRRRVRTEIRELQQRLgfTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFM 239
Cdd:PRK14246 188 NSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-230 |
6.76e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 130.73 E-value: 6.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-----EHPTSGRILIGDQDVTMLPAN----ERDVS 83
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpievRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMTALDNVAYGLQSSGLRKA--EAREKAEEGLKLVGL-AGMGHRL---PAELSGGQQQRVAVARALVLEP 157
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLVKSkkELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRlgFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-229 |
1.39e-35 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 129.27 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG--AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSM 84
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFpHMTALDNVAYGlqssglRKAEAREKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVARAL 153
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG------RPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-225 |
1.51e-35 |
|
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: 136.92 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTF-GAFT-AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:TIGR03375 462 GEIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFpHMTALDNVAYGlqSSGLRKAEAREKAEEG--LKLVGLAGMGHRLP-----AELSGGQQQRVAVARALVL 155
Cdd:TIGR03375 542 GYVPQDPRLF-YGTLRDNIALG--APYADDEEILRAAELAgvTEFVRRHPDGLDMQigergRSLSGGQRQAVALARALLR 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHDQdEALAVSDRIIVMKDGEIAQSGaPRE 225
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADG-PKD 684
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-217 |
1.72e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 129.13 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 29 LTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER------DVSMVFQSYALFPHMTALDNVA 102
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIR 182
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190
....*....|....*....|....*....|....*
gi 1028514096 183 ELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEI 217
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
9-228 |
2.84e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 130.24 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG-----AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE---- 79
Cdd:PRK13643 2 IKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 --RDVSMVFQsyalFPHM-----TALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAG-MGHRLPAELSGGQQQRVAVAR 151
Cdd:PRK13643 82 vrKKVGVVFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-225 |
2.84e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 129.36 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMV 85
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYG----LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLL 161
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-212 |
7.14e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 133.57 E-value: 7.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 6 PGSVTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:TIGR02857 319 ASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHmTALDNVAYGlqssglRKAEAREKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVAR 151
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLA------RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHDqDEALAVSDRIIVM 212
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
16-226 |
1.25e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.82 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 16 KTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL----EHPTSGRILIGD--QDVTMLPANERD----VSMV 85
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRtvQREGRLARDIRKsranTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYG-LQSSGLRKA-------EAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIGaLGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-234 |
1.38e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.91 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 15 RKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTT----LRMLAglehpTSGRILIGDQDV------TMLPANERdVSM 84
Cdd:PRK15134 293 KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLhnlnrrQLLPVRHR-IQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQ--SYALFPHMTALDNVAYGLQ--SSGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAF 234
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-225 |
1.54e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 128.67 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGA-----FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRI-----------------L 66
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 67 IGDQDVTMLP-------ANE--RDVSMVFQ--SYALFpHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL-AGMGHR 134
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkIKEirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 135 LPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKD 214
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|.
gi 1028514096 215 GEIAQSGAPRE 225
Cdd:PRK13651 241 GKIIKDGDTYD 251
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-217 |
1.61e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 126.14 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDV 82
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELqQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-242 |
1.73e-34 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.03 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 18 FGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE---RDVSMVFQSYALFPH 94
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 MTALDN--VAYGLQS-----SGL------RKAE--AREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK11300 95 MTVIENllVAQHQQLktglfSGLlktpafRRAEseALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPasAFIADFM 239
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIKAYL 252
|
...
gi 1028514096 240 GEA 242
Cdd:PRK11300 253 GEA 255
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
23-227 |
1.99e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.66 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM----LPANERDVSMVFQS--YALFPhMT 96
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 97 ALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRR 176
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 177 VRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-226 |
4.06e-34 |
|
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: 125.42 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVrkTFGAFTAIP---DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RD 81
Cdd:cd03254 1 GEIEFENV--NFSYDEKKPvlkDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHmTALDNVAYGLQSSglrkaeAREKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVA 150
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLGRPNA------TDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdqdeALAV---SDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTHDEL 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-235 |
5.56e-33 |
|
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: 122.48 E-value: 5.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP----TSGRILIGDQDVTMLPANERDVSMVFQS--YALFPHMTALD 99
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYGLQSSGLRKAEAREKAEEGLKLVGL---AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRR 176
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 177 VRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFI 235
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETT 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
7.06e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 123.37 E-value: 7.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSY--ALFPh 94
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNPddQIFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 MTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLR 174
Cdd:PRK13652 94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 175 RRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-242 |
8.32e-33 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 122.98 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF----GAF-----TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD- 81
Cdd:PRK15112 8 RNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 -VSMVFQ--SYALFPHMTALDNVAYGLQSSGLRKAEAREKA-EEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLE 156
Cdd:PRK15112 88 rIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 157 PQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP----AS 232
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTK 247
|
250
....*....|
gi 1028514096 233 AFIADFMGEA 242
Cdd:PRK15112 248 RLIAGHFGEA 257
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-227 |
1.26e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 123.19 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVtmlPAN--------- 78
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PANlkkikevkr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 -ERDVSMVFQ--SYALFPHMTALDnVAYGLQSSGLRKAEAREKAEEGLKLVGLA-GMGHRLPAELSGGQQQRVAVARALV 154
Cdd:PRK13645 88 lRKEIGLVFQfpEYQLFQETIEKD-IAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-227 |
1.42e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.97 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFT-----AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT-------ML 75
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 76 PANERdVSMVFQsyalFPHMTAL-DNVA----YGLQSSGLRKAEAREKAEEGLKLVGLA-GMGHRLPAELSGGQQQRVAV 149
Cdd:PRK13646 82 PVRKR-IGMVFQ----FPESQLFeDTVEreiiFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 150 ARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
26-212 |
1.86e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 120.97 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHmTALDNVAY 103
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 104 GLQssgLRKAEAREKA-EEGLKLVGLA-GMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEI 181
Cdd:PRK10247 104 PWQ---IRNQQPDPAIfLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEII 180
|
170 180 190
....*....|....*....|....*....|.
gi 1028514096 182 RELQQRLGFTAVYVTHDQDEaLAVSDRIIVM 212
Cdd:PRK10247 181 HRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-210 |
3.01e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.26 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 18 FGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDqdvtmlpanERDVSMVFQSYAL---FPh 94
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 MTALDNVAYGL--QSSGLRK--AEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:NF040873 72 LTVRDLVAMGRwaRRGLWRRltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1028514096 171 ARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRII 210
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-261 |
5.20e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.12 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKpgsvtfkNVRKTF----------GAF-----------TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEH 59
Cdd:COG4586 1 IIEVE-------NLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 60 PTSGRILIGDQDvtmlP-----ANERDVSMVF-QSYALFPHMTALDNVA-----YGLQssglrKAEAREKAEEglkLVGL 128
Cdd:COG4586 74 PTSGEVRVLGYV----PfkrrkEFARRIGVVFgQRSQLWWDLPAIDSFRllkaiYRIP-----DAEYKKRLDE---LVEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 129 AGMGHRL--PA-ELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAV 205
Cdd:COG4586 142 LDLGELLdtPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 206 SDRIIVMKDGEIAQSGAPRELYE--APASAFIADFMGEANVV----GCEVIRLDGPDAMVRV 261
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKErfGPYKTIVLELAEPVPPLelprGGEVIEREGNRVRLEV 283
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-231 |
7.23e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.86 E-value: 7.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV---TMLPANERDVSMVFQS-YALFPHMTAL 98
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 99 DNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVR 178
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 179 TEIRELQQRlGFTAVYVTHDQDEaLAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-229 |
1.61e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.03 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 15 RKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLpanerDVSMVFQsyalfPH 94
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 MTALDNVAYGLQSSGLRKAEAREKAEEglkLVGLAGMGHRLPAEL---SGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDE---IVEFAELGDFIDQPVktySSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 172 RLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:COG1134 180 AFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-226 |
5.79e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 117.30 E-value: 5.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANER---DVSMVFQS 88
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQ-SSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-223 |
6.22e-31 |
|
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: 124.36 E-value: 6.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 6 PGsVTFKNVRKTFGAF--TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV-TMLPANERDV 82
Cdd:TIGR01257 927 PG-VCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 163 DEPLSNLDARLRRRVRTEIreLQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAP 223
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-239 |
7.17e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.83 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-----EHPTSGRILIGDQDVTMLPAN---- 78
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 ERDVSMVFQSYALFPhMTALDNVAYGLQSSGLR-KAEAREKAEEGLKLVGL----AGMGHRLPAELSGGQQQRVAVARAL 153
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKD-----GEIAQSGAPRELYE 228
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
250
....*....|.
gi 1028514096 229 APASAFIADFM 239
Cdd:PRK14258 246 SPHDSRTREYV 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-234 |
8.58e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 120.72 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVF 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYAL--------------FPHMTALDnvayglqssglRKAEAREKA-EEGLKLVGLAGMGHRLPAELSGGQQQRVAVAR 151
Cdd:PRK09536 84 QDTSLsfefdvrqvvemgrTPHRSRFD-----------TWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDarLRRRVRTeiRELQQRL---GFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLD--INHQVRT--LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
....*...
gi 1028514096 229 AP--ASAF 234
Cdd:PRK09536 229 ADtlRAAF 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-225 |
9.47e-31 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 122.55 E-value: 9.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHmTALDNVAy 103
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENIA- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 104 glqssglRKAEA-REKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:COG4618 428 -------RFGDAdPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 172 RLRRRVRTEIRELQQRlGFTAVYVTHDQdEALAVSDRIIVMKDGEIAQSGaPRE 225
Cdd:COG4618 501 EGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG-PRD 551
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-231 |
1.04e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 118.80 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 16 KTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD-----------QDVTMLPAN------ 78
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnheLITNPYSKKiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 -ERDVSMVFQ--SYALFPHmTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:PRK13631 114 lRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
26-217 |
1.15e-30 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 114.62 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTML-PANERD-VSMVFQSYALFPHmTALDNVay 103
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDhVGYLPQDDELFSG-SIAENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 104 glqssglrkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRE 183
Cdd:cd03246 97 -----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA 141
|
170 180 190
....*....|....*....|....*....|....
