|
Name |
Accession |
Description |
Interval |
E-value |
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-352 |
0e+00 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 546.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-SQLHVRDRNIGFV 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGLESLPkkqrPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRP----PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGH 239
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 240 VNVLSGLVKGQKLVQGDAWVSLPGIRQDQEAQLYLRPHEVQLSRSPAAKARLPLRIEAISLIGSEVRIELAPEGWQsDEI 319
Cdd:COG1118 237 VNVLRGRVIGGQLEADGLTLPVAEPLPDGPAVAGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLEDGE-GQP 315
|
330 340 350
....*....|....*....|....*....|...
gi 1430737237 320 WEIGMSHAEFARQNPTRGELWYAVPDVGHLFVA 352
Cdd:COG1118 316 LEAEVTKEAWAELGLAPGDPVYLRPRPARVFLP 348
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-341 |
5.19e-166 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 468.02 E-value: 5.19e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVF 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHV 240
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 241 NVLSGLVKGQKLVQGDAWVSLPGIRQDQ-EAQLYLRPHEVQLSRSPAAKARLPLRIEAISLIGSEVRIELAPEGWQSDE- 318
Cdd:PRK10851 241 NRLQGTIRGGQFHVGAHRWPLGYTPAYQgPVDLFLRPWEVDISRRTSLDSPLPVQVLEVSPKGHYWQLVVQPLGWYNEPl 320
|
330 340
....*....|....*....|....*
gi 1430737237 319 --IWEiGMSHAefarqnPTRGELWY 341
Cdd:PRK10851 321 tvVMH-GDIDA------PQRGERLF 338
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-351 |
2.23e-152 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 433.37 E-value: 2.23e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQ 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:COG3842 85 DYALFPHLTVAENVAFGL----RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVN 241
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 242 VLSGLVKGqklvQGDAWVSLPG----------IRQDQEAQLYLRPHEVQLSRSPAAkARLPLRIEAISLIGSEVRIELAp 311
Cdd:COG3842 241 LLPGTVLG----DEGGGVRTGGrtlevpadagLAAGGPVTVAIRPEDIRLSPEGPE-NGLPGTVEDVVFLGSHVRYRVR- 314
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1430737237 312 egWQSDEIWEIGMSHAEFArqNPTRGELWYAVPDVGHLFV 351
Cdd:COG3842 315 --LGDGQELVVRVPNRAAL--PLEPGDRVGLSWDPEDVVV 350
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-238 |
5.70e-148 |
|
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: 417.90 E-value: 5.70e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVF 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLG 238
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-313 |
1.34e-134 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 388.28 E-value: 1.34e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQ 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:COG3839 83 SYALYPHMTVYENIAFPL----KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLG--H 239
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGspP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 240 VNVLSGLVKGQKLVQGDAWVSLPGI---RQDQEAQLYLRPHEVQLsrSPAAKARLPLRIEAISLIGSEVRIELAPEG 313
Cdd:COG3839 239 MNLLPGTVEGGGVRLGGVRLPLPAAlaaAAGGEVTLGIRPEHLRL--ADEGDGGLEATVEVVEPLGSETLVHVRLGG 313
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-243 |
2.07e-134 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 383.38 E-value: 2.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEI----RKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNV 242
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
.
gi 1430737237 243 L 243
Cdd:TIGR00968 237 L 237
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-313 |
6.80e-122 |
|
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: 355.88 E-value: 6.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKN----RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNV 242
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 243 LSGLV-KGQKLVQGDAWVSL-PGIRQDQEA-QLYLRPHEVQLSRSPAAKARLPLRIEAISLIGSEVRIELAPEG 313
Cdd:TIGR03265 241 LPGTRgGGSRARVGGLTLACaPGLAQPGASvRLAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEG 314
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-238 |
2.08e-115 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 334.98 E-value: 2.08e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03300 81 YALFPHLTVFENIAFGL----RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLG 238
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-218 |
1.71e-110 |
|
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: 321.78 E-value: 1.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03259 81 YALFPHLTVAENIAFGL----KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQV 218
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-247 |
6.47e-100 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 300.71 E-value: 6.47e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK09452 95 YALFPHMTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNV 242
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINI 250
|
....*
gi 1430737237 243 LSGLV 247
Cdd:PRK09452 251 FDATV 255
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-213 |
2.17e-99 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 295.07 E-value: 2.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLhvrDRNIGF 78
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP---GPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLEslpkKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLE----LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-239 |
6.40e-97 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 290.45 E-value: 6.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFV 79
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFglesLPKKQRPSKQEIRQRVAKLLEMIQLP--ELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG1125 82 IQQIGLFPHMTVAENIAT----VPRLLGWDKERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFL 237
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
..
gi 1430737237 238 GH 239
Cdd:COG1125 238 GA 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-211 |
2.30e-96 |
|
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: 285.90 E-value: 2.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHvrdRNIGF 78
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLEL----QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMS 211
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-304 |
8.59e-93 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 281.73 E-value: 8.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVF 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGL----KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGH- 239
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSp 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 240 -VNVLSGLVKGQKL-VQGDAWVSLP-----GIRQDQEAQLYLRPHEVQLSrspAAKARLPLRIEAISLIGSE 304
Cdd:PRK11650 239 aMNLLDGRVSADGAaFELAGGIALPlgggyRQYAGRKLTLGIRPEHIALS---SAEGGVPLTVDTVELLGAD 307
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-218 |
2.56e-91 |
|
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: 272.98 E-value: 2.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGL----KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQV 218
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-287 |
9.29e-89 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 270.52 E-value: 9.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 33 LLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQHYALFRHLTVAENIAFGLeslpKKQRPSKQE 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGL----KMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 113 IRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIF 192
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 193 VTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNVLSGLVK---GQKLVQGDAWVSLPGIRQD-- 267
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIerkSEQVVLAGVEGRRCDIYTDvp 236
|
250 260
....*....|....*....|....
gi 1430737237 268 ----QEAQLYLRPHEVQLSRSPAA 287
Cdd:TIGR01187 237 vekdQPLHVVLRPEKIVIEEEDEA 260
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-309 |
6.58e-88 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 268.87 E-value: 6.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQaLKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:NF040840 81 YMLFPHKTVFENIAFGL----KLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNV 242
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 243 LSGLVK----GQKLVQGDAWVSLPGIRQDQeAQLYLRPHEVQLSRSP---AAKARLPLRIEAISLIGSEVRIEL 309
Cdd:NF040840 237 IEGVAEkggeGTILDTGNIKIELPEEKKGK-VRIGIRPEDITISTEKvktSARNEFKGKVEEIEDLGPLVKLTL 309
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-283 |
9.57e-88 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 268.90 E-value: 9.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQHYALFR 87
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PRK11432 92 HMSLGENVGYGL----KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 168 DAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNVLSGLV 247
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPATL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1430737237 248 KGQKLVQGDAWVSLPGIRQ----DQEAQLYLRPHEVQLSR 283
Cdd:PRK11432 248 SGDYVDIYGYRLPRPAAFAfnlpDGECTVGVRPEAITLSE 287
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-242 |
3.28e-85 |
|
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: 258.03 E-value: 3.28e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQaLKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGL----KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNV 242
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-238 |
8.49e-85 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 257.23 E-value: 8.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFV 79
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFglesLPKKQRPSKQEIRQRVAKLLEMIQLP--ELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL----VPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFL 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
.
gi 1430737237 238 G 238
Cdd:cd03295 237 G 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-221 |
1.06e-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: 256.83 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNIG 77
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHLTVAENIAFGLESLPKKqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
9.62e-83 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 251.50 E-value: 9.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFG----GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL------HVR 72
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserelaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 DRNIGFVFQHYALFRHLTVAENIAFGLEslpkKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA 152
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLL----LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDqEEALELSDQVVVMSQGQVE 216
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
1.96e-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: 250.48 E-value: 1.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR---- 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 75 --NIGFVFQHYALFRHLTVAENIAFGLEslpkKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA 152
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEAlELSDQVVVMSQGQV 215
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-240 |
9.57e-82 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 249.53 E-value: 9.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ-----LHVRdRNIG 77
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdiNKLR-RKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHLTVAENIAFGLESLPKKqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKM---SKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFL 237
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
...
gi 1430737237 238 GHV 240
Cdd:COG1126 237 SKV 239
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-309 |
3.99e-79 |
|
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: 246.94 E-value: 3.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDqINKHFGGFqALkNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG----DDVSQLHV--RDR 74
Cdd:COG4148 1 MMLEVD-FRLRRGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqDSARGIFLppHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 75 NIGFVFQHYALFRHLTVAENIAFGLESLPKKQRPSKQEirqRVAKLLEmiqLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFD---EVVELLG---IGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVF 234
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 235 DFLGHVNVLSGLVKGQ---------KLVQGDAWVSLPGIRQDQEAQLYLRPHEVQLSRSPA----AKARLPLRIEAISLI 301
Cdd:COG4148 232 GGEEAGSVLEATVAAHdpdygltrlALGGGRLWVPRLDLPPGTRVRVRIRARDVSLALEPPegssILNILPGRVVEIEPA 311
|
330
....*....|.
gi 1430737237 302 GS---EVRIEL 309
Cdd:COG4148 312 DGgqvLVRLDL 322
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-217 |
1.31e-78 |
|
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: 240.66 E-value: 1.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 7 QINKHFGGFQAlkNVSLDIPEgQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG---DDVSQ---LHVRDRNIGFVF 80
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLeslpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:cd03297 82 QQYALFPHLNVRENLAFGL------KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQ 217
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-287 |
1.58e-78 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 245.90 E-value: 1.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQHYA 84
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 LFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PRK11607 102 LFPHMTVEQNIAFGL----KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 165 GALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNVLS 244
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 245 GLVKGQklvQGDAWV-SLPG----IRQDQEA--------QLYLRPHEVQLSRSPAA 287
Cdd:PRK11607 258 GVLKER---QEDGLViDSPGlvhpLKVDADAsvvdnvpvHVALRPEKIMLCEEPPA 310
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-353 |
2.06e-77 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 243.01 E-value: 2.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQ 81
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:PRK11000 83 SYALYPHLSVAENMSFGL----KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLG--H 239
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 240 VNVLSGLV----KGQKLVQ--GDAWVSLP----GIRQDQEAQLYLRPHevQLSRSPAAKARLPLRIEAISLIGSEVRIEL 309
Cdd:PRK11000 239 MNFLPVKVtataIEQVQVElpNRQQVWLPvegrGVQVGANMSLGIRPE--HLLPSDIADVTLEGEVQVVEQLGNETQIHI 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1430737237 310 APEGWQSDEIWeigmshaefaRQNPTR----GELWYA--VPDVGHLFVAD 353
Cdd:PRK11000 317 QIPAIRQNLVY----------RQNDVVlveeGATFAIglPPERCHLFRED 356
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-240 |
3.59e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 241.14 E-value: 3.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD----- 73
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RNIGFVFQHYALFRHLTVAENIAFGLEsLPKKqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALAT 153
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLE-IAGV---PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFV 233
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
|
....*..