gi 1028514096 184 LQQRlGFTAVYVTHdQDEALAVSDRIIVMKDGEI 217
Cdd:cd03246 142 LKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-240 |
1.26e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.50 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLE-----HPTSGRILIGDQDVTmlpaNERDV----- 82
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIF----NYRDVlefrr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 --SMVFQSYALFPhMTALDNVAYGLQSSGL-RKAEAREKAEEGLKLVGL-AGMGHRL---PAELSGGQQQRVAVARALVL 155
Cdd:PRK14271 102 rvGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLgfTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFI 235
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
....*
gi 1028514096 236 ADFMG 240
Cdd:PRK14271 259 ARYVA 263
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-207 |
1.55e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.81 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEH--PT---SGRILIGDQDV---TMLPAN-ERDV 82
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyapDVDPVEvRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHmTALDNVAYGLQSSG------------LRKAEAREKAEEGLKLVGLAgmghrlpaeLSGGQQQRVAVA 150
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYGARINGykgdmdelversLRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlgFTAVYVTHDQDEALAVSD 207
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-239 |
2.01e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.41 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-----EHPTSGRILIGDQDVTMLPAN----E 79
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDtvdlR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPhMTALDNVAYGLQSSGLR-KAEAREKAEEGLKLVGL----AGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlgFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAF 234
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKE 242
|
....*
gi 1028514096 235 IADFM 239
Cdd:PRK14239 243 TEDYI 247
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-229 |
3.30e-30 |
|
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: 120.98 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGA--FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT--MLPANERDV 82
Cdd:TIGR02203 329 GDVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHmTALDNVAYGlqssglRKAEA-REKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVA 150
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYG------RTEQAdRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-226 |
3.98e-30 |
|
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: 114.89 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFT--AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN--ERDVSM 84
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFpHMTALDNVAYGlqssglRKAEAREKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVARAL 153
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-252 |
1.26e-29 |
|
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: 118.75 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLE--HPTSGRIL-----------------IGD 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpskVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 70 Q------------------DVTMLPANERDVSMVFQ-SYALFPHMTALDNVAYGLQSSGLRKAEAREKAeegLKLVGLAG 130
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRA---VDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 131 MGHR---LPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSD 207
Cdd:TIGR03269 158 LSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1028514096 208 RIIVMKDGEIAQSGAPRELYEAPASAFiADFMGEANV-VGCEVIRL 252
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEGV-SEVEKECEVeVGEPIIKV 282
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-226 |
2.33e-29 |
|
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: 118.77 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 4 VKPGSVTFKNVRktFGAFTAIP---DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVtmlpaneR 80
Cdd:COG5265 353 VGGGEVRFENVS--FGYDPERPilkGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-------R 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 DVS---------MVFQSYALFpHMTALDNVAYGlqssglrKAEA-REKAEEGLKLVGLAGMGHRLPA-----------EL 139
Cdd:COG5265 424 DVTqaslraaigIVPQDTVLF-NDTIAYNIAYG-------RPDAsEEEVEAAARAAQIHDFIESLPDgydtrvgerglKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 140 SGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTH------DqdealavSDRIIVMK 213
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLE 566
|
250
....*....|...
gi 1028514096 214 DGEIAQSGAPREL 226
Cdd:COG5265 567 AGRIVERGTHAEL 579
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-217 |
3.77e-29 |
|
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: 112.43 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDqdvtMLPANERD-----VSMVF-Q 87
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKkflrrIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1028514096 168 NLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-244 |
3.99e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.03 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-----RDVSMVFQS-YA-LFPHM 95
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 96 TALDNVAYGLQSSGLRKAE-AREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARL 173
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 174 RRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIADFMGEANV 244
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-221 |
4.39e-29 |
|
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: 111.86 E-value: 4.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIgdqdvtmlpaNERDVSMVFQSYALFPHMTAL 98
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSLLGLGGGFNPELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 99 DNVAYGLQSSGLRKAEAREKAEEglkLVGLAGMGHRLPA---ELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRR 175
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDE---IIEFSELGDFIDLpvkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1028514096 176 RVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03220 180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-217 |
4.48e-29 |
|
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: 111.79 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVrkTFgAFTAIPD------LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-- 78
Cdd:cd03248 10 GIVKFQNV--TF-AYPTRPDtlvlqdVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 ERDVSMVFQSYALFPHmTALDNVAYGLQSSGLRK-AEAREKAEEGLKLVGLA-----GMGHRlPAELSGGQQQRVAVARA 152
Cdd:cd03248 87 HSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECvKEAAQKAHAHSFISELAsgydtEVGEK-GSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlgfTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-230 |
4.06e-28 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 110.26 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTML--PANERDVSMVFQSYALFPHMTALDNVAYG 104
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 105 LQ----SSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTE 180
Cdd:PRK10575 110 RYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1028514096 181 IRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-227 |
4.81e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 110.48 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIG----DQDVTMLPANERDVSMVFQSYALFPHMTALD-NV 101
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKRGLLALRQQVATVFQDPEQQIFYTDIDsDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 102 AYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEI 181
Cdd:PRK13638 100 AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1028514096 182 RELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PRK13638 180 RRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-221 |
8.37e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 113.73 E-value: 8.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP---ANERDVSMV 85
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYGLQSSglRK---------AEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLE 156
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLT--KKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 157 PQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-230 |
9.39e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 114.43 E-value: 9.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGAFTAIP---DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN--ERD 81
Cdd:TIGR00958 477 GLIEFQDVSFSYPNRPDVPvlkGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHmTALDNVAYGLQSSglRKAEAREKAEEGLKLVGLAGMGHRLPAE-------LSGGQQQRVAVARALV 154
Cdd:TIGR00958 557 VALVGQEPVLFSG-SVRENIAYGLTDT--PDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRtEIRELQQRlgfTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQ-ESRSRASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-217 |
1.06e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdqdvtMLPANERdVSMVFQSYA 90
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 91 LFPHMTALDNVAYGLQssGLRKAEAR--------EKAEEGLKLVG---------------------LAGMG------HRL 135
Cdd:COG0488 72 LDDDLTVLDTVLDGDA--ELRALEAEleeleaklAEPDEDLERLAelqeefealggweaearaeeiLSGLGfpeedlDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 136 PAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDArlrrrvrtEIRE-----LQQRLGfTAVYVTHDQ---DealAVSD 207
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------ESIEwleefLKNYPG-TVLVVSHDRyflD---RVAT 217
|
250
....*....|
gi 1028514096 208 RIIVMKDGEI 217
Cdd:COG0488 218 RILELDRGKL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-256 |
1.74e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 110.31 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 3 SVKPGSVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVtmlPANER-- 80
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARla 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 --DVSMVFQSYALFPHMTALDN-VAYGlQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:PRK13536 113 raRIGVVPQFDNLDLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEapasafiad 237
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID--------- 261
|
250
....*....|....*....
gi 1028514096 238 fmgeaNVVGCEVIRLDGPD 256
Cdd:PRK13536 262 -----EHIGCQVIEIYGGD 275
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-217 |
1.83e-27 |
|
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: 106.36 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP---ANERDVSMV---FQSYALFPHMTALD 99
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdAIRAGIAYVpedRKREGLVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAyglqssglrkaearekaeeglklvglagmghrLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRT 179
Cdd:cd03215 98 NIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1028514096 180 EIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:cd03215 146 LIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-221 |
1.88e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.47 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILI-----GDQDVTMLPANER------ 80
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 DVSMVFQSYA--LFPHMTALDNVAYGLQSSGLRK-AEAREKAEEGLKLVGLAGmgHR---LPAELSGGQQQRVAVARALV 154
Cdd:PRK11701 90 EWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDA--ARiddLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqdeaLAV----SDRIIVMKDGEIAQSG 221
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHD----LAVarllAHRLLVMKQGRVVESG 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-226 |
3.37e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 111.68 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP---ANERDVSMVFQS 88
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLGIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQssglRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:PRK15439 95 PLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 169 LDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:PRK15439 171 LTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-215 |
3.63e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 111.54 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlpANERD-----VSMV 85
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAalaagVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYG-LQSSG--LRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDG 215
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-221 |
4.76e-27 |
|
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: 106.59 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 24 IPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP---TSGRILIGDQDVTmlPANERD-VSMVFQSYALFPHMTALD 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK--PDQFQKcVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYGLQSSGLRKAEAREKAEE----GLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRR 175
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1028514096 176 RVRTEIRELQQRlgFTAVYVTHDQ--DEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03234 181 NLVSTLSQLARR--NRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-219 |
9.26e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.05 E-value: 9.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 24 IPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILigdqdvtmLPANERdvsMVF---QSYalFPHMTALDN 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGAR---VLFlpqRPY--LPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 VAYGLQSSglrkAEAREKAEEGLKLVGLAGMGHRLPAE------LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLR 174
Cdd:COG4178 446 LLYPATAE----AFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1028514096 175 RRVrteIRELQQRL-GFTAVYVTHdQDEALAVSDRIIVMKDGEIAQ 219
Cdd:COG4178 522 AAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGDGSWQ 563
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-217 |
9.66e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIG--------DQDVTMLPaner 80
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGetvkigyfDQHQEELD---- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 dvsmvfqsyalfPHMTALDNVAYGlqSSGLRKAEARE-------KAEEGLKLVGlagmghrlpaELSGGQQQRVAVARAL 153
Cdd:COG0488 392 ------------PDKTVLDELRDG--APGGTEQEVRGylgrflfSGDDAFKPVG----------VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 154 VLEPQVLLLDEPLSNLDarlrrrVRTeIRELQQRL-GF--TAVYVTHDQD--EALAvsDRIIVMKDGEI 217
Cdd:COG0488 448 LSPPNVLLLDEPTNHLD------IET-LEALEEALdDFpgTVLLVSHDRYflDRVA--TRILEFEDGGV 507
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-226 |
1.10e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.68 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKNVRKTF--GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLpaNE 79
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY--SE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RD----VSMVFQSYALFPHmTALDNVAyglqssgLRKAEAR-EKAEEGLKLVGLA-------------GMGHRlpaELSG 141
Cdd:PRK11160 410 AAlrqaISVVSQRVHLFSA-TLRDNLL-------LAAPNASdEALIEVLQQVGLEklleddkglnawlGEGGR---QLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 142 GQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQG 555
|
....*
gi 1028514096 222 APREL 226
Cdd:PRK11160 556 THQEL 560
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-221 |
1.86e-26 |
|
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: 103.78 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 6 PGSVTFKNVRKT------FGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL--EHPTSGRILIGDQDVTMLPA 77
Cdd:cd03213 1 GVTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 78 NERdVSMVFQSYALFPHMTALDNVAYglqSSGLRKaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEP 157
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMF---AAKLRG--------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQrLGFTAVYVTHD-QDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-216 |
2.33e-26 |
|
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: 109.53 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLeHPT---SGRILIGDQDV---TMLPANERDV 82
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLkasNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYG----LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLP-AELSGGQQQRVAVARALVLEP 157
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
8.33e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 105.59 E-value: 8.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKTFGAFTAIpdlSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-EHP---TSGRILIGDQDVTMLP 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRI---SYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 77 ANER------DVSMVFQSyalfpHMTALdNVAY--GLQ-------SSGLRKAEAREKAEEGLKLVGLAGMGHRL---PAE 138
Cdd:PRK11022 80 EKERrnlvgaEVAMIFQD-----PMTSL-NPCYtvGFQimeaikvHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 139 LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250
....*....|..
gi 1028514096 219 QSGAPRELYEAP 230
Cdd:PRK11022 234 ETGKAHDIFRAP 245
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-230 |
1.09e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.01 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEhPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFpHMTALDNVAYG 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 105 LQS-------SGLRKAEARE---KAEEGLKL-VGLAGMGhrlpaeLSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARL 173
Cdd:PRK11174 447 NPDasdeqlqQALENAWVSEflpLLPQGLDTpIGDQAAG------LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 174 RRRVRTEIRELQQRLgfTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK11174 521 EQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-221 |
2.45e-25 |
|
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: 100.47 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFG--AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERD-VSMV 85
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFpHMTALDNVayglqssGLRkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:cd03247 81 NQRPYLF-DTTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 166 LSNLDARLRRRV-RTEIRELQQRlgfTAVYVTHdQDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03247 126 TVGLDPITERQLlSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-216 |
5.51e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.40 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-EHPT-SGRILIGDQDVTmlPANERD-----VSM 84
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELQ--ASNIRDteragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALDNVAYG--LQSSGLRK-AEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLL 161
Cdd:PRK13549 87 IHQELALVKELSVLENIFLGneITPGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-229 |
6.46e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.60 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 18 FGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHM 95
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 96 TALDNVA---YGLQSSGLR-KAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:PRK10253 97 TVQELVArgrYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 172 RLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-197 |
1.01e-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: 99.36 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLpANERDVSMVFQSY--ALFPHMTALDNVAYG 104
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHlpGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 105 LQSSGlrkaEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIREL 184
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|...
gi 1028514096 185 QQRLGfTAVYVTH 197
Cdd:TIGR01189 174 LARGG-IVLLTTH 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-226 |
1.16e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLE--HPTSGRILIGDQDVTMLPANER---DVSMVFQSYALFPHMTALD- 99
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSNf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 -NVAYGLQS-SGLRKAEAREKAEEGLKLVGL-AGMGHR-LPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRR 175
Cdd:COG0396 98 lRTALNARRgEELSAREFLKLLKEKMKELGLdEDFLDRyVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 176 RVRTEIRELQQRlGFTAVYVTHdQDEALA--VSDRIIVMKDGEIAQSGAPrEL 226
Cdd:COG0396 178 IVAEGVNKLRSP-DRGILIITH-YQRILDyiKPDFVHVLVDGRIVKSGGK-EL 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-235 |
2.78e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.18 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE---RDVSMV 85
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 FQSYALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLkLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYEL-FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIA--QSGAPRELYEAPASAFI 235
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDALLANEAVRSAYL 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-226 |
3.55e-24 |
|
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: 103.67 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFG-AFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVS 83
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHmTALDNVAYGlqssglrkaeAREKA--EEGLKLVGLA-----------GMGHRLPAE---LSGGQQQRV 147
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLG----------AKENVsqDEIWAACEIAeikddienmplGYQTELSEEgssISGGQKQRI 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 148 AVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlgfTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
13-230 |
3.98e-24 |
|
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: 99.13 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQD-----VTMLPANERDVSMvfQ 87
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLM--R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SYALFPHMTALD----------NVAYGLQSSGLRK-AEAREKAEEGLKLVGL-AGMGHRLPAELSGGQQQRVAVARALVL 155
Cdd:TIGR02323 86 TEWGFVHQNPRDglrmrvsagaNIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-234 |
4.44e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.86 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKTFgafTAIPDLSLTIEPGTLVTLLGPSGCGKT-TTLRMLAGLEHP----TSGRILIGDQDvtML 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVR---TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGES--LL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 76 PANER--------DVSMVFQS--YALFPHMTaLDNVAYGLQS--SGLRKAEAREKAEEGLKLVGLAGMGHRL---PAELS 140
Cdd:PRK15134 80 HASEQtlrgvrgnKIAMIFQEpmVSLNPLHT-LEKQLYEVLSlhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 141 GGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQS 220
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250
....*....|....
gi 1028514096 221 GAPRELYEAPASAF 234
Cdd:PRK15134 239 NRAATLFSAPTHPY 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-198 |
7.42e-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: 102.44 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFpHMT 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 97 ALDNVAYGlqssglRKAEAREKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:TIGR02868 425 VRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQrlGFTAVYVTHD 198
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-231 |
1.02e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.80 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTF----GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP---TSGRILIGDQDVTMLPANE----- 79
Cdd:PRK09473 16 KDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKElnklr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 -RDVSMVFQS--YALFPHMTALDNVAYGLQ-SSGLRKAEAREKAEEGLKLVGLAGMGHRL---PAELSGGQQQRVAVARA 152
Cdd:PRK09473 96 aEQISMIFQDpmTSLNPYMRVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPA 231
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-226 |
1.14e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTF-GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN--ERDVS 83
Cdd:PRK13657 333 GAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMTAlDNVAYGLQSSG---LRKAEAR-------EKAEEGLK-LVGLAGmghrlpAELSGGQQQRVAVARA 152
Cdd:PRK13657 413 VVFQDAGLFNRSIE-DNIRVGRPDATdeeMRAAAERaqahdfiERKPDGYDtVVGERG------RQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdqdeALAV---SDRIIVMKDGEIAQSGAPREL 226
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH----RLSTvrnADRILVFDNGRVVESGSFDEL 556
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-226 |
2.12e-23 |
|
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: 100.89 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHMTAlDNVA- 102
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPGTVA-ENIAr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGlqssglRKAEArEKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:TIGR01842 415 FG------ENADP-EKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 172 RLRRRVRTEIRELQQRlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:TIGR01842 488 EGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-218 |
2.19e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT-------------MLPANeRdvsmvfQSYALF 92
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairagiaYVPED-R------KGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 PHMTALDNVAYGLQSSG-----LRKAEAREKAEEGLKLVGLAGMGHRLPA-ELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:COG1129 343 LDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-171 |
6.72e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.49 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVtmlpANERDvsmVFQSYALF--------PHMTA 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRD---EYHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 98 LDNVAYGLQSSGLRKAEAREKAeegLKLVGLAGMGHRLPAELSGGQQQRVAVARaLVLEPQVL-LLDEPLSNLDA 171
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDK 162
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-228 |
1.21e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.94 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTF-GAFT-AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT--MLPANERDV 82
Cdd:PRK11176 340 GDIEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFpHMTALDNVAYGLQSSGLRK---AEAR--------EKAEEGLK-LVGLAGmghrlpAELSGGQQQRVAVA 150
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYARTEQYSREqieEAARmayamdfiNKMDNGLDtVIGENG------VLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLgfTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYE 228
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-216 |
1.53e-22 |
|
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: 91.74 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGdQDVTMlpanerdvsmvfqs 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-STVKI-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 yALFPHmtaldnvayglqssglrkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03221 66 -GYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1028514096 169 LDARLRRRVRTEIRELQQrlgfTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-197 |
1.55e-22 |
|
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: 93.71 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILI-GDQDVTMLPANERDVSMVFQSYALFPHMTALDNVAYgl 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 qssgLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQ 185
Cdd:cd03231 97 ----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|..
gi 1028514096 186 QRlGFTAVYVTH 197
Cdd:cd03231 173 AR-GGMVVLTTH 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-226 |
2.46e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 22 TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-RDVSMVF-----QSYALFPHM 95
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYipedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 96 TALDNVAYGLQSSG-------LRKAEAREKAEEGLKLVGLAGMGHRLPAE-LSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:COG3845 352 SVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVILARELSRDPKLLIAAQPTR 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 168 NLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:COG3845 432 GLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-197 |
4.50e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERdVSMVFQSYALFPHMTALDNVAYGL 105
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 QSSGlrkaEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRE-L 184
Cdd:PRK13539 99 AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhL 174
|
170
....*....|...
gi 1028514096 185 QQrlGFTAVYVTH 197
Cdd:PRK13539 175 AQ--GGIVIAATH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-231 |
5.14e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 1 MISVKPGSVTFKNVRKTFgafTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGR---------------I 65
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKI---AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmllrrrsrqvI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 66 LIGDQ-DVTMLPANERDVSMVFQS--YALFPHMTALDNVAYGLQ-SSGLRKAEAREKAEEGLKLVGLA---GMGHRLPAE 138
Cdd:PRK10261 89 ELSEQsAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIPeaqTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 139 LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250
....*....|...