gi 1430737237 234 FDFLGHV 240
Cdd:COG1135 238 RRFLPTV 244
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-229 |
2.00e-76 |
|
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: 235.30 E-value: 2.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQH--YALFrH 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAFGLESLPKkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:COG1122 91 PTVEEDVAFGPENLGL----PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 169 AKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:COG1122 167 PRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-228 |
4.79e-76 |
|
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: 243.66 E-value: 4.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD---- 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 -RNIGFVFQH--YALFRHLTVAENIAFGLESLPKKqrpSKQEIRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALAR 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLL---SRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-216 |
5.04e-76 |
|
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: 234.70 E-value: 5.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNIG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHLTVAENIAFGLEslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLR---EHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVE 216
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-214 |
1.32e-74 |
|
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: 229.00 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH----VRDRNIGF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGleslpkkqrpskqeirqrvakllemiqlpelakrypaqLSGGQKQRVALARALATQPRIL 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-227 |
4.11e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 229.57 E-value: 4.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR-NIGFVFQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAF--GLESLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLYGLPRKEA------RERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-243 |
6.66e-72 |
|
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: 225.22 E-value: 6.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 6 DQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL------HVRDRNIGFV 79
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrELRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEV----QGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGH 239
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
....
gi 1430737237 240 VNVL 243
Cdd:cd03294 264 VDRA 267
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-214 |
7.41e-72 |
|
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: 223.11 E-value: 7.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQH--YALFRHlTV 91
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQNpdDQFFGP-TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFGLESLPKkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKV 171
Cdd:cd03225 94 EEEVAFGLENLGL----PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1430737237 172 RKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:cd03225 170 RRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
9.03e-71 |
|
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: 220.48 E-value: 9.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS----QLHVRDRNIGF 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLESLPKKqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGM---SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-238 |
7.35e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 218.86 E-value: 7.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFqaLKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLE-SLpkkqRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRpGL----KLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLG 238
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-229 |
1.10e-69 |
|
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: 218.22 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD----- 73
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RNIGFVFQHYALFRHLTVAENIAFGLESLpkkqRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALAT 153
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIA----GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-217 |
5.76e-69 |
|
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: 216.22 E-value: 5.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH-----VRD 73
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RNIGFVFQHY--ALFRHLTVAENIAfglESLPKKQRPSKQEIRQR-VAKLLEMIQLPE-LAKRYPAQLSGGQKQRVALAR 149
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIA---EPLRIHGKLSKKEARKEaVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-230 |
1.01e-67 |
|
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: 213.90 E-value: 1.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFG----GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNI 76
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHY--ALFRHLTVAENIAFGLESLpkkqrpSKQEIRQRVAKLLEMIQLP-ELAKRYPAQLSGGQKQRVALARALAT 153
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIH------GLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPES 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-227 |
1.31e-67 |
|
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: 213.18 E-value: 1.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ--LHVRdRNIGFVF 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepREAR-RQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFgLESLpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:COG4555 81 DERGLYDRLTVRENIRY-FAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-217 |
1.03e-65 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 211.97 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD----- 73
Cdd:PRK11153 2 IELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RNIGFVFQHYALFRHLTVAENIAFGLEsLPKKqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALAT 153
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLE-LAGT---PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRlVEQ 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-224 |
3.79e-65 |
|
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: 206.65 E-value: 3.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESS-----DSGRVLFGGDDVSQLHVRD---- 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RNIGFVFQHYALFRhLTVAENIAFGLESLPKKqrpSKQEIRQRVAKLLEMIQLPELAKR--YPAQLSGGQKQRVALARAL 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIK---LKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 152 ATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGL 224
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-213 |
2.93e-64 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 205.48 E-value: 2.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MS-ITIDQINKHFGGF----QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVrDRn 75
Cdd:COG4525 1 MSmLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 iGFVFQHYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQP 155
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGL----RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-215 |
4.81e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 203.36 E-value: 4.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFGLESLPKKQRpskqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRK----EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFV-THDQEEALELSDQVVVMSQGQV 215
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIaTHDLELVDRMPKRVLELEDGRL 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-229 |
6.84e-64 |
|
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: 204.99 E-value: 6.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ---LHVRD--RNIGFVFQH--YALFR 87
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDlrKKVGLVFQFpeHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 hLTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPE-LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:TIGR04521 98 -ETVYKDIAFG----PKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 167 LDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-215 |
9.91e-64 |
|
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: 203.73 E-value: 9.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFVFQ 81
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgIARTFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLESL-----------PKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARA 150
Cdd:COG0411 87 NPRLFPELTVLENVLVAAHARlgrgllaallrLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 151 LATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-215 |
2.94e-63 |
|
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: 201.90 E-value: 2.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFVFQ 81
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLES------LPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQP 155
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQArtgsglLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-215 |
4.29e-63 |
|
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: 202.20 E-value: 4.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVF 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFG-LESLPKKQRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:COG1120 82 QEPPAPFGLTVRELVALGrYPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-240 |
2.71e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 199.55 E-value: 2.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNI----GFVFQHY 83
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFRHLTVAENIAFGleslPKKQR-PSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK09493 87 YLFPHLTALENVMFG----PLRVRgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHV 240
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-230 |
1.28e-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: 205.91 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF--GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL---ESSDSGRVLFGGDDVSQL--HVRDRN 75
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELseALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 IGFVFQHY-ALFRHLTVAENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:COG1123 85 IGMVFQDPmTQLNPVTVGDQIAEALEN----LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPES 230
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-215 |
6.12e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.43 E-value: 6.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFGLesLPKK-------QRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALAR 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGR--LGRTstwrsllGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-229 |
8.28e-61 |
|
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: 196.50 E-value: 8.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV---SQLH-VRdRNIGFVFQH------YAl 85
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWeIR-KKVGMVFQNpdnqfvGA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 86 frhlTVAENIAFGLESLpkkQRPSKqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:TIGR04520 94 ----TVEDDVAFGLENL---GVPRE-EMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALeLSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:TIGR04520 166 MLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
5.71e-60 |
|
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: 191.07 E-value: 5.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR-NIGFVFQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIafgleslpkkqrpskqeirqrvakllemiqlpelakrypaQLSGGQKQRVALARALATQPRILLLD 161
Cdd:cd03230 81 EPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-215 |
4.40e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.46 E-value: 4.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQlhvRDRNIGFVFQH 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRH--LTVAENIAFGLesLPKK---QRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGR--YGRRglfRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-299 |
2.79e-58 |
|
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: 193.02 E-value: 2.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 7 QINKHFGGFQAlkNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD------SGRVLFGGDDVSQLHVRDRNIGFVF 80
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDegeivlNGRTLFDSRKGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQrvAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGM----KRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFdFLGHV 240
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 241 NVLSGLVKGQ-------KLVQGDAWVSLPGIRQD--QEAQLYLRPHEVQLSRSP--AAKAR--LPLRIEAIS 299
Cdd:TIGR02142 235 SLIEGVVAEHdqhygltALRLGGGHLWVPENLGPtgARLRLRVPARDVSLALQKpeATSIRniLPARVVEIE 306
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-217 |
3.86e-57 |
|
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: 186.10 E-value: 3.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL------HVR 72
Cdd:COG4181 9 IELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedaraRLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 DRNIGFVFQHYALFRHLTVAENIAFGLEslpkkqRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA 152
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLE------LAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 153 TQPRILLLDEPFGALDAKVRK---DLrrwLRALHDEYHFTSIFVTHDQEEAlELSDQVVVMSQGQVEQ 217
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEqiiDL---LFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-202 |
6.54e-57 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 184.61 E-value: 6.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD---SGRVLFGGDDVSQLHVRDRNIGF 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGL-ESLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALpPTIGRAQR------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALE 202
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
1.04e-56 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 185.22 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD--DVSQ-LHVRD---- 73
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKAirll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 -RNIGFVFQHYALFRHLTVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA 152
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENL---IEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALhDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRiIEQ 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
2.29e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.09 E-value: 2.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVF 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHlTVAENIAFGLESlpKKQRPSkqeiRQRVAKLLEMIQLPE--LAKRYpAQLSGGQKQRVALARALATQPRIL 158
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQL--RERKFD----RERALELLERLGLPPdiLDKPV-ERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-215 |
4.14e-56 |
|
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: 183.54 E-value: 4.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFG-GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFG-------LESLPkkQRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALAR 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRSLF--GLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-217 |
6.83e-56 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 183.29 E-value: 6.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD--DVSQ-------LHV 71
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtpsdkaiREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 72 RdRNIGFVFQHYALFRHLTVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARAL 151
Cdd:PRK11124 81 R-RNVGMVFQQYNLWPHLTVQQNL---IEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 152 ATQPRILLLDEPFGALDAKVRKDLRRWLRALHdEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHiVEQ 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-230 |
8.02e-56 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 183.46 E-value: 8.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS-------QLHVRDR- 74
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 75 -------NIGFVFQHYALFRHLTVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVAL 147
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENV---IEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 148 ARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
...