gi 1028514096 219 QSGAPRELYEAPA 231
Cdd:PRK10261 249 ETGSVEQIFHAPQ 261
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-228 |
1.19e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 91.05 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGleHP----TSGRILIGDQDVTMLPANER---DVSMVFQSYALFPHMTAL 98
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPkyevTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 99 D---NVAYGlqssglrkaearekaeeglklvglagmghrlpaeLSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRR 175
Cdd:cd03217 96 DflrYVNEG----------------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 176 RVRTEIRELQQRlGFTAVYVTHDQDEALAV-SDRIIVMKDGEIAQSGaPRELYE 228
Cdd:cd03217 142 LVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELAL 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-197 |
2.04e-21 |
|
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: 89.52 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 24 IPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILI-GDQDVTMLPAnerdvsmvfQSYalFPHMTALDNVA 102
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQ---------RPY--LPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQSsglrkaearekaeeglklvglagmghrlpaELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIR 182
Cdd:cd03223 86 YPWDD------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170
....*....|....*
gi 1028514096 183 ElqqrLGFTAVYVTH 197
Cdd:cd03223 136 E----LGITVISVGH 146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-238 |
5.33e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.56 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdqdvtmlpanERDVSM---- 84
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLrigy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTAldNVAYGLQssgLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDE 164
Cdd:PRK09544 72 VPQKLYLDTTLPL--TVNRFLR---LRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 165 PLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMkDGEIAQSGAPRELYEAPasAFIADF 238
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP--EFISMF 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-225 |
8.39e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.90 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLeHPTSGRILIGDQDVT------------MLPANERDVSM--VFQSYALF 92
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSdwsaaelarhraYLSQQQSPPFAmpVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 phmtaldnvayglQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALV-------LEPQVLLLDEP 165
Cdd:COG4138 94 -------------QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRE 225
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-216 |
8.42e-21 |
|
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: 89.07 E-value: 8.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKNVRKTfgAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQdvtmlpanerd 81
Cdd:cd03250 1 ISVEDASFTWDSGEQE--TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPhMTALDNVAYGLQssgLRKAEARE--KA---EEGLKL--------VGLAGMGhrlpaeLSGGQQQRVA 148
Cdd:cd03250 68 IAYVSQEPWIQN-GTIRENILFGKP---FDEERYEKviKAcalEPDLEIlpdgdlteIGEKGIN------LSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 149 VARALVLEPQVLLLDEPLSNLDARLRRRVRTE-IRELqQRLGFTAVYVTHdQDEALAVSDRIIVMKDGE 216
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGL-LLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-221 |
9.87e-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: 89.77 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 16 KTFGAFTaipdlsLTIEPGTL-----VTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPAN-ERDVSMVFQSY 89
Cdd:cd03237 8 KTLGEFT------LEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 90 alfphmtaLDNVAYGLQSSGLRKAEAREKaeegLKLVGLagMGHRLPaELSGGQQQRVAVARALVLEPQVLLLDEPLSNL 169
Cdd:cd03237 82 --------LSSITKDFYTHPYFKTEIAKP----LQIEQI--LDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 170 DARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMkDGEIAQSG 221
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNG 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-230 |
2.06e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.08 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 22 TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDVSMVFQSYALFPHMTAlD 99
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSDTVA-N 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYGlqssglRKAEAREKAEEGLKLVGLAGMGHRLP-----------AELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:PRK10789 408 NIALG------RPDATQQEIEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 169 LDARLRRRVRTEIRelQQRLGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK10789 482 VDGRTEHQILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-214 |
3.63e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 87.71 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGA------FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLE--HPTSGRILIGDQDVtmlpanERDVSMV 85
Cdd:COG2401 30 VLEAFGVelrvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF------GREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 86 fqsyalfphmtalDNVAyglqssglRKAEAREKAEEgLKLVGL--AGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:COG2401 104 -------------DAIG--------RKGDFKDAVEL-LNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 164 EPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKD 214
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-198 |
3.98e-20 |
|
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: 91.54 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDqdvTMlpanerDVSMVFQS 88
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE---TV------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 Y-ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGL---------KLVGlagmghrlpaELSGGQQQRVAVARALVLEPQ 158
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRfnfkgsdqqKKVG----------QLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1028514096 159 VLLLDEPLSNLDarlrrrVRTeIRELQQRL-GF--TAVYVTHD 198
Cdd:TIGR03719 464 VLLLDEPTNDLD------VET-LRALEEALlNFagCAVVISHD 499
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-226 |
7.63e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.42 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFG--AFTAIPdLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM--LPANERDVSMVF 86
Cdd:PRK10522 325 LRNVTFAYQdnGFSVGP-INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAeqPEDYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMtaldnvaygLQSSGlrKAEAREKAEEGLKLVglaGMGHRLPAE--------LSGGQQQRVAVARALVLEPQ 158
Cdd:PRK10522 404 TDFHLFDQL---------LGPEG--KPANPALVEKWLERL---KMAHKLELEdgrisnlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 159 VLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDqDEALAVSDRIIVMKDGEIAQ-SGAPREL 226
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-236 |
2.71e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.41 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 18 FGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlpANE----RDVSMVFQSYALFP 93
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDiatrRRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 94 HMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARL 173
Cdd:NF033858 353 ELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 174 RRRVRTEIRELQQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRELYEAPAS-----AFIA 236
Cdd:NF033858 433 RDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAARGAatleeAFIA 499
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-221 |
2.85e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 88.71 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFtaipdlSLTIEPGTL-----VTLLGPSGCGKTTTLRMLAGLEHPTSGRILI------------GDQD 71
Cdd:PRK13409 341 VEYPDLTKKLGDF------SLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPelkisykpqyikPDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 72 VTmlpanerdVSMVfqsyalfphmtaLDNVAYGLQSSGLrkaeareKAE--EGLKLVGLagMGHRLPaELSGGQQQRVAV 149
Cdd:PRK13409 415 GT--------VEDL------------LRSITDDLGSSYY-------KSEiiKPLQLERL--LDKNVK-DLSGGELQRVAI 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 150 ARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHD---QDealAVSDRIIVMkDGEIAQSG 221
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDiymID---YISDRLMVF-EGEPGKHG 535
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-233 |
3.15e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.91 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP----TSGRILIGDQDVTMLPANERDVSMVFQS--YALFPHMTALD 99
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYGLQSSGLRKAEARekAEEGLKLVGLAGMGHRL---PAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRR 176
Cdd:PRK10418 101 HARETCLALGKPADDAT--LTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 177 VRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASA 233
Cdd:PRK10418 179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-213 |
3.56e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 84.90 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlpANERDVSMVFQSY--ALFPHMTALDNVAYg 104
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHlpGLKADLSTLENLHF- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 105 lqSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARaLVLEPQVL-LLDEPLSNLDAR----LRRRVRT 179
Cdd:PRK13543 106 --LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEgitlVNRMISA 182
|
170 180 190
....*....|....*....|....*....|....
gi 1028514096 180 EIRElqqrlGFTAVYVTHDQDEALAVSDRIIVMK 213
Cdd:PRK13543 183 HLRG-----GGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-238 |
4.50e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.37 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 27 LSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEhPTSGRILIGDQDVTMLPANERDV-------------SM-VFQSYALF 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARhraylsqqqtppfAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 phmtaldnvayglQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVA-------RALVLEPQVLLLDEP 165
Cdd:PRK03695 94 -------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 166 LSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP--ASAFIADF 238
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEnlAQVFGVNF 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-223 |
4.95e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 84.47 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTF--GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHmTALDNVA-YGLQSSglrkaearEKAEEGLKLVGL----AGMGHRLPAE-------LSGGQQQRVAVA 150
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDpFGEYSD--------EELWQALERVGLkefvESLPGGLDTVveeggenLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 151 RALVLEPQVLLLDEPLSNLD----ARLRRRVRTEIRelqqrlGFTAVYVTHDQDeALAVSDRIIVMKDGEIAQSGAP 223
Cdd:cd03244 152 RALLRKSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-215 |
1.07e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 87.76 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlpanerDVSMVFQSYALFPHMTALDNVA 102
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQS-------SGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRR 175
Cdd:TIGR01257 2028 TGREHlylyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1028514096 176 RVRTEIRELqQRLGFTAVYVTHDQDEALAVSDRIIVMKDG 215
Cdd:TIGR01257 2108 MLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-229 |
1.44e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKNvrktfgAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlPANERD 81
Cdd:PRK15056 7 IVVNDVTVTWRN------GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYAL---FPHMTAlDNVAYGL--QSSGLRKAEAREKA--EEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALV 154
Cdd:PRK15056 80 VAYVPQSEEVdwsFPVLVE-DVVMMGRygHMGWLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKdGEIAQSGAPRELYEA 229
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTA 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-217 |
1.90e-18 |
|
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: 86.39 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTF------GAFTAIPdLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlpANERD 81