gi 1430737237 228 PES 230
Cdd:COG4598 245 PKS 247
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-215 |
1.95e-54 |
|
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: 178.46 E-value: 1.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQHYALFRHLTVAENIAFGLeS 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL-S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 102 LPKKQRPskqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRA 181
Cdd:cd03298 97 PGLKLTA---EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 1430737237 182 LHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
2.18e-54 |
|
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: 178.81 E-value: 2.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHvRDRNIgfVFQHYALFRHLTVAENIAF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-PDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 GLES-LPKKQRPSKQEIrqrVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLR 176
Cdd:TIGR01184 78 AVDRvLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1430737237 177 RWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-227 |
4.27e-54 |
|
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: 189.66 E-value: 4.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQ--ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIG 77
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFrHLTVAENIAFGLESlpkkqrPSKQEIRQ--RVAKLLEMIQlpELAKRYP-------AQLSGGQKQRVALA 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDPD------ATDEEIIEaaRLAGLHDFIE--ALPMGYDtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 149 RALATQPRILLLDEPFGALD----AKVRKDLRRWLRalhdeyHFTSIFVTHDqEEALELSDQVVVMSQGQV------EQV 218
Cdd:COG2274 624 RALLRNPRILILDEATSALDaeteAIILENLRRLLK------GRTVIIIAHR-LSTIRLADRIIVLDKGRIvedgthEEL 696
|
....*....
gi 1430737237 219 NSPTGLYAR 227
Cdd:COG2274 697 LARKGLYAE 705
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-164 |
4.74e-54 |
|
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: 175.14 E-value: 4.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ--LHVRDRNIGFVFQHYALFRHLTVAENI 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 96 AFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKR----YPAQLSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:pfam00005 81 RLGLLL----KGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-208 |
6.25e-54 |
|
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: 177.04 E-value: 6.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH-------VRDRnIGFVF 80
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNskkaskfRREK-LGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:TIGR03608 83 QNFALIENETVEENLDLGL----KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEAlELSDQVV 208
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVA-KQADRVI 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-228 |
1.13e-53 |
|
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: 179.86 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESS---DSGRVLFGGDDVSQL------ 69
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 70 HVRDRNIGFVFQH-Y-ALFRHLTVAENIAfglESLPKKQRPSKQEIRQRVAKLLEMIQLP---ELAKRYPAQLSGGQKQR 144
Cdd:COG0444 82 KIRGREIQMIFQDpMtSLNPVMTVGDQIA---EPLRIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 145 VALARALATQPRILLLDEPFGALDAKVRK---DLrrwLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQvnS 220
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAqilNL---LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRiVEE--G 233
|
....*....
gi 1430737237 221 PTG-LYARP 228
Cdd:COG0444 234 PVEeLFENP 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-231 |
2.90e-53 |
|
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: 176.19 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR---NIGFV 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGLESLPKkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL----SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVT-HDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESR 231
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRG--IGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
3.02e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 176.37 E-value: 3.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRN-IG 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHLTVAENIAFGLESLPKkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKL----SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDeyHFTSIFVT-HDQEEALELSDQVVVMSQGQV 215
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKE--RGIGVLITdHNVRETLGICDRAYIISEGKV 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-214 |
5.20e-53 |
|
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: 174.74 E-value: 5.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFGLESLPKKqrpsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKK----EREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDeYHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-215 |
1.95e-52 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 174.87 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQlhVRDrNIGFVFQH 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--ARE-DTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLeslpkkqrpsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGL----------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-213 |
1.48e-51 |
|
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: 170.79 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 12 FGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRdrnIGFVFQHYALFRH--L 89
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRRSIDRDfpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:cd03235 86 SVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1430737237 170 KVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:cd03235 166 KTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-224 |
1.68e-51 |
|
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: 171.15 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG--FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG-DDVSQLHVRDRNIGFV 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAF--GLESLPKKqrpskqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLKGLPKS------EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 158 LLLDEPFGALDAKVRKDLrrWlRALHDEYHFTSI-FVTHDQEEALELSDQVVVMSQGQVEQVNSPTGL 224
Cdd:cd03263 155 LLLDEPTSGLDPASRRAI--W-DLILEVRKGRSIiLTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-214 |
3.86e-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: 167.81 E-value: 3.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 hyalfrhltvaeniafgleslpkkqrpskqeirqrvakllemiqlpelakrypaqLSGGQKQRVALARALATQPRILLLD 161
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-215 |
1.10e-50 |
|
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: 169.79 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFG-GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFG-LESLPKKQ---RPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA 152
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrLGYKPTWRsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-215 |
1.20e-50 |
|
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: 168.77 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFV 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGLeslpkkQRPSKQEIRQRVAKLLEMI-QLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGA------YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
2.11e-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: 166.84 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRnigfvfqhy 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 alfrhltvAENIAFgleslpkkqrpskqeirqrVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:cd03214 72 --------ARKIAY-------------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 164 FGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-215 |
4.07e-50 |
|
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: 167.85 E-value: 4.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFVF 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLESlpkkqRPSKQEIRQRVAKLLEMiqLPELAKRY--PA-QLSGGQKQRVALARALATQPRI 157
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYA-----RRDRAEVRADLERVYEL--FPRLKERRrqRAgTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-217 |
4.11e-50 |
|
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: 175.64 E-value: 4.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 10 KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSdSGRVLFGGDDVSQLHVRD-----RNIGFVFQH-Y 83
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALF--RHlTVAENIAFGLESLPKKqrPSKQEIRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:COG4172 373 GSLspRM-TVGQIIAEGLRVHGPG--LSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKvVEQ 507
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-215 |
6.85e-50 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 167.91 E-value: 6.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLR-------IIAGLESsdSGRVLFGGDD-----VSQLH 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDiydpdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 71 VRdRNIGFVFQHYALFRHlTVAENIAFGleslPKKQ-RPSKQEIRQRVAKLLEMIQLPE-----LaKRYPAQLSGGQKQR 144
Cdd:COG1117 90 LR-RRVGMVFQKPNPFPK-SIYDNVAYG----LRLHgIKSKSELDEIVEESLRKAALWDevkdrL-KKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 145 VALARALATQPRILLLDEPFGALD----AKVrKDLrrwLRALHDEYhfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpistAKI-EEL---ILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-229 |
1.19e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 168.37 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHY-ALFRHLTVAEN 94
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKD 174
Cdd:PRK13650 103 VAFGLEN----KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 175 LRRWLRALHDEYHFTSIFVTHDQEEaLELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-221 |
1.82e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 167.92 E-value: 1.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNI----GFVFQH--YALFRHlT 90
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQYpeYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLP--ELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK13637 101 IEKDIAFG----PINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 169 AKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-213 |
2.01e-49 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 166.80 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVrDRniGFVFQH 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ER--GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLE--SLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQlaGVEKMQR------LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-214 |
2.14e-49 |
|
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: 163.71 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGF--QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGF 78
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFrHLTVAENIafgleslpkkqrpskqeirqrvakllemiqlpelakrypaqLSGGQKQRVALARALATQPRIL 158
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDqEEALELSDQVVVMSQGQ 214
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGK--TVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-212 |
3.25e-49 |
|
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: 164.57 E-value: 3.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVR-DRNIGFV 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGLESLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD------REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRAlHDEYHFTSIFVTHDQEEAleLSDQVVVMSQ 212
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-215 |
4.67e-49 |
|
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: 164.81 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRV------LFGGDDVSQLHVR 72
Cdd:TIGR02982 2 ISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLkvlgqeLHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 dRNIGFVFQHYALFRHLTVAENIAFGLESLPKKqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA 152
Cdd:TIGR02982 82 -RRIGYIFQAHNLLGFLTARQNVQMALELQPNL---SYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQeEALELSDQVVVMSQGQV 215
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-215 |
7.28e-49 |
|
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: 163.58 E-value: 7.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQIN-KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQlHVRDRNIGFVFQH 82
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 --YALFRHlTVAENIAFGLESLPKKQrpskqeirQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELDAGN--------EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
1.06e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 171.35 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD---RNIGFV 79
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGLEsLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGRE-PRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-215 |
1.12e-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: 163.68 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL------HVRDRNIGFVFQHYALFRHL 89
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLssneraKLRNKKLGFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLesLPKKQrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:TIGR02211 99 TALENVAMPL--LIGKK--SVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1430737237 170 KVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELsDQVVVMSQGQV 215
Cdd:TIGR02211 175 NNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-224 |
2.55e-48 |
|
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: 162.92 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ--LHVRdRNIGFVF 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRepREVR-RRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAF--GLESLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:cd03265 80 QDLSVDDELTGWENLYIhaRLYGVPGAER------RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGL 224
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
2.63e-48 |
|
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: 162.92 E-value: 2.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ--LHVRdRNI 76
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEAR-RRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAF--GLESLpkkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaGLYGL------KGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-228 |
3.31e-48 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 165.68 E-value: 3.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 10 KHF---GGF--------QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD----- 73
Cdd:COG4608 15 KHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RNIGFVFQH-YA-LFRHLTVAENIAFGLE---SLPKKQRpskqeiRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVAL 147
Cdd:COG4608 95 RRMQMVFQDpYAsLNPRMTVGDIIAEPLRihgLASKAER------RERVAELLELVGLrPEHADRYPHEFSGGQRQRIGI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 148 ARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDqeeaL----ELSDQVVVMSQGQ-VEQVNSPT 222
Cdd:COG4608 169 ARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LsvvrHISDRVAVMYLGKiVEIAPRDE 244
|
....*.