Cdd:COG4615 327 TLELRGVTYRYpgedgdEGFTLGP-IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 V-----SMVFQSYALFPHMtaldnvaYGLQSsglrkAEAREKAEEGLKLVGLAGM-----GHRLPAELSGGQQQRVAVAR 151
Cdd:COG4615 403 AyrqlfSAVFSDFHLFDRL-------LGLDG-----EADPARARELLERLELDHKvsvedGRFSTTDLSQGQRKRLALLV 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEI-RELQQRlGFTAVYVTHDqDEALAVSDRIIVMKDGEI 217
Cdd:COG4615 471 ALLEDRPILVFDEWAADQDPEFRRVFYTELlPELKAR-GKTVIAISHD-DRYFDLADRVLKMDYGKL 535
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-221 |
4.17e-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: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFtaipdlSLTIEPGTL-----VTLLGPSGCGKTTTLRMLAGLEHPTSGRIlIGDQDVTMLPAN-ERDV 82
Cdd:COG1245 342 VEYPDLTKSYGGF------SLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISYKPQYiSPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYalfphmtaLDNVAYG-LQSSGLRkaearekaEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLL 161
Cdd:COG1245 415 DGTVEEF--------LRSANTDdFGSSYYK--------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHD---QDealAVSDRIIVMkDGEIAQSG 221
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDiylID---YISDRLMVF-EGEPGVHG 537
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-216 |
5.37e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 84.78 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDV---TMLPANERDVSMVFQS 88
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGL---------QSSGLRKAEA-----------REKAeeglklvglagmghrlpAELSGGQQQRVA 148
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRyptkgmfvdQDKMYRDTKAifdeldididpRAKV-----------------ATLSVSQMQMIE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 149 VARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-226 |
7.02e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.18 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGlEHPTSGR----ILIGDQDVTMLPANERDVSMVFQSYALFPH------- 94
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaqpafa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 MTALDNVAYG----LQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARAL---------VLEPQVLL 161
Cdd:PRK13547 98 FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 162 LDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-220 |
8.08e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlpANERD-----VSMVF 86
Cdd:PRK10762 8 KGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF--NGPKSsqeagIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTALDNVAYGLQSS----GLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE-IAQS 220
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQfIAER 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-226 |
1.51e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 31 IEPGTLVTLLGPSGCGKTTTLRMLAGLEHP---TSGRILIGDQDVTmLPANERDVSMVFQSYALFPHMTALDNVAYglqS 107
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVREHLMF---Q 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 108 SGLR------KAEAREKAEEGLKLVGLA-------GMGHRLPAeLSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLR 174
Cdd:TIGR00955 124 AHLRmprrvtKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 175 RRVRTEIRELQQRlGFTAVYVTHD-QDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:TIGR00955 203 YSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-226 |
1.90e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.02 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTF--KNVRKTfgaftaIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPane 79
Cdd:PLN03130 615 ISIKNGYFSWdsKAERPT------LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP--- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 rDVSMVFQSyalfphmTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAG-----MGHRlPAELSGGQQQRVAVARALV 154
Cdd:PLN03130 686 -QVSWIFNA-------TVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGgdlteIGER-GVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028514096 155 LEPQVLLLDEPLSNLDARLRRRV-RTEIR-ELQQRlgfTAVYVThDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVfDKCIKdELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-220 |
4.78e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVT-MLPANERDVSMVF-----QSYALFphmtaLD 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINaLSTAQRLARGLVYlpedrQSSGLY-----LD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 -----NV---AYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAE-LSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:PRK15439 356 aplawNVcalTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1028514096 171 ARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQS 220
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-212 |
4.84e-17 |
|
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: 82.14 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 30 TIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTsgrilIGDQDVtmlPANERDVSMVFQSYALFPHMTALDN----VAYGL 105
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPN-----LGDYDE---EPSWDEVLKRFRGTELQDYFKKLANgeikVAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 Q--------SSG-----LRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:COG1245 167 QyvdlipkvFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1028514096 173 LRRRVRTEIRELQQRlGFTAVYVTHDqdeaLAV----SDRIIVM 212
Cdd:COG1245 247 QRLNVARLIRELAEE-GKYVLVVEHD----LAIldylADYVHIL 285
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-198 |
6.07e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.70 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDqdvTMlpanerDVSMVFQS 88
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE---TV------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 Y-ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGL---------KLVGlagmghrlpaELSGGQQQRVAVARALVLEPQ 158
Cdd:PRK11819 396 RdALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRfnfkggdqqKKVG----------VLSGGERNRLHLAKTLKQGGN 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1028514096 159 VLLLDEPLSNLDarlrrrVRTeIRELQQRL-GF--TAVYVTHD 198
Cdd:PRK11819 466 VLLLDEPTNDLD------VET-LRALEEALlEFpgCAVVISHD 501
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-207 |
2.51e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.53 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM-LPANERDVSMVFQSYALFPHMTALDNVAYG 104
Cdd:PRK13540 19 QISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENCLYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 105 LQSSglrkaearEKAEEGLKLVGLAGMGHRLP---AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEI 181
Cdd:PRK13540 99 IHFS--------PGAVGITELCRLFSLEHLIDypcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170 180
....*....|....*....|....*.
gi 1028514096 182 RELQQRLGftAVYVTHDQDEALAVSD 207
Cdd:PRK13540 171 QEHRAKGG--AVLLTSHQDLPLNKAD 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-217 |
3.82e-16 |
|
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: 75.76 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPT---SGRILIGDqdVTMLPANE---RDVSMVF 86
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEkypGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTAldnvayglqssglrkaeaREKAEEGLKLvglagMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPL 166
Cdd:cd03233 90 EEDVHFPTLTV------------------RETLDFALRC-----KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 167 SNLDARLRRRVRTEIRELQQRLGFTAVyVTHDQ--DEALAVSDRIIVMKDGEI 217
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-238 |
4.20e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 13 NVRKTFGAFTAIPDLSLTIE-------------PGTLVTLLGPSGCGKTTTLRMLAGLEHPTS--GRILIGDQDVTMlPA 77
Cdd:PLN03211 60 NIKRILGHKPKISDETRQIQertilngvtgmasPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-QI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 78 NERdVSMVFQSYALFPHMTALDNVAY----GLQSSgLRKAEAREKAEEGLKLVGLAG-----MGHRLPAELSGGQQQRVA 148
Cdd:PLN03211 139 LKR-TGFVTQDDILYPHLTVRETLVFcsllRLPKS-LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 149 VARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQdealavSDRIIVMKDGEIAQSGApRELYE 228
Cdd:PLN03211 217 IAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQP------SSRVYQMFDSVLVLSEG-RCLFF 288
|
250
....*....|
gi 1028514096 229 APASAFIADF 238
Cdd:PLN03211 289 GKGSDAMAYF 298
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-236 |
1.30e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRI--LIGDqdvtMLPANERDvsMVF 86
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGD----MADARHRR--AVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYA---------LFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:NF033858 76 PRIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIREL-QQRLGFTAVYVTHDQDEAlAVSDRIIVMKDGEIAQSGAPRELYEAPAS---- 232
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAELLARTGAdtle 234
|
....*
gi 1028514096 233 -AFIA 236
Cdd:NF033858 235 aAFIA 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-223 |
1.86e-15 |
|
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: 73.99 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGAF--TAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:cd03369 5 GEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSgLRKAEAREKAEEGLKLvglagmghrlpaelSGGQQQRVAVARALVLEPQVLLL 162
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFDEYSD-EEIYGALRVSEGGLNL--------------SQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 163 DEPLSNL----DARLRRRVRTEIRelqqrlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAP 223
Cdd:cd03369 150 DEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-229 |
3.56e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 4 VKPG--SVTFKNVRKTFGAFTAIPDLS---LTIEPGTLVTLLGPSGCGKTTTLR-MLAGLEHPTSGRILIGDQdVTMLPa 77
Cdd:PLN03232 608 LQPGapAISIKNGYFSWDSKTSKPTLSdinLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-VAYVP- 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 78 nerDVSMVFQSyalfphmTALDNVAYG--LQSSGLRKAEAREKAEEGLKLVG---LAGMGHRlPAELSGGQQQRVAVARA 152
Cdd:PLN03232 686 ---QVSWIFNA-------TVRENILFGsdFESERYWRAIDVTALQHDLDLLPgrdLTEIGER-GVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 153 LVLEPQVLLLDEPLSNLDARLRRRVRTEI--RELQqrlGFTAVYVThDQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVFDSCmkDELK---GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-239 |
5.58e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.52 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 3 SVKPG---SVTFKNVrkTFGAFTAIP----DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD------ 69
Cdd:TIGR00957 628 TIKPGegnSITVHNA--TFTWARDLPptlnGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayvp 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 70 -----QDVTM-------LPANERDVSMVFQSYALFPHMTALdnvayglqSSGLRKaearEKAEEGLKlvglagmghrlpa 137
Cdd:TIGR00957 706 qqawiQNDSLrenilfgKALNEKYYQQVLEACALLPDLEIL--------PSGDRT----EIGEKGVN------------- 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 138 eLSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRL-GFTAVYVTHDQdEALAVSDRIIVMKDGE 216
Cdd:TIGR00957 761 -LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGK 838
|
250 260
....*....|....*....|...
gi 1028514096 217 IAQSGAPRELYEAPASafIADFM 239
Cdd:TIGR00957 839 ISEMGSYQELLQRDGA--FAEFL 859
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-229 |
6.02e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP--ANERDVSMVFQSYALFPHmTALDNVAY 103
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAMVQQDPVVLAD-TFLANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 104 GLQSSglrkaeaREKAEEGLKLVGLAGMGHRLPA-----------ELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:PRK10790 438 GRDIS-------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 173 LRRRVRTEIRELQQRLgfTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEA 229
Cdd:PRK10790 511 TEQAIQQALAAVREHT--TLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-207 |
1.02e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 73.17 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 32 EPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdQDvtmlPANERDVSMVFQSYALFPHMTALDN----------- 100
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF----DD----PPDWDEILDEFRGSELQNYFTKLLEgdvkvivkpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 ------VAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLR 174
Cdd:cd03236 96 vdlipkAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190
....*....|....*....|....*....|...