gi 1430737237 223 gLYARP 228
Cdd:COG4608 245 -LYARP 249
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-227 |
4.43e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.12 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrHLT 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFGleslpkKQRPSKQEIRQ--RVAKLLEMI-QLPE-----LAKRyPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:COG1132 430 IRENIRYG------RPDATDEEVEEaaKAAQAHEFIeALPDgydtvVGER-GVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHdqeealELS-----DQVVVMSQGQVEQVNSPT------GLYAR 227
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGR--TTIVIAH------RLStirnaDRILVLDDGRIVEQGTHEellargGLYAR 570
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-215 |
6.92e-48 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 169.44 E-value: 6.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV---SQLHVRDRNIGFVFQHYA 84
Cdd:COG3845 11 ITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRDAIALGIGMVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 LFRHLTVAENIAFGLESLpKKQRPSKQEIRQRVAkllemiqlpELAKRYP---------AQLSGGQKQRVALARALATQP 155
Cdd:COG3845 91 LVPNLTVAENIVLGLEPT-KGGRLDRKAARARIR---------ELSERYGldvdpdakvEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
5.89e-47 |
|
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: 168.01 E-value: 5.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQIN-KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGF 78
Cdd:COG4988 336 SIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFrHLTVAENIAFGleslpkKQRPSKQEIRQ--RVAKLLEMI-QLPE-----LAKRyPAQLSGGQKQRVALARA 150
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLG------RPDASDEELEAalEAAGLDEFVaALPDgldtpLGEG-GRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 151 LATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDqEEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-221 |
8.71e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 160.54 E-value: 8.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHY-ALFRHLTVA 92
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIFQNPdNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:PRK13632 103 DDIAFGLEN----KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 173 KDLRRWLRALHDEYHFTSIFVTHDQEEALeLSDQVVVMSQGQVEQVNSP 221
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-215 |
2.73e-46 |
|
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: 157.69 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRN-IGFVF 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLppHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIqlpelaKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLKEML------GRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.42e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 159.42 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITID------QINKHFGGfQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGgDDVSQLHVRDR 74
Cdd:PRK13634 1 MDITFQkvehryQYKTPFER-RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG-ERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 75 N-------IGFVFQ--HYALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPE-LAKRYPAQLSGGQKQR 144
Cdd:PRK13634 79 KlkplrkkVGIVFQfpEHQLFEE-TVEKDICFG----PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 145 VALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGL 224
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
....*
gi 1430737237 225 YARPE 229
Cdd:PRK13634 234 FADPD 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-215 |
7.18e-46 |
|
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: 156.41 E-value: 7.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFGLESLPKKQRpskqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPR----EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-239 |
1.16e-45 |
|
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: 156.67 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDR-NIGF 78
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARlGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLESLPKkqrPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKD---LDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVT-HDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVfdFL 237
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERG--IGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV--YL 233
|
..
gi 1430737237 238 GH 239
Cdd:TIGR04406 234 GE 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-239 |
1.28e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.83 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MS-ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFG----------GDDVSQL 69
Cdd:PRK11264 1 MSaIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 70 HVRDRNIGFVFQHYALFRHLTVAENIAFGleSLPKKQRPsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALAR 149
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEG--PVIVKGEP-KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
250
....*....|....
gi 1430737237 230 S----RFVFDFLGH 239
Cdd:PRK11264 237 QprtrQFLEKFLLQ 250
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-320 |
3.53e-45 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 158.50 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 20 NVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD---DVSQ---LHVRDRNIGFVFQHYALFRHLTVAE 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGLeslpkkqrpsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRK 173
Cdd:PRK11144 96 NLRYGM----------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 174 DLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNVLSGLVKGQ--- 250
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILKVTVLEHhph 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 251 ----KLVQGDAWVSLPGIRQDQEAQLYLRPH--EVQLSRSPAAKAR----LPLRIEAISLIGSEVRIELAPEGwqsDEIW 320
Cdd:PRK11144 246 yamtALALGDQHLWVNKLDAPLGTALRIRIQasDVSLVLQPPQQSSirniLRAKVVEIYDDNGQVEVKLEVGG---KTLW 322
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-215 |
4.11e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 156.81 E-value: 4.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVrdRNIGFVFQ 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR--RRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAF-----GLeslpkkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:COG4152 79 ERGLYPKMKVGEQLVYlarlkGL---------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
6.75e-45 |
|
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: 153.90 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQ--ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIG 77
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHlTVAENIAFGleslpkkqRPSKQEirQRVAKLLEMIQLPELAKRYP-----------AQLSGGQKQRVA 146
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLG--------APLADD--ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 147 LARALATQPRILLLDEPFGALD----AKVRKDLRRWLRalhdeyHFTSIFVTHDQeEALELSDQVVVMSQGQV 215
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDmnseERLKERLRQLLG------DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-215 |
1.04e-44 |
|
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: 153.12 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGqLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN-IGFVFQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAF--GLESLPKKQrpskqeIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:cd03264 80 EFGVYPNFTVREFLDYiaWLKGIPSKE------VKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-237 |
1.28e-44 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 154.36 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS-------QLHVRDRN 75
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 --------IGFVFQHYALFRHLTVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAK-RYPAQLSGGQKQRVA 146
Cdd:PRK10619 86 qlrllrtrLTMVFQHFNLWSHMTVLENV---MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 147 LARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYA 226
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|.
gi 1430737237 227 RPESRFVFDFL 237
Cdd:PRK10619 242 NPQSPRLQQFL 252
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-215 |
1.32e-44 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 154.09 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVF 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGleSLPKKQ-RPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:COG4604 82 QENHINSRLTVRELVAFG--RFPYSKgRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-215 |
1.73e-44 |
|
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: 152.37 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENiafgLESLPKKQRPSKQEIRQrvakLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03268 81 PGFYPNLTAREN----LRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGI-TVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-218 |
4.99e-44 |
|
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: 151.55 E-value: 4.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQHYALFRHLTVAENIAFGLES 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 102 LPKKQRPSKQEIRQrvakLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRA 181
Cdd:TIGR01277 98 GLKLNAEQQEKVVD----AAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1430737237 182 LHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQV 218
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-215 |
5.81e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 152.04 E-value: 5.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQHYALFRHLTVAENIAFGLE- 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 101 --SLPKKQRPSKQEIRQRVAkllemiqLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRW 178
Cdd:PRK10771 99 glKLNAAQREKLHAIARQMG-------IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1430737237 179 LRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
5.88e-44 |
|
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: 149.50 E-value: 5.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARragIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FqhyalfrhltvaeniafgleslpkkqrpskqeirqrvakllemiqlpelakrypaQLSGGQKQRVALARALATQPRILL 159
Cdd:cd03216 81 Y-------------------------------------------------------QLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGV-AVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-230 |
6.24e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 152.98 E-value: 6.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQH-YALFRHLTVAE 93
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRK 173
Cdd:PRK13648 104 DVAFGLEN----HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 174 DLRRWLRALHDEYHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSPTGLYARPES 230
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-229 |
1.07e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 152.85 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG-------DDVSQLHVRDRNIGFVFQ--HYAL 85
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 86 FRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLP-ELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PRK13645 104 FQE-TIEKDIAFG----PVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 165 GALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-242 |
1.22e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 155.96 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL------HVRDRNI 76
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFGLE--SLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMElaGINAEER------REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVF 234
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
....*...
gi 1430737237 235 DFLGHVNV 242
Cdd:PRK10070 263 TFFRGVDI 270
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-215 |
1.71e-43 |
|
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: 151.01 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLE---SSDSGRVL---FGGDDVSQLHvrdRNI 76
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptYGNDVRLFgerRGGEDVWELR---KRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFV--FQHYALFRHLTVAENIAFGLES---LPkkQRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARAL 151
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVLSGFFDsigLY--REPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 152 ATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-229 |
1.43e-42 |
|
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: 155.61 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKT----TLLRIIAGLESSDSGRVLFGGDDVSQL------HVRDRNIGFVFQH 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLserelrRIRGNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 --YALFRHLTVAENIAfglESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKR---YPAQLSGGQKQRVALARALATQPRI 157
Cdd:COG4172 101 pmTSLNPLHTIGKQIA---EVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDqeeaL----ELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LgvvrRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-229 |
7.56e-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: 154.15 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlT 90
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFGleslpkKQRPSKQEIRQrvakLLEMIQLPELAKRYP-----------AQLSGGQKQRVALARALATQPRILL 159
Cdd:COG4987 425 LRENLRLA------RPDATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 160 LDEPFGALDA----KVRKDLRRWLRalhdeyHFTSIFVTHDqEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:COG4987 495 LDEPTEGLDAateqALLADLLEALA------GRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-221 |
4.99e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.54 E-value: 4.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHY-ALFRHLTVA 92
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQNPdNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:PRK13635 101 DDVAFGLEN----IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 173 KDLRRWLRALHDEYHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSP 221
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-215 |
6.38e-41 |
|
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: 152.71 E-value: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrHLTVAEN 94
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGleslpkKQRPSKQEIrQRVAKLlemIQLPELAKRYP-----------AQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:TIGR03375 559 IALG------APYADDEEI-LRAAEL---AGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 164 FGALD----AKVRKDLRRWLRalhdeyHFTSIFVTHDQeEALELSDQVVVMSQGQV 215
Cdd:TIGR03375 629 TSAMDnrseERFKDRLKRWLA------GKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-215 |
2.24e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 143.37 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGF 78
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLESLPKkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA------ 152
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGL----SRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-217 |
2.26e-40 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 143.41 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF--GGF-------QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD 73
Cdd:TIGR02769 3 LEVRDVTHTYrtGGLfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 -----RNIGFVFQ--HYALFRHLTVAENIAFGLESLpkkQRPSKQEIRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRV 145
Cdd:TIGR02769 83 rrafrRDVQLVFQdsPSAVNPRMTVRQIIGEPLRHL---TSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 146 ALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQiVEE 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-202 |
2.37e-40 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 141.22 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 12 FGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLfggddvsqlHVRDRNIGFVFQHYALFRHL-- 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|...
gi 1430737237 170 KVRKDLRRWLRALHDEyHFTSIFVTHDQEEALE 202
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
2.81e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 142.56 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRN-IGFVFQ 81
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLdeHEIARLgIGRKFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENiafgLE-SLPKKQRP-------SKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALAT 153
Cdd:COG4674 93 KPTVFEELTVFEN----LElALKGDRGVfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEyHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4674 169 DPKLLLLDEPVAGMTDAETERTAELLKSLAGK-H-SVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
9.63e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 141.76 E-value: 9.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFG-GF----QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRN 75
Cdd:COG1101 2 LELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 IGFVFQHYAL--FRHLTVAENIA--------FGLE-SLPKKQRpskQEIRQRVAKL---LEmiqlpelaKRYPAQ---LS 138
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRrGLTKKRR---ELFRELLATLglgLE--------NRLDTKvglLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 139 GGQKQRVALARALATQPRILLLDEPFGALD----AKVRKDLRRWLRalhdEYHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDpktaALVLELTEKIVE----ENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
.
gi 1430737237 215 V 215
Cdd:COG1101 227 I 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-215 |
2.43e-39 |
|
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: 138.95 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDrnIGFVFQH 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--IGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFgLESLpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03269 79 RGLYPKMKVIDQLVY-LAQL---KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-200 |
5.64e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 138.76 E-value: 5.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH------VR 72
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 DRNIGFVFQHYALFRHLTVAENIafgleSLPKKQR-PSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARAL 151
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENV-----ELPALLRgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 152 ATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEA 200
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-227 |
9.79e-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: 138.13 E-value: 9.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 9 NKHFG---GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS--QLHVRDRNIGFVFQHY 83
Cdd:cd03253 5 NVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFrHLTVAENIAFGleslpkkqRP--SKQEIRQ--RVAKLLEMIQlpELAKRYPAQ-------LSGGQKQRVALARALA 152
Cdd:cd03253 85 VLF-NDTIGYNIRYG--------RPdaTDEEVIEaaKAAQIHDKIM--RFPDGYDTIvgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDeyHFTSIFVTHDQEEALElSDQVVVMSQGQV------EQVNSPTGLYA 226
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIvergthEELLAKGGLYA 230
|
.
gi 1430737237 227 R 227
Cdd:cd03253 231 E 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-237 |
1.15e-38 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 139.13 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 20 NVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-----SQLHVRDRNIGFVFQHYALFRHLTVAEN 94
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGLEslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKD 174
Cdd:PRK11831 105 VAYPLR---EHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 175 LRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRfVFDFL 237
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFL 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
1.21e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.22 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGG-----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-- 73
Cdd:PRK13651 1 MQIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 ------------------------RNIGFVFQ--HYALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLP 127
Cdd:PRK13651 81 ekvleklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFG----PVSMGVSKEEAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 128 E-LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQ 206
Cdd:PRK13651 156 EsYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKR 234
|
....*....
gi 1430737237 207 VVVMSQGQV 215
Cdd:PRK13651 235 TIFFKDGKI 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-215 |
1.25e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 137.70 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINK-HFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNI 76
Cdd:PRK10908 2 IRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAFGLeslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPL----IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRwlraLHDEYH---FTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILR----LFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-235 |
1.41e-38 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 138.61 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGF 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLES-LPKKQRPSkQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPwLSLWGRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV------EQVNSPTGLyarpesR 231
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVmaqgtpEEVMTPGLL------R 232
|
....
gi 1430737237 232 FVFD 235
Cdd:PRK11231 233 TVFD 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-229 |
1.96e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.78 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL---ESSDSGRVLFGGDDVSQ---LHVRDRnIGFVFQHY-ALFRHL 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktvWDIREK-VGIVFQNPdNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLESlpkKQRPsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:PRK13640 101 TVGDDVAFGLEN---RAVP-RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 170 KVRKDLRRWLRALHDEYHFTSIFVTHDQEEAlELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-229 |
3.59e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 137.28 E-value: 3.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKH--FGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL-ESSDSGRV-----LFGGD----DVSQ 68
Cdd:PRK14267 1 MKFAIETVNLRvyYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlELNEEARVegevrLFGRNiyspDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 69 LHVRdRNIGFVFQHYALFRHLTVAENIAFGLESlpKKQRPSKQEIRQRVAKLLEMIQLPELAKR----YPAQLSGGQKQR 144
Cdd:PRK14267 81 IEVR-REVGMVFQYPNPFPHLTIYDNVAIGVKL--NGLVKSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 145 VALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGL 224
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
....*
gi 1430737237 225 YARPE 229
Cdd:PRK14267 236 FENPE 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-223 |
4.80e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 136.48 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL------HVRDRNIGFVFQHYALFRHLTV 91
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFGLesLPKKQRPskQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKV 171
Cdd:PRK11629 105 LENVAMPL--LIGKKKP--AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 172 RKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQvVVMSQGQVEQVNSPTG 223
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAELSLMG 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-231 |
5.91e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.13 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-----RNIGFVFQHY--ALFRH 88
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAfglESLPKKQRPSKQEIRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PRK10419 106 KTVREIIR---EPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 168 DAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV--EQVNSPTGLYARPESR 231
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSPAGR 248
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-229 |
5.92e-38 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 136.13 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrHLTVAE 93
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGLEslpkkqrPSKQEIRQRVAKLLE----MIQLPE----LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:cd03249 96 NIRYGKP-------DATDEEVEEAAKKANihdfIMSLPDgydtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 166 ALDAKVRKDLRRWL-RALHDeyhFTSIFVTHdqeealELS-----DQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:cd03249 169 ALDAESEKLVQEALdRAMKG---RTTIVIAH------RLStirnaDLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
6.34e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 137.24 E-value: 6.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQ 81
Cdd:PRK13652 6 TRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HY--ALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:PRK13652 86 NPddQIFSP-TVEQDIAFG----PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-227 |
1.01e-37 |
|
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: 135.44 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrHLTVAEN 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGleslpkKQRPSKQEIRQ--RVAKLLEMI-QLPE-----LAKRyPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:cd03251 96 IAYG------RPGATREEVEEaaRAANAHEFImELPEgydtvIGER-GVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 167 LDAKVRKDLRRWLRALHDeyHFTSIFVTHdQEEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:cd03251 169 LDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
2.20e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 135.24 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVF 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA-------T 153
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAP----HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
2.52e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 135.04 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL-----ESSDSGRVLFGGDDVSQLHVRD--RN 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 IGFVFQHYALFRHLTVAENIAFGleslPKKQR--PSKQEIRQRVAKLLEMIQLPELAKRY---PA-QLSGGQKQRVALAR 149
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG----LKLNRlvKSKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEyhFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-215 |
4.18e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 135.25 E-value: 4.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH---VRDRnIGFVFQHY--ALFRh 88
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwVRSK-VGLVFQDPddQVFS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK13647 95 STVWDDVAFG----PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1430737237 169 AKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-213 |
6.39e-37 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 133.96 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 12 FGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRnIGFV--FQHYALFR 87
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIAR-MGVVrtFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAF------------GLESLPKKQRpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQP 155
Cdd:PRK11300 94 EMTVIENLLVaqhqqlktglfsGLLKTPAFRR-AESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-215 |
8.22e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 134.19 E-value: 8.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD--DVSQLHVRDRNIGFVFQH--YALFRHLT 90
Cdd:COG4167 26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKYRCKHIRMIFQDpnTSLNPRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFGLE---SLPKKQRpskqeiRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:COG4167 106 IGQILEEPLRlntDLTAEER------EERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 167 LDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4167 180 LDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-215 |
9.94e-37 |
|
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: 131.52 E-value: 9.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESS--DSGRVLFGGDDVSQLHVRDRnIGFVFQHYALFRHLT 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFgleslpkkqrpskqeirqrVAKLlemiqlpelakrypAQLSGGQKQRVALARALATQPRILLLDEPFGALDAK 170
Cdd:cd03213 99 VRETLMF-------------------AAKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1430737237 171 VRKDLRRWLRALHDEyHFTSIFVTHD-QEEALELSDQVVVMSQGQV 215
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-215 |
2.10e-36 |
|
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: 130.03 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAENI 95
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 afgleslpkkqrpskqeirqrvakllemiqlpelakrypaqLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDL 175
Cdd:cd03246 97 -----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1430737237 176 RRWLRALhDEYHFTSIFVTHdQEEALELSDQVVVMSQGQV 215
Cdd:cd03246 136 NQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-221 |
3.05e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.90 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL-HVRD--RNIGFVFQH-----YALFrh 88
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDirNKAGMVFQNpdnqiVATI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 ltVAENIAFGLESLPKKQrpskQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK13633 103 --VEEDVAFGPENLGIPP----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 169 AKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSP 221
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-229 |
1.21e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 131.37 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHY-ALFRHLTVAEN 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGLESlpkkQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKD 174
Cdd:PRK13642 103 VAFGMEN----QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 175 LRRWLRALHDEYHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-227 |
4.83e-35 |
|
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: 134.54 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLES--SDSGRVLF------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 62 -----------------GGDDVSQLHVRDRnIGFVFQH-YALFRHLTVAENIafgLESLPKKQRPSKQEIrQRVAKLLEM 123
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKR-IAIMLQRtFALYGDDTVLDNV---LEALEEIGYEGKEAV-GRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 124 IQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALEL 203
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|....
gi 1430737237 204 SDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-217 |
5.74e-35 |
|
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: 134.88 E-value: 5.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAENI 95
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 A-FGleslpkkqRPSKQEIRQ--RVAKLLEMIQlpELAKRY-------PAQLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:COG4618 427 ArFG--------DADPEKVVAaaKLAGVHEMIL--RLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQeEALELSDQVVVMSQGQVEQ 217
Cdd:COG4618 497 NLDDEGEAALAAAIRALKARGA-TVVVITHRP-SLLAAVDKLLVLRDGRVQA 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
1.29e-34 |
|
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: 133.39 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-----GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFG-GD---DVSQLHVRD 73
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 RN-----IGFVFQHYALFRHLTVAENI--AFGLEsLPKKQRPSKQEIRQRVAKLLEMiQLPELAKRYPAQLSGGQKQRVA 146
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGLE-LPDELARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 147 LARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-215 |
1.55e-34 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 134.47 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH------VRDRNIGFVFQHYALFRHLTV 91
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaqLRREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFG--LESLPKKQRpskqeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:PRK10535 104 AQNVEVPavYAGLERKQR------LLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1430737237 170 KVRKDLRRWLRALHDEYHfTSIFVTHDQEEALElSDQVVVMSQGQV 215
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-234 |
1.66e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 127.32 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS--QLHVRD-RNIGF 78
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARArRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGLESlpkKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQI---RDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDeYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVF 234
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-229 |
1.22e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG-----DDVSQLHVRdRNIGFVFQHY--ALF 86
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikyDKKSLLEVR-KTVGIVFQNPddQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 87 RHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:PRK13639 93 AP-TVEEDVAFG----PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 167 LDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
2.15e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 125.35 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFG-GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD--DVSQ---LHVRdRNI 76
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRkglMKLR-ESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQH--YALFRhLTVAENIAFGLESLpkkQRPsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNL---KLP-EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-227 |
3.28e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 129.44 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTT----LLRIIAGlessdSGRVLFGGDDVSQLHVRD-----RNIGFVFQ--HYA 84
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 LFRHLTVAENIAFGLESLPKKQRPSKQEirQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 164 FGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV-EQ------VNSPTGLYAR 227
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVvEQgdcervFAAPQQEYTR 523
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-215 |
3.28e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 124.35 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDS---GRVLFGGDDVSQLHVRDRNI--- 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARDIrks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 ----GFVFQHYALFRHLTVAENIAFG-LESLPKKQ---RPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALA 148
Cdd:PRK09984 85 rantGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 149 RALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
3.41e-33 |
|
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: 129.33 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGG-FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRNIGF 78
Cdd:TIGR02857 321 SLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdaDSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHlTVAENIAFGleslpkkqRP--SKQEIRQ--RVAKLLEMIQ-LPE----LAKRYPAQLSGGQKQRVALAR 149
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLA--------RPdaSDAEIREalERAGLDEFVAaLPQgldtPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDqEEALELSDQVVVM 210
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-237 |
5.92e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.35 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL-----ESSDSGRVLFGGDDV-----SQLHVR 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprtDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 dRNIGFVFQHYALFRhLTVAENIAFGLESLPKKQrpsKQEIRQRVAKLLEMIQL-PELAKRYPAQ---LSGGQKQRVALA 148
Cdd:PRK14239 86 -KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKD---KQVLDEAVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 149 RALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
....*....