gi 1028514096 175 RRVRTEIRELQQRLGFTAVyVTHDqdeaLAVSD 207
Cdd:cd03236 176 LNAARLIRELAEDDNYVLV-VEHD----LAVLD 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-276 |
1.22e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.00 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 8 SVTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTlRMLAGLEHPTSGRiliGDQDVTMLPANERDVSMVFQ 87
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 SY-----ALFPHMTALDNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLL 162
Cdd:NF000106 89 *Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 163 DEPLSNLDARLRRRVRTEIRELqQRLGFTAVYVTHDQDEA------LAVSDRIIVMKDG---EIAQSGAPRELYEAPASA 233
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAeqlaheLTVIDRGRVIADGkvdELKTKVGGRTLQIRPAHA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1028514096 234 FIADFM----GEANVVGCEVIRLDGPDAMVRVGGI-DYRLSAGNARLG 276
Cdd:NF000106 248 AELDRMvgaiAQAGLDGIAGATADHEDGVVNVPIVsDEQLSAVVGMLG 295
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-221 |
1.35e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGleHP----TSGRILIGDQDVTMLPANERD---VSM 84
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEERAhlgIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 VFQSYALFPHMTALD--NVAYG--LQSSGLRKAEAREKAE---EGLKLVGL-AGMGHRLPAE-LSGGQQQRVAVARALVL 155
Cdd:CHL00131 89 AFQYPIEIPGVSNADflRLAYNskRKFQGLPELDPLEFLEiinEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 156 EPQVLLLDEPLSNLDARLRRRVRTEIRELqQRLGFTAVYVTHDQ---DeaLAVSDRIIVMKDGEIAQSG 221
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQrllD--YIKPDYVHVMQNGKIIKTG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-198 |
1.66e-14 |
|
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: 74.59 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTFGAFTAI-PDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILigdqdvtmlPANERDVSMVFQS 88
Cdd:TIGR03719 6 TMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 YALFPHMTALDNVAYGLQSsgLRKAEAR----------------EKAEEGLKLVGL--AGMGH-------------RLP- 136
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAE--IKDALDRfneisakyaepdadfdKLAAEQAELQEIidAADAWdldsqleiamdalRCPp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 137 -----AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDArlrRRVRTEIRELQQRLGfTAVYVTHD 198
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-207 |
2.36e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 30 TIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRiligdqdvtmlPANERDVSMVFQSYA---LFPHMTALDN----VA 102
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-----------YEEEPSWDEVLKRFRgteLQNYFKKLYNgeikVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQ-------------SSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNL 169
Cdd:PRK13409 164 HKPQyvdlipkvfkgkvRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|....*...
gi 1028514096 170 DARLRRRVRTEIRELQQrlGFTAVYVTHDqdeaLAVSD 207
Cdd:PRK13409 244 DIRQRLNVARLIRELAE--GKYVLVVEHD----LAVLD 275
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-219 |
2.82e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTM---LPANERDVSMVFQSY---ALFPHMTALD 99
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspLDAVKKGMAYITESRrdnGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYG--LQSSGLRKA-------EAREKAEEGLKLVGL--AGMGHRLpAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:PRK09700 361 NMAISrsLKDGGYKGAmglfhevDEQRTAENQRELLALkcHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 169 LDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQ 219
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
62-229 |
2.95e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.30 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 62 SGRILIGDQDVTmlPANERDV----SMVFQSYALFpHMTALDNVAYGlqssglRKAEAREKAEEGLKLVGLAGMGHRLPA 137
Cdd:PTZ00265 1276 SGKILLDGVDIC--DYNLKDLrnlfSIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPN 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 138 E-----------LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHdQDEALAVS 206
Cdd:PTZ00265 1347 KydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRS 1425
|
170 180
....*....|....*....|....*...
gi 1028514096 207 DRIIVM----KDGEIAQS-GAPRELYEA 229
Cdd:PTZ00265 1426 DKIVVFnnpdRTGSFVQAhGTHEELLSV 1453
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-230 |
6.26e-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: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLE----HPTSGRILIGDQDVTMLPANER------DVSMVFQ- 87
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 -SYALFPHMTALDNVAYGLQSSGL------RKAEAREKAEEGLKLVGLAGmgHR-----LPAELSGGQQQRVAVARALVL 155
Cdd:COG4170 98 pSSCLDPSAKIGDQLIEAIPSWTFkgkwwqRFKWRKKRAIELLHRVGIKD--HKdimnsYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 156 EPQVLLLDEPLSNLDArlrrRVRTEIRELQQRL----GFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:COG4170 176 QPRLLIADEPTNAMES----TTQAQIFRLLARLnqlqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-234 |
6.33e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNV--RKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:PLN03232 1233 GSIKFEDVhlRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQS-SGLRKAEAREKAEEGLKL--VGLAGMGHRLPAELSGGQQQRVAVARALVLEPQV 159
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDPFSEHNdADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRElqQRLGFTAVYVTHDQDEALAVsDRIIVMKDGEIAQSGAPRELYEAPASAF 234
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-170 |
1.41e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 29 LTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIgDQDVTML------PANE------------RDVSMVFQSYA 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLIVArlqqdpPRNVegtvydfvaegiEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 91 LFPHMTALD------NVAYGLQS----SGLRKAEAREKaeEGLKLVGLAGmgHRLPAELSGGQQQRVAVARALVLEPQVL 160
Cdd:PRK11147 103 DISHLVETDpseknlNELAKLQEqldhHNLWQLENRIN--EVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170
....*....|
gi 1028514096 161 LLDEPLSNLD 170
Cdd:PRK11147 179 LLDEPTNHLD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-217 |
1.94e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 2 ISVKPGSVTFKnVRKTFGAftAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRI-LIGDQDVTMLPANER 80
Cdd:PRK10762 249 LDKAPGEVRLK-VDNLSGP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtLDGHEVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 DVSMVFQSY-----ALFPHM--------TALDNVAYGlqSSGLRKAEAREKAEEGLKL--VGLAGMGHRLpAELSGGQQQ 145
Cdd:PRK10762 326 ANGIVYISEdrkrdGLVLGMsvkenmslTALRYFSRA--GGSLKHADEQQAVSDFIRLfnIKTPSMEQAI-GLLSGGNQQ 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 146 RVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-236 |
3.24e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIgdqdvtmlpanERDVSMVFQSyALFPHMTALDNVAYGL 105
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQ-AWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 QSSGLRKAEA-REKAEEGlklvGLAGMGHRLPAE-------LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRV 177
Cdd:PTZ00243 746 EEDAARLADAvRVSQLEA----DLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 178 RTEIreLQQRL-GFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEAPASAFIA 236
Cdd:PTZ00243 822 VEEC--FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-215 |
5.70e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLeHPT---SGRILIGDQdvtmlPANERDVS----- 83
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGE-----VCRFKDIRdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 ---MVFQSYALFPHMTALDNVAYG--LQSSGL-RKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEP 157
Cdd:NF040905 79 givIIHQELALIPYLSIAENIFLGneRAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 158 QVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDG 215
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-215 |
6.95e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.97 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGAFTAIPDLS------LTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANERDVSMVFq 87
Cdd:cd03290 1 VQVTNGYFSWGSGLAtlsninIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 syalfphmtaldNVAYGLQSSGLRKAEAREKAEEG-------LKLVGLA----------------GMGHRlPAELSGGQQ 144
Cdd:cd03290 80 ------------SVAYAAQKPWLLNATVEENITFGspfnkqrYKAVTDAcslqpdidllpfgdqtEIGER-GINLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028514096 145 QRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTE-IRELQQRLGFTAVYVTHdQDEALAVSDRIIVMKDG 215
Cdd:cd03290 147 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-230 |
1.05e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 19 GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP----TSGRILIGDQDVTMLPANER------DVSMVFQ- 87
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERrklvghNVSMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 88 -SYALFPH-------MTALDNVAYG---LQSSGLRKaearEKAEEGLKLVGLA---GMGHRLPAELSGGQQQRVAVARAL 153
Cdd:PRK15093 98 pQSCLDPServgrqlMQNIPGWTYKgrwWQRFGWRK----RRAIELLHRVGIKdhkDAMRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 154 VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-217 |
1.27e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.70 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGL-EHPTSGRILIGDQDV---TMLPANERDVSMVFQS---YALFPHMTAL 98
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirNPAQAIRAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 99 DNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHR-----LP-AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR 172
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaspfLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1028514096 173 LRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-230 |
1.42e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAI---PDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGD----QDVTmLPANERD 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHmTALDNVAYGLQSSGLRKAEAREKAEEGL-------------------------------------- 123
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakcagdlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 124 -------------KLVGLAGMGHRLP-----------AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRT 179
Cdd:PTZ00265 541 yqtikdsevvdvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 180 EIRELQQRLGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPRELYEAP 230
Cdd:PTZ00265 621 TINNLKGNENRITIIIAH-RLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-234 |
2.52e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.27 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 4 VKPGSVTFKNVRKTF--GAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE-- 79
Cdd:PTZ00243 1304 VQAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElr 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTALdNVAYGLQSSGlrkaearEKAEEGLKLVGLAGmghRLPAELSG--------------GQQQ 145
Cdd:PTZ00243 1384 RQFSMIPQDPVLFDGTVRQ-NVDPFLEASS-------AEVWAALELVGLRE---RVASESEGidsrvleggsnysvGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 146 RVAVARALVLEPQ-VLLLDEPLSNLDARLRRRVRTEIRELQQrlGFTAVYVTHdQDEALAVSDRIIVMKDGEIAQSGAPR 224
Cdd:PTZ00243 1453 LMCMARALLKKGSgFILMDEATANIDPALDRQIQATVMSAFS--AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPR 1529
|
250
....*....|
gi 1028514096 225 ELYEAPASAF 234
Cdd:PTZ00243 1530 ELVMNRQSIF 1539
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-218 |
3.91e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 28 SLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTmlPANERDV---SMVF-----QSYALFPHMTALD 99
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDAiraGIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 100 NVAYGLQSSGLR-------KAEArEKAEEGLKLVGLAGMGHRLP-AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDA 171
Cdd:PRK11288 351 NINISARRHHLRagclinnRWEA-ENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1028514096 172 RLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:PRK11288 430 GAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-217 |
5.93e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGlEHP---TSGRILIGDQ--------DVtmlpanERDVSMVfqSYALfpH 94
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPqgySNDLTLFGRRrgsgetiwDI------KKHIGYV--SSSL--H 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 95 M------TALDNVAYG-LQSSGLRKA---EAREKAEEGLKLVGLAGMGHRLP-AELSGGQQQRVAVARALVLEPQVLLLD 163
Cdd:PRK10938 347 LdyrvstSVRNVILSGfFDSIGIYQAvsdRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 164 EPLSNLDA--RL--RRRVRTEIRELQQRLGFTAvyvTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK10938 427 EPLQGLDPlnRQlvRRFVDVLISEGETQLLFVS---HHAEDAPACITHRLEFVPDGDI 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-211 |
9.18e-12 |
|
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: 62.97 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSlTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdqdvtmlpanERDvsmvfqs 88
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWD------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 89 yalfphmtaLDNVAYGLQSsglrkaearekaeeglklvglagmghrlpAELSGGQQQRVAVARALVLEPQVLLLDEPLSN 168
Cdd:cd03222 60 ---------GITPVYKPQY-----------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1028514096 169 LDARLRRRVRTEIRELQQRLGFTAVYVTHDQDEALAVSDRIIV 211
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-172 |
2.07e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.26 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 6 PGSVTFKNVRKTFGAFTA----IPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHP--TSGRILIGDQDVTmlPANE 79
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD--KNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 80 RDVSMVFQSYALFPHMTaldnvayglqssglrkaeAREKAEEGLKLVGlagmghrlpaeLSGGQQQRVAVARALVLEPQV 159
Cdd:cd03232 79 RSTGYVEQQDVHSPNLT------------------VREALRFSALLRG-----------LSVEQRKRLTIGVELAAKPSI 129
|
170
....*....|...