gi 1430737237 229 ESRFVFDFL 237
Cdd:PRK14239 239 KHKETEDYI 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-228 |
6.49e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 125.20 E-value: 6.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-----SQLHVRDRNIGFVFQH--YALFRH 88
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAFGLESL-PKKqrpSKQEIRQRV-AKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:PRK15079 115 MTIGEIIAEPLRTYhPKL---SRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 167 LDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-232 |
7.48e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 123.23 E-value: 7.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL-ESSDS-----GRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHL 89
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLESLPKKQrpsKQEIRQRVAKLLEMIQL-PELAKRY--PA-QLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKE---KREIKKIVEECLRKVGLwKEVYDRLnsPAsQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEyhFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRF 232
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-214 |
8.27e-33 |
|
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: 122.16 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF-----GG--FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLF----GGDDVSQ--- 68
Cdd:COG4778 5 LEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 69 ---LHVRDRNIGFVFQhyalfrHLTV-----AENIAfgLESLpKKQRPSKQEIRQRVAKLLEMIQLPE-LAKRYPAQLSG 139
Cdd:COG4778 85 reiLALRRRTIGYVSQ------FLRViprvsALDVV--AEPL-LERGVDREEARARARELLARLNLPErLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 140 GQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIF-VTHDQEEALELSDQVVVMSQGQ 214
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARG--TAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-228 |
9.48e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 124.69 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-----SQLHVRDRNIGFVFQH-YAlfrHL 89
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpEAQKLLRQKIQIVFQNpYG---SL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLE-------SLPKKQRpskqeiRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:PRK11308 106 NPRKKVGQILEepllintSLSAAER------REKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-215 |
1.17e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 122.06 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-RNIGFVF-QHYALFRHLTVAEn 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 iafGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKD 174
Cdd:cd03267 115 ---SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1430737237 175 LRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-215 |
1.44e-32 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.74 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQlhvRD-RNIGFVFQHY 83
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDlHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFRHLTVAEN--IAFGLESLPKkqrpskqeirQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:TIGR03740 80 PLYENLTARENlkVHTTLLGLPD----------SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-227 |
1.48e-32 |
|
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: 128.30 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTV 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFGleslpkkqRPsKQEIRQRVAKLLEMIQLPELAKRYP-----------AQLSGGQKQRVALARALATQPRILLL 160
Cdd:TIGR02203 423 ANNIAYG--------RT-EQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHdQEEALELSDQVVVMSQGQV------EQVNSPTGLYAR 227
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQGR--TTLVIAH-RLSTIEKADRIVVMDDGRIvergthNELLARNGLYAQ 563
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-221 |
2.98e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 122.16 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQIN------KHFGGfQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-SQLHVRD 73
Cdd:PRK13649 1 MGINLQNVSytyqagTPFEG-RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 -----RNIGFVFQ--HYALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPE-LAKRYPAQLSGGQKQRV 145
Cdd:PRK13649 80 ikqirKKVGLVFQfpESQLFEE-TVLKDVAFG----PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 146 ALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHdEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-169 |
4.19e-32 |
|
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: 120.45 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD---SGRVLFGGDDVSQLHVRDRnIGFVFQHYALFRHLTVA 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 93 ENIAFGLESlpKKQRPSKQEIRQRVAKLLEMIQLP--ELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:cd03234 100 ETLTYTAIL--RLPRKSSDAIRKKRVEDVLLRDLAltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-215 |
4.61e-32 |
|
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: 119.07 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFV---FQHYALFRHLT 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFgleslpkkqrpskqeirqrvakllemiqlpelakryPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAK 170
Cdd:cd03215 95 VAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1430737237 171 VRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03215 139 AKAEIYRLIRELADAGK-AVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-227 |
4.68e-32 |
|
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: 126.86 E-value: 4.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDD---VSQLHVRdRNIGFVFQHYALFRHlTVA 92
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLR-AAIGIVPQDTVLFND-TIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAFGleslpkkqRP--SKQEIRQ--RVAKLLEMI-QLPElakRYPAQ-------LSGGQKQRVALARALATQPRILLL 160
Cdd:COG5265 450 YNIAYG--------RPdaSEEEVEAaaRAAQIHDFIeSLPD---GYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALhdEYHFTSIFVTHdqeealELS-----DQVVVMSQGQ-VEQVNSPT-----GLYAR 227
Cdd:COG5265 519 DEATSALDSRTERAIQAALREV--ARGRTTLVIAH------RLStivdaDEILVLEAGRiVERGTHAEllaqgGLYAQ 588
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-229 |
7.58e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.47 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS------QLHVRDRNIGFVFQ--HYALFR 87
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPE-LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:PRK13641 101 N-TVLKDVEFG----PKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 167 LDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-230 |
9.15e-32 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 119.78 E-value: 9.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 20 NVSLDIPEGQLTALLGPSGSGKTT----LLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH--YALFRHLTVAE 93
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIafgLESLPKKQRPSKQEiRQRVAKLLEMIQLP---ELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAK 170
Cdd:TIGR02770 84 HA---IETLRSLGKLSKQA-RALILEALEAVGLPdpeEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 171 VRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPES 230
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-313 |
1.04e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 123.41 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGF 78
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHLTVAENIAFGleSLPKKQR--PSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMG--RTPHRSRfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 157 ILLLDEPFGALDakVRKDLR--RWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVF 234
Cdd:PRK09536 160 VLLLDEPTASLD--INHQVRtlELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 235 DflGHVNVLSGLVKGQKLVqgdawVSLPGIRQDQEAQLyLRPHEVQlSRSPAAKARLPLrIEAisliGSEVRIELAPEG 313
Cdd:PRK09536 237 D--ARTAVGTDPATGAPTV-----TPLPDPDRTEAAAD-TRVHVVG-GGQPAARAVSRL-VAA----GASVSVGPVPEG 301
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-196 |
1.16e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.18 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDdvsqlhVRdrnIGFVFQHYA 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------LR---IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 LFRHLTVAENIAFGLESLPKKQR---------------PSKQ-------------EIRQRVAKLLEMIQLP-ELAKRYPA 135
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAeleeleaklaepdedLERLaelqeefealggwEAEARAEEILSGLGFPeEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 136 QLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRalhdEYHFTSIFVTHD 196
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK----NYPGTVLVVSHD 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-205 |
1.21e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 120.27 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLR-------IIAGLESsdSGRVLFGGD-----DVSQLHVRdRN 75
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKnlyapDVDPVEVR-RR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 IGFVFQHYALFRHlTVAENIAFGleslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQ----LSGGQKQRVALARAL 151
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYG-----ARINGYKGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 152 ATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDQEEALELSD 205
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-233 |
1.65e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.09 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG---DDVSQLHVRDRNIGFVFQH-YALFRHL 89
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAFGLESL--PkkqrPSkqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PRK13644 94 TVEEDLAFGPENLclP----PI--EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 168 DAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEaLELSDQVVVMSQGQVEQVNSPTGLYARPESRFV 233
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-196 |
1.75e-31 |
|
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: 124.78 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 11 HFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrH 88
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAFGleslpkkqRPSKQEirQRVAKLLEMIQLPELAKRYP-----------AQLSGGQKQRVALARALATQPRI 157
Cdd:TIGR02868 423 TTVRENLRLA--------RPDATD--EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHD 196
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-214 |
1.83e-31 |
|
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: 117.96 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGddvsqlhvrdrNIGFVFQhYALFRHLTVAENIA 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQ-EPWIQNGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 97 FGLESLPkkqrpskqeirQRVAKLLEMIQL-PELaKRYPAQ-----------LSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:cd03250 88 FGKPFDE-----------ERYEKVIKACALePDL-EILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 165 GALDAKVRKDL-RRWLR-ALHDeyHFTSIFVTHdQEEALELSDQVVVMSQGQ 214
Cdd:cd03250 156 SAVDAHVGRHIfENCILgLLLN--NKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-216 |
7.47e-31 |
|
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: 116.86 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLhvrDRNIGFVfqhyalfRHLTVA 92
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---GLGGGFN-------PELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAF-----GLeslpkkqrpSKQEIRQRVAkllEMIQLPELAKRYPAQL---SGGQKQRVALARALATQPRILLLDEPF 164
Cdd:cd03220 103 ENIYLngrllGL---------SRKEIDEKID---EIIEFSELGDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 165 GALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVE 216
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-211 |
8.56e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.74 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQA-----LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRNIGFVFQHYALF 86
Cdd:PRK10247 14 GYLAgdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 87 RHlTVAENIAFGLESlpKKQRPSkqeiRQRVAKLLEMIQLPE--LAKRYpAQLSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PRK10247 94 GD-TVYDNLIFPWQI--RNQQPD----PAIFLDDLERFALPDtiLTKNI-AELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1430737237 165 GALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEaLELSDQVVVMS 211
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQ 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-229 |
1.26e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 118.80 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRV----LFGGDDVSQLHVRD--------------RNI 76
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITnpyskkiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQ--HYALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLPE-LAKRYPAQLSGGQKQRVALARALAT 153
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-215 |
1.53e-30 |
|
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: 117.24 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLF-----GGDDVSQLHVRDRNI- 76
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 -----GFVFQHYA--LFRHLTVAENIAFGLESLPKKQRpskQEIRQRVAKLLEMIQLPelAKRY---PAQLSGGQKQRVA 146
Cdd:TIGR02323 84 mrtewGFVHQNPRdgLRMRVSAGANIGERLMAIGARHY---GNIRATAQDWLEEVEID--PTRIddlPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 147 LARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-221 |
2.26e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 116.33 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 10 KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLhvrdrNIGFVFQHyalfrHL 89
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFHP-----EL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIAF-----GLeslpkkqrpSKQEIRQRV------AKLLEMIQLPelAKRYpaqlSGGQKQRVALARALATQPRIL 158
Cdd:COG1134 104 TGRENIYLngrllGL---------SRKEIDEKFdeivefAELGDFIDQP--VKTY----SSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:COG1134 169 LVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-226 |
5.14e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.42 E-value: 5.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGG-----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG-------DDVSQ 68
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 69 LHVRDRnIGFVFQ--HYALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLP-ELAKRYPAQLSGGQKQRV 145
Cdd:PRK13646 81 RPVRKR-IGMVFQfpESQLFED-TVEREIIFG----PKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 146 ALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLY 225
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
.
gi 1430737237 226 A 226
Cdd:PRK13646 235 K 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-215 |
8.91e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.02 E-value: 8.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 4 TIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD-----DVSQLHVRDRNI-- 76
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 ----GFVFQHYA--LFRHLTVAENIAFGLESLPKKQRpskQEIRQRVAKLLEMIQLPelAKR---YPAQLSGGQKQRVAL 147
Cdd:PRK11701 88 rtewGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHY---GDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 148 ARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-227 |
1.50e-29 |
|
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: 114.12 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDD---VSQLHVRdRNIGFVFQHYALFRHlTVAE 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalADPAWLR-RQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGLESLPKKqrpsKQEIRQRVAKLLEMI-QLPE----LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:cd03252 95 NIALADPGMSME----RVIEAAKLAGAHDFIsELPEgydtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 169 AKVRKDLRRWLRALHDEYhfTSIFVTHdQEEALELSDQVVVMSQGQV------EQVNSPTGLYAR 227
Cdd:cd03252 171 YESEHAIMRNMHDICAGR--TVIIIAH-RLSTVKNADRIIVMEKGRIveqgshDELLAENGLYAY 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-215 |
1.95e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 113.82 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH---VRDRNIGFV 79
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtakIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGleslpkKQRPSKQEIRQRVAKLLEMiqLPELAKR---YPAQLSGGQKQRVALARALATQPR 156
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYEL--FPRLHERriqRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
7-225 |
2.05e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 114.83 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 7 QINKHFGGfQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS------QLHVRDRNIGFVF 80
Cdd:PRK13643 12 QPNSPFAS-RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 Q--HYALFRHlTVAENIAFGleslPKKQRPSKQEIRQRVAKLLEMIQLP-ELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:PRK13643 91 QfpESQLFEE-TVLKDVAFG----PQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLY 225
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-242 |
4.16e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.42 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-----SQLHVRDRNIGFVFQ--HYALFRHL 89
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 TVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK10261 419 TVGDSI---MEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 169 AKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRFVFDFLGHVNV 242
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-215 |
6.70e-29 |
|
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: 111.93 E-value: 6.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 9 NKHFG---GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRNIGFVFQHY 83
Cdd:cd03254 7 NVNFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFRHlTVAENIAFGLESlpkkqrpSKQEIRQRVAKLLEMIQLPE-LAKRYPAQ-------LSGGQKQRVALARALATQP 155
Cdd:cd03254 87 FLFSG-TIMENIRLGRPN-------ATDEEVIEAAKEAGAHDFIMkLPNGYDTVlgenggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHdQEEALELSDQVVVMSQGQV 215
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAH-RLSTIKNADKILVLDDGKI 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-215 |
8.41e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 114.03 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD-RNIGFVF-QHYALFRHLTVAE 93
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFaRRIGVVFgQRSQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NiafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRyPA-QLSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:COG4586 116 S----FRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1430737237 173 KDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-214 |
8.46e-29 |
|
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: 116.85 E-value: 8.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL--ESSDSGRVLFGGDDVSQLHVRD---RNIG 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDterAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHLTVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPEL-AKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHdEYHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-214 |
9.41e-29 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 116.57 E-value: 9.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL--ESSDSGRVLFGGDDVSQLHVRD---RNIGFVFQH 82
Cdd:PRK13549 11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDterAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLESLPKKqRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK13549 91 LALVKELSVLENIFLGNEITPGG-IMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 163 PFGALDAK---VRKDLRRWLRAlHDeyhFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PRK13549 170 PTASLTESetaVLLDIIRDLKA-HG---IACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-214 |
1.00e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.36 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRnIGFVF 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRarHARQR-VGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIA-----FGLeslpkkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQP 155
Cdd:PRK13537 87 QFDNLDPDFTVRENLLvfgryFGL---------SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-214 |
1.03e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 116.55 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 6 DQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD---RNIGFVFQH 82
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGleSLPKK-----QRPSKQEIRQRVAKLLEMIQlPELAKRYpaqLSGGQKQRVALARALATQPRI 157
Cdd:PRK11288 88 LHLVPEMTVAENLYLG--QLPHKggivnRRLLNYEAREQLEHLGVDID-PDTPLKY---LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHFTsIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-228 |
1.13e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.52 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRNIGFVFQHYALFRHlTVAE 93
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhHYLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGLESLPKkqrpskQEIRQRVAKLLEMIQLPELAKRYP-------AQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:TIGR00958 574 NIAYGLTDTPD------EEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 167 LDAKVRKDLRRWLRAlhdeYHFTSIFVTHdQEEALELSDQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:TIGR00958 648 LDAECEQLLQESRSR----ASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-169 |
2.37e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 109.96 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRnigfvfQHY-----ALFR 87
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA------CHYlghrnAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAFGLESLpkKQRPSkqeirqRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PRK13539 87 ALTVAENLEFWAAFL--GGEEL------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
..
gi 1430737237 168 DA 169
Cdd:PRK13539 159 DA 160
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-215 |
2.37e-28 |
|
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: 115.91 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAENI 95
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 A-FGleslpkkQRPSKQEIRQ--RVAKLLEMIQ-LP-----ELAKRyPAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:TIGR01842 413 ArFG-------ENADPEKIIEaaKLAGVHELILrLPdgydtVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 167 LDAKVRKDLRRWLRALHDEyHFTSIFVTHdQEEALELSDQVVVMSQGQV 215
Cdd:TIGR01842 485 LDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRI 531
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-213 |
2.47e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.00 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-SQLHVRDRNIGFV 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAEN-IAFGleslpKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:PRK13536 120 PQFDNLDLEFTVRENlLVFG-----RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-228 |
7.82e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 111.37 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGG----FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSdSGRVL-----FGGDDVSQLHVRD 73
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMaekleFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 74 R------NIGFVFQH--YALFRHLTVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKR---YPAQLSGGQK 142
Cdd:PRK11022 83 RrnlvgaEVAMIFQDpmTSLNPCYTVGFQI---MEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 143 QRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPT 222
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
....*.
gi 1430737237 223 GLYARP 228
Cdd:PRK11022 240 DIFRAP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-215 |
8.28e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 10 KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD---RNIGFV---FQHY 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFRHLTVAENIAFG-LESLPKKQRPSKQEIRQRVAKLLEmiqlpELAKRYP------AQLSGGQKQRVALARALATQPR 156
Cdd:COG1129 340 GLVLDLSIRENITLAsLDRLSRGGLLDRRRERALAEEYIK-----RLRIKTPspeqpvGNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAEGK-AVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-240 |
1.04e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.19 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 12 FGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESS-----DSGRVLFGGDDVsqLHVRD-----RNIGFVFQ 81
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSI--FNYRDvlefrRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRhLTVAENIAFGLES---LPKKQRPSKQEIRQRVAKLLEMIQlpELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:PRK14271 109 RPNPFP-MSIMDNVLAGVRAhklVPRKEFRGVAQARLTEVGLWDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEyhFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE----SRFVF 234
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKhaetARYVA 263
|
....*.