gi 1028514096 160 LLLDEPLSNLDAR 172
Cdd:cd03232 130 LFLDEPTSGLDSQ 142
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-172 |
2.20e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 33 PGTLVTLLGPSGCGKTTTLRMLAglEHPTSGRILIGDQDVTMLPANE---RDVSMVFQSYALFPHMT---ALDNVAYGLQ 106
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSsfqRSIGYVQQQDLHLPTSTvreSLRFSAYLRQ 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 107 SSGLRKAEAREKAEEGLKL----------VGLAGMGhrlpaeLSGGQQQRVAVARALVLEPQVLL-LDEPLSNLDAR 172
Cdd:TIGR00956 866 PKSVSKSEKMEYVEEVIKLlemesyadavVGVPGEG------LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-197 |
2.47e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.77 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 24 IPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLeHPTSGRILIGDQDVTMLPANERdvsmvfqsyalfPHM---TALDN 100
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAKGKLFYVPQR------------PYMtlgTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 VAYGLQSSGLRKAEAREKA-EEGLKLVGLagmGHRLPAE------------LSGGQQQRVAVARALVLEPQVLLLDEPLS 167
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDlEQILDNVQL---THILEREggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 1028514096 168 NLDARLRRRvrteIRELQQRLGFTAVYVTH 197
Cdd:TIGR00954 612 AVSVDVEGY----MYRLCREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-170 |
3.38e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTF--KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGdqdvTMLpanerDVSM 84
Cdd:PRK11147 316 GKIVFemENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKL-----EVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 vFQSY--ALFPHMTALDNVAYGLQS---SGlRKAEAREKAEEGLklvgLAGMGHRLPAE-LSGGQQQRVAVARaLVLEPQ 158
Cdd:PRK11147 387 -FDQHraELDPEKTVMDNLAEGKQEvmvNG-RPRHVLGYLQDFL----FHPKRAMTPVKaLSGGERNRLLLAR-LFLKPS 459
|
170
....*....|...
gi 1028514096 159 VLL-LDEPLSNLD 170
Cdd:PRK11147 460 NLLiLDEPTNDLD 472
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-216 |
3.52e-11 |
|
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: 61.85 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 30 TIEPGTLVTLL-GPSGCGKTTTLRML-AGL--EHPTSGRILIGDQDVTMLPANERDVSMVFQS-----YALFPHMTALDN 100
Cdd:cd03240 17 EIEFFSPLTLIvGQNGAGKTTIIEALkYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 101 VAYGLQssglrkaearekaEEGLKLVglagmgHRLPAELSGGQQQ------RVAVARALVLEPQVLLLDEPLSNLDA-RL 173
Cdd:cd03240 97 VIFCHQ-------------GESNWPL------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1028514096 174 RRRVRTEIRELQQRLGFTAVYVTHDqDEALAVSDRII-VMKDGE 216
Cdd:cd03240 158 EESLAEIIEERKSQKNFQLIVITHD-EELVDAADHIYrVEKDGR 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-217 |
5.27e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 137 AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGE 216
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
.
gi 1028514096 217 I 217
Cdd:PRK13549 483 L 483
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-238 |
7.75e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 21 FTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdqdvtmlpanER--DVSMVFQSYALFPHMTAL 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------------DRngEVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 99 DNVAYGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVR 178
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 179 TEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL---YEapasAFIADF 238
Cdd:PRK13546 184 DKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYE----AFLNDF 241
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-174 |
1.53e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.89 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPanERDVSMVFQSYALFPHMTALDNVAYgl 105
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKF-- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 106 QSSGLRKAEAREKAEEGLKLVGLAGmghRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLR 174
Cdd:PRK13541 94 WSEIYNSAETLYAAIHYFKLHDLLD---EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-198 |
1.66e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 10 TFKNVRKTFGAFTAI-PDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGR------ILIGdqdvtMLPanerdv 82
Cdd:PRK11819 8 TMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVG-----YLP------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 smvfQSYALFPHMTALDNVAYGLQSsgLRKAEAR----------------EKAEEGLKLVGL--AGMGH----------- 133
Cdd:PRK11819 77 ----QEPQLDPEKTVRENVEEGVAE--VKAALDRfneiyaayaepdadfdALAAEQGELQEIidAADAWdldsqleiamd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 134 --RLP------AELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDArlrrrvrteirE----LQQRL----GfTAVYVTH 197
Cdd:PRK11819 151 alRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-----------EsvawLEQFLhdypG-TVVAVTH 218
|
.
gi 1028514096 198 D 198
Cdd:PRK11819 219 D 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-215 |
1.97e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGleHPTSGRILiGDQDVTMLPANERDVSMVF----QSYALFPHMTALDNV 101
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKKQETFARISgyceQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 102 AYglqSSGLRKAEAREKAE--------------EGLK--LVGLAGMghrlpAELSGGQQQRVAVARALVLEPQVLLLDEP 165
Cdd:PLN03140 975 IY---SAFLRLPKEVSKEEkmmfvdevmelvelDNLKdaIVGLPGV-----TGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 166 LSNLDAR----LRRRVRTEIRElqqrlGFTAVYVTH----DQDEALavsDRIIVMKDG 215
Cdd:PLN03140 1047 TSGLDARaaaiVMRTVRNTVDT-----GRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-229 |
4.23e-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: 61.50 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKN--VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLPANE--RDV 82
Cdd:TIGR00957 1283 GRVEFRNycLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSglrkaearEKAEEGLKLVGLAGMGHRLPAE-----------LSGGQQQRVAVAR 151
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLRMNLDPFSQYSD--------EEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRTEIRelQQRLGFTAVYVTHDQDEALAVSdRIIVMKDGEIAQSGAPRELYEA 229
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-216 |
5.11e-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: 57.38 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 33 PGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMlpanerdvsmvfqsyalfphmtaldnvayglqssglrk 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 113 aearekaeEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIR-----ELQQR 187
Cdd:smart00382 43 --------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180 190
....*....|....*....|....*....|....
gi 1028514096 188 LGFTAVYVTH-----DQDEALAVSDRIIVMKDGE 216
Cdd:smart00382 115 KNLTVILTTNdekdlGPALLRRRFDRRIVLLLIL 148
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-217 |
7.52e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRI------LIG--DQDVTMLPANER 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGyyAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 81 DvsmvfqsyaLFPHMtaldnvayglqsSGLRKAEAREKAeeglklvgLAGMGHRL----------PAELSGGQQQRVAVA 150
Cdd:PRK15064 400 T---------LFDWM------------SQWRQEGDDEQA--------VRGTLGRLlfsqddikksVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDARlrrrvrtEIRELQQRL----GfTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDME-------SIESLNMALekyeG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-218 |
1.71e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 139 LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-221 |
2.04e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 9 VTFKNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLE--HPTSGRILIGDQDVTMLPANER---DVS 83
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHM-------TALDNVAYGLQSSGLRKAEAREKAEEGLKLVglagmghRLPAEL---------SGGQQQRV 147
Cdd:PRK09580 82 MAFQYPVEIPGVsnqfflqTALNAVRSYRGQEPLDRFDFQDLMEEKIALL-------KMPEDLltrsvnvgfSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 148 AVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQ-RLGFtaVYVTHDQDEALAVS-DRIIVMKDGEIAQSG 221
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSF--IIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-219 |
2.80e-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: 57.17 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKN--VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHpTSGRILIGDQDVTMLPANE--RDV 82
Cdd:cd03289 1 GQMTVKDltAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALF--PHMTALDnvAYGLQSSglrkAEAREKAEEglklVGLAGMGHRLPAE-----------LSGGQQQRVAV 149
Cdd:cd03289 80 GVIPQKVFIFsgTFRKNLD--PYGKWSD----EEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 150 ARALVLEPQVLLLDEPLSNLDARLRRRVRteiRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQ 219
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-170 |
3.22e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 12 KNVRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLA-----GLehPTSGRIL------IGDQ---------- 70
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILhveqevVGDDttalqcvlnt 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 71 DVTMLPANERDVSMVFQSYAL-FPHMTALDNVAyglQSSGLRKAEAREKAEEGLK-----------------LVGL---A 129
Cdd:PLN03073 259 DIERTQLLEEEAQLVAQQRELeFETETGKGKGA---NKDGVDKDAVSQRLEEIYKrlelidaytaearaasiLAGLsftP 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1028514096 130 GMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-226 |
1.01e-08 |
|
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: 56.84 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdqdvtmlpANERDVSMVFQSYALFPHmTALDNVAYGL 105
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSPQTSWIMPG-TIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 QSSGLR-----KAEAREK-----AEEGLKLVGLAGMghrlpaELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDarlrr 175
Cdd:TIGR01271 512 SYDEYRytsviKACQLEEdialfPEKDKTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLD----- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 176 rVRTEiRELQQR------LGFTAVYVThDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:TIGR01271 581 -VVTE-KEIFESclcklmSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-198 |
1.20e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 39 LLGPSGCGKTTTLRMLAGLEHPTSGRILIG----------DQ---------DVTML-------PANERDvsmvfQSYALf 92
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklrqDQfafeeftvlDTVIMghtelweVKQERD-----RIYAL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 93 PHMTALDnvayglqssGLRKAE------------AREKAEEGLKLVGLAGMGHRLP-AELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK15064 106 PEMSEED---------GMKVADlevkfaemdgytAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1028514096 160 LLLDEPLSNLDarlrrrVRTeIRELQQRL---GFTAVYVTHD 198
Cdd:PRK15064 177 LLLDEPTNNLD------INT-IRWLEDVLnerNSTMIIISHD 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-216 |
1.55e-08 |
|
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: 55.25 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRIligdqdvtmlpANERDVSMVFQSYALFPHmTALDNVAYGL 105
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 106 QSSGLR-----KAEAREK-----AEEGLKLVGLAGMghrlpaELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDarlrr 175
Cdd:cd03291 123 SYDEYRyksvvKACQLEEditkfPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD----- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1028514096 176 rVRTEIRELQQRL-----GFTAVYVThDQDEALAVSDRIIVMKDGE 216
Cdd:cd03291 192 -VFTEKEIFESCVcklmaNKTRILVT-SKMEHLKKADKILILHEGS 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-234 |
2.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKNVRKTFGaftaiPDL-------SLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIGDQDVTMLP-AN 78
Cdd:PLN03130 1236 GSIKFEDVVLRYR-----PELppvlhglSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 79 ERDV-SMVFQSYALFPhmtalDNVAYGLQSSGLRKA----EAREKAEegLKLV------GLAGMGHRLPAELSGGQQQRV 147
Cdd:PLN03130 1311 LRKVlGIIPQAPVLFS-----GTVRFNLDPFNEHNDadlwESLERAH--LKDVirrnslGLDAEVSEAGENFSVGQRQLL 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 148 AVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRElqQRLGFTAVYVTHDQDEALAvSDRIIVMKDGEIAQSGAPRELY 227
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
....*..
gi 1028514096 228 EAPASAF 234
Cdd:PLN03130 1461 SNEGSAF 1467
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-221 |
2.69e-08 |
|
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: 53.10 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLrmLAGLEhpTSGRILIgdqdVTMLPANERDVSMVFQSyalfphMTALDNVA 102
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLY--ASGKARL----ISFLPKFSRNKLIFIDQ------LQFLIDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQSSGlRKAearekaeeglklvglagmghrlpAELSGGQQQRVAVARALVLEPQ--VLLLDEPLSNLDARLRRRVRTE 180
Cdd:cd03238 76 LGYLTLG-QKL-----------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1028514096 181 IRELQQrLGFTAVYVTHDqDEALAVSDRIIVMKDGEIAQSG 221
Cdd:cd03238 132 IKGLID-LGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGG 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-226 |
1.92e-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: 52.99 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 7 GSVTFKN--VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHpTSGRILIG--DQDVTMLPANERDV 82
Cdd:TIGR01271 1216 GQMDVQGltAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDgvSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 83 SMVFQSYALFPHMTALDNVAYGLQSSglrkAEAREKAEEglklVGLAGMGHRLPAE-----------LSGGQQQRVAVAR 151
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDPYEQWSD----EEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028514096 152 ALVLEPQVLLLDEPLSNLDARLRRRVRteiRELQQRLGFTAVYVTHDQDEALAVSDRIIVMKDGEIAQSGAPREL 226
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-239 |
2.04e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 11 FKNVRKTFgAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEH----PTSGRIL---IGDQDvtMLPANERDVS 83
Cdd:TIGR00956 65 LKKFRDTK-TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITydgITPEE--IKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 84 MVFQSYALFPHMT---ALDNVAY----GLQSSGL-RKAEAREKAEEGLKLVGLA-----GMGHRLPAELSGGQQQRVAVA 150
Cdd:TIGR00956 142 YNAETDVHFPHLTvgeTLDFAARcktpQNRPDGVsREEYAKHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 151 RALVLEPQVLLLDEPLSNLDA----RLRRRVRTEIRELQqrlgfTAVYVTHDQ--DEALAVSDRIIVMKDGEIAQSGAPR 224
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSatalEFIRALKTSANILD-----TTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFGPAD 296
|
250 260
....*....|....*....|...
gi 1028514096 225 EL--------YEAPASAFIADFM 239
Cdd:TIGR00956 297 KAkqyfekmgFKCPDRQTTADFL 319
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-217 |
5.10e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 14 VRKTFGAFTAIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRI---------LIGDQDVTMLPANERDVSm 84
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLRADESPLQ- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 85 vfqsyalfpHMTALdnvayglqssglrkaeAREKAEEGLK--LVGLAGMGHRLP---AELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK10636 397 ---------HLARL----------------APQELEQKLRdyLGGFGFQGDKVTeetRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028514096 160 LLLDEPLSNLDARLRRRVRTEIRELQQRLgftaVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-197 |
8.33e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 23 AIPDLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILIgdqdvtmlpanERDVSMVFQSYALFPHMTALDNVA 102
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 103 YGLQSSGLRKAEAREKAEEGLKLVGLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIR 182
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170
....*....|....*
gi 1028514096 183 ELQQRlGFTAVYVTH 197
Cdd:PRK13545 188 EFKEQ-GKTIFFISH 201
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-170 |
1.59e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 26 DLSLTIEPGTLVTLLGPSGCGKTTTLRMLAGLEHPTSGRILigdqdvtmlpaNERDVSM-VFQSYalfpHMTALDnvayg 104
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMaVFSQH----HVDGLD----- 586
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028514096 105 LQSSGLR------KAEAREKAEEGLKLVGLAGMGHRLPA-ELSGGQQQRVAVARALVLEPQVLLLDEPLSNLD 170
Cdd:PLN03073 587 LSSNPLLymmrcfPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-232 |
7.50e-06 |
|
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: 47.70 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 134 RLPAELSGGQQQRVAVARAL------VLepqvLLLDEPLSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDeALAVSD 207
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIgsgltgVL----YVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDED-TIRAAD 557
|
90 100 110
....*....|....*....|....*....|.
gi 1028514096 208 RIIVM------KDGEIAQSGAPRELYEAPAS 232
Cdd:TIGR00630 558 YVIDIgpgageHGGEVVASGTPEEILANPDS 588
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
280-344 |
8.24e-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: 43.38 E-value: 8.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028514096 280 LAVRPGSISISQPGGqGVAGRVLHCAYLGGHVEYEVETEIGTLFII--DHMAETGLPPASDVTLGFR 344
Cdd:pfam08402 1 LAIRPEKIRLAAAAN-GLSGTVTDVEYLGDHTRYHVELAGGEELVVrvPNAHARPPAPGDRVGLGWD 66
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
139-217 |
1.13e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 139 LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEI 217
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
31-234 |
1.36e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.06 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 31 IEPGTLVTLLGPSGCGKTTT----LRMLAGLEhptsGRILIGDQDVTMLPAN--ERDVSMVFQSYALFPHMTALdNVAYG 104
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILFSGSIRF-NLDPE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 105 LQSSGLRKAEAREKAEegLKLV------GLAGMGHRLPAELSGGQQQRVAVARALVLEPQVLLLDEPLSNLDAR----LR 174
Cdd:cd03288 119 CKCTDDRLWEALEIAQ--LKNMvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAteniLQ 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 175 RRVRTEIRELqqrlgfTAVYVTHDQDEALAvSDRIIVMKDGEIAQSGAPRELYEAPASAF 234
Cdd:cd03288 197 KVVMTAFADR------TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
139-226 |
1.39e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 139 LSGGQQQRVAVARALVLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAVSDRIIVMKDGEIA 218
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
....*...
gi 1028514096 219 QSGAPREL 226
Cdd:PRK10938 215 ETGEREEI 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-210 |
1.92e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 28 SLTIEPGTLVTLLGPSGCGKTTTLRMLAG--------------------------LEHPTSGRILIGDQDVTMLPANERD 81
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsytfpgnwqlawvnqetpaLPQPALEYVIDGDREYRQLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 82 VSMVFQSYALFPHMTALDNV-AYGLQSsglrkaeareKAEEGLKLVGLAGMGHRLP-AELSGGQQQRVAVARALVLEPQV 159
Cdd:PRK10636 101 ANERNDGHAIATIHGKLDAIdAWTIRS----------RAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1028514096 160 LLLDEPLSNLDarLRRRVRTEiRELQQRLGfTAVYVTHDQDEALAVSDRII 210
Cdd:PRK10636 171 LLLDEPTNHLD--LDAVIWLE-KWLKSYQG-TLILISHDRDFLDPIVDKII 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
87-225 |
3.44e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 87 QSYALFPHMTaLDNVaYGLQSSGLRKAEAREKAEEGLK-----LVGLaGMGHRLP----AELSGGQQQRVAVARALVLEP 157
Cdd:PRK00635 419 KTFAEFQQMS-LQEL-FIFLSQLPSKSLSIEEVLQGLKsrlsiLIDL-GLPYLTPeralATLSGGEQERTALAKHLGAEL 495
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028514096 158 Q--VLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDqDEALAVSDRIIVMK------DGEIAQSGAPRE 225
Cdd:PRK00635 496 IgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-EQMISLADRIIDIGpgagifGGEVLFNGSPRE 569
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
130-221 |
2.14e-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: 42.24 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028514096 130 GMGH----RLPAELSGGQQQRVAVARAL--VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQrLGFTAVYVTHDQDEAL 203
Cdd:cd03270 125 GLGYltlsRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTIR 203
|
90 100
....*....|....*....|....
gi 1028514096 204 AvSDRIIVM------KDGEIAQSG 221
Cdd:cd03270 204 A-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
139-213 |
4.16e-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: 40.42 E-value: 4.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028514096 139 LSGGQQQRVAVARAL----VLEPQVLLLDEPLSNLDARLRRRVRTEIRELQQRlGFTAVYVTHDQDEALAvSDRIIVMK 213
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
36-65 |
5.10e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 37.48 E-value: 5.10e-03
10 20 30
....*....|....*....|....*....|...
gi 1028514096 36 LVTLLGPSGCGKTTTLRMLA---GLEHPTSGRI 65
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEI 34
|
|
| |