gi 1430737237 235 DFLGHV 240
Cdd:PRK14271 264 GLSGDV 269
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-215 |
1.43e-27 |
|
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: 108.33 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ-----LHvrdRNIGFVFQHYALFRHlT 90
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLH---SKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFGLESLPKkqrpskQEIRQRVAKLLEMIQLPELAKRYP-------AQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:cd03248 104 LQDNIAYGLQSCSF------ECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 164 FGALDAKVRKDLRrwlRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:cd03248 178 TSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-305 |
2.08e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 113.41 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHF----GGFQALKNVSLDIPEGQLTALLGPSGSGKT----TLLRII--AGLESSDSGRVL---------FGG 63
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrrrsrqvieLSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 64 DDVSQL-HVRDRNIGFVFQH--YALFRHLTVAENIAfglESLPKKQRPSKQEIRQRVAKLLEMIQLPE---LAKRYPAQL 137
Cdd:PRK10261 93 QSAAQMrHVRGADMAMIFQEpmTSLNPVFTVGEQIA---ESIRLHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 138 SGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQ 217
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 218 VNSPTGLYARPESRFVFDFLGHVNVLsGLVKGQKLVQGDAWVSL--PGIRQDQEAQLYLRPHEVQLsRSPAAKARLPLRI 295
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTRALLAAVPQL-GAMKGLDYPRRFPLISLehPAKQEPPIEQDTVVDGEPIL-QVRNLVTRFPLRS 327
|
330
....*....|
gi 1430737237 296 EAISLIGSEV 305
Cdd:PRK10261 328 GLLNRVTREV 337
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
4.91e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 4.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGgddvsqLHVRdrnIGFVFQH 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------ETVK---IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFR-HLTVAENIAfglESLPKKQRpskQEIRQRVAKLL---EMIQlpelakRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:COG0488 387 QEELDpDKTVLDELR---DGAPGGTE---QEVRGYLGRFLfsgDDAF------KPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 159 LLDEPFGALDAkvrkDLRRWL-RALhDEYHFTSIFVTHDqEEALE-LSDQVVVMSQGQVE 216
Cdd:COG0488 455 LLDEPTNHLDI----ETLEALeEAL-DDFPGTVLLVSHD-RYFLDrVATRILEFEDGGVR 508
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-221 |
6.43e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 107.76 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 6 DQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHY 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFRHLTVAENIAFG-LESLPKKQRPSKQEiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK10253 91 TTPGDITVQELVARGrYPHQPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
13-228 |
7.09e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 111.97 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlT 90
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLGVVLQNGRLMSG-S 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFGleslpkkqRPSKQEIRQRVAKlleMIQLPELAKRYP-----------AQLSGGQKQRVALARALATQPRILL 159
Cdd:TIGR03797 543 IFENIAGG--------APLTLDEAWEAAR---MAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 160 LDEPFGALD----AKVRKDLRRwLRAlhdeyhfTSIFVTHdqeealELS-----DQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:TIGR03797 612 FDEATSALDnrtqAIVSESLER-LKV-------TRIVIAH------RLStirnaDRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-270 |
1.15e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.91 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 7 QINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL---HVRDRNIGFVFQHY 83
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpaKAHQLGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 ALFRHLTVAENIAFGlesLPKKQRPSKQeIRQRVAKLLEMIQLPELAkrypAQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:PRK15439 96 LLFPNLSVKENILFG---LPKRQASMQK-MKQLLAALGCQLDLDSSA----GSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 164 FGALDAKVRKDLRRWLRALHDEYHFTsIFVTHDQEEALELSDQVVVMSQGQVeQVNSPTGLYARPEsrfVFDFLGHVNVL 243
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGI-VFISHKLPEIRQLADRISVMRDGTI-ALSGKTADLSTDD---IIQAITPAARE 242
|
250 260
....*....|....*....|....*..
gi 1430737237 244 SGLVKGQKLvqgdaWVSLPGIRQDQEA 270
Cdd:PRK15439 243 KSLSASQKL-----WLELPGNRRQQAA 264
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-217 |
1.21e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.09 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSdSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrHLTV 91
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFGleslpkKQRPSKQEIRQRV--AKLLEMIQLPELAKRYP-----AQLSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PRK11174 440 RDNVLLG------NPDASDEQLQQALenAWVSEFLPLLPQGLDTPigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 165 GALDAKVRkdlRRWLRALHDEY-HFTSIFVTHdQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:PRK11174 514 ASLDAHSE---QLVMQALNAASrRQTTLMVTH-QLEDLAQWDQIWVMQDGQiVQQ 564
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-170 |
1.83e-26 |
|
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: 104.36 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL-HVRDRNIGFVFQHYALFRHLTV 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 92 AENIAFGLESLPKKQRpskqeirqRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAK 170
Cdd:TIGR01189 91 LENLHFWAAIHGGAQR--------TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-215 |
4.32e-26 |
|
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: 109.83 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFG-GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRNIGF 78
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 79 VFQHYALFRHlTVAENIAFGleslpKKQRPSKQEIRQ--RVAKLLEMI-QLP-----ELAKRyPAQLSGGQKQRVALARA 150
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLG-----AKENVSQDEIWAacEIAEIKDDIeNMPlgyqtELSEE-GSSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 151 LATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEyhfTSIFVTHDQEEAlELSDQVVVMSQGQV 215
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKI 686
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-216 |
5.77e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.39 E-value: 5.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN-IGFVFQHYALFrHLTVAEN 94
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQRPYLF-DTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAfgleslpkkqrpskqeirqrvakllemiqlpelakrypAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKV-RK 173
Cdd:cd03247 95 LG--------------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1430737237 174 DLRRWLRALHDEyhfTSIFVTHdQEEALELSDQVVVMSQGQVE 216
Cdd:cd03247 137 LLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-227 |
6.96e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 109.06 E-value: 6.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLH---VRdRNIGFVFQHYALFRHlTVAEN 94
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADpawLR-RQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGleslpkKQRPSKQEIRQ--RVAKLLEMIQlpELAKRYPAQ-------LSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:TIGR01846 551 IALC------NPGAPFEHVIHaaKLAGAHDFIS--ELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEYhfTSIFVTHdQEEALELSDQVVVMSQGQV------EQVNSPTGLYAR 227
Cdd:TIGR01846 623 ALDYESEALIMRNMREICRGR--TVIIIAH-RLSTVRACDRIIVLEKGQIaesgrhEELLALQGLYAR 687
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-198 |
7.28e-26 |
|
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: 100.99 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVlfggddvsqlhvrdrnigfvfqh 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 yalfrhltvaeniafgleslpkkQRPSKQEIRqrvakllemiqlpelakrYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03221 58 -----------------------TWGSTVKIG------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|....*.
gi 1430737237 163 PFGALDAKVRKDLRRWLRalhdEYHFTSIFVTHDQE 198
Cdd:cd03221 97 PTNHLDLESIEALEEALK----EYPGTVILVSHDRY 128
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-228 |
7.48e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.87 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS--QLHVRDRNIGFVFQHYAlfrhltvae 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDPS--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 niafglESLPKKQRPSK--------------QEIRQRVAKLLEMIQL-PELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:PRK15112 98 ------TSLNPRQRISQildfplrlntdlepEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARP 228
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-215 |
1.41e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.42 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR---NIGFV---FQHYALF 86
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 87 RHLTVAENIAFGLESLPKKQRP---SKQEIRQRVAKLLEM--IQLPELakRYPA-QLSGGQKQRVALARALATQPRILLL 160
Cdd:COG3845 349 PDMSVAENLILGRYRRPPFSRGgflDRKAIRAFAEELIEEfdVRTPGP--DTPArSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-225 |
1.62e-25 |
|
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: 108.56 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV-SQLHVRDRNIGFVFQHYALFRHLTVA 92
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAFglesLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:TIGR01257 1022 EHILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 173 KDLrrWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP--------TGLY 225
Cdd:TIGR01257 1098 RSI--WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPlflkncfgTGFY 1156
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-213 |
2.60e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.79 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR---NIGFV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYALFRHLTVAENIAFGleSLPKKQ-----RPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG--RHLTKKvcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-239 |
3.23e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.06 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD---SGRVLFGGD--DVSQLHVRDrniGFVFQHYALFRHLTVA 92
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpiDAKEMRAIS---AYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAFGLEsLPKKQRPSKQEIRQRVAKLLEM----------IQLPELAKrypaQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:TIGR00955 118 EHLMFQAH-LRMPRRVTKKEKRERVDEVLQAlglrkcantrIGVPGRVK----GLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYhfTSIFVTHDQ--EEALELSDQVVVMSQGQVEQVNSPTglyarpESRFVFDFLGH 239
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKG--KTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPD------QAVPFFSDLGH 263
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-214 |
9.33e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 105.09 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFVFQ 81
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLD 161
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 162 EPFGALDAKVRKDLRRWLRALHDEYHFTsIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKSQGRGI-VYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-229 |
2.25e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.40 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKT-TLLRIIAGLESSD----SGRVLFGGDDVsqLH--------VRDRNIGFVFQH 82
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL--LHaseqtlrgVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YAL-FRHLTVAENIAFGLESLPKKQRpsKQEIRQRVAKLLEMIQLPELAKR---YPAQLSGGQKQRVALARALATQPRIL 158
Cdd:PRK15134 101 PMVsLNPLHTLEKQLYEVLSLHRGMR--REAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-215 |
7.41e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.60 E-value: 7.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLES--SDSGRVLFGGDDVSQLHVRDR---NIGFVFQHYALFRHLTVA 92
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAFGLESLPKKqRPSKQEIRQRVAKLLEMIQL-PELAKRYPAQ-LSGGQKQRVALARALATQPRILLLDEPFGALDAK 170
Cdd:COG0396 96 NFLRTALNARRGE-ELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDID 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1430737237 171 VRKDLRRWLRALHDEyHFTSIFVTHdQEEALEL--SDQVVVMSQGQV 215
Cdd:COG0396 175 ALRIVAEGVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRI 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
1.09e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDS-----GRVLFGGDDVSQLHVR---- 72
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 DRNIGFVFQHYALFRhLTVAENIAFGLESLpkKQRPsKQEIRQRVAKLLEMIQLPELAK----RYPAQLSGGQKQRVALA 148
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIV--GWRP-KLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 149 RALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSD 205
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-215 |
2.24e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 101.63 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAEN 94
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFgleslPKKQRPSKQEIRQ--RVAKLLEMIQ-----LPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PRK11176 437 IAY-----ARTEQYSREQIEEaaRMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1430737237 168 DAKVRKDLRRWLRALHDEYhfTSIFVTHdQEEALELSDQVVVMSQGQV 215
Cdd:PRK11176 512 DTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEI 556
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-195 |
2.64e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 20 NVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLhvRD---RNIGFVFQHYALFRHLTVAENIA 96
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ--RDeyhQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 97 FgleSLPKKQRPSKQEIRQRVAKLlemiqlpELAKR--YPA-QLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRK 173
Cdd:PRK13538 97 F---YQRLHGPGDDEALWEALAQV-------GLAGFedVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|..
gi 1430737237 174 DLRRWLRAlHDEYHFTSIFVTH 195
Cdd:PRK13538 167 RLEALLAQ-HAEQGGMVILTTH 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
4.84e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 100.67 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQInkHFG----GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RN 75
Cdd:PRK11160 338 SLTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 76 IGFVFQHYALFRHlTVAENIAFGlesLPKKQRPSKQEIRQRV--AKLLEMIQ-----LPELAKrypaQLSGGQKQRVALA 148
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA---APNASDEALIEVLQQVglEKLLEDDKglnawLGEGGR----QLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 149 RALATQPRILLLDEPFGALDAKVRkdlRRWLRALHDeyHF---TSIFVTHdQEEALELSDQVVVMSQGQ-VEQ 217
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETE---RQILELLAE--HAqnkTVLMITH-RLTGLEQFDRICVMDNGQiIEQ 554
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-229 |
7.83e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.61 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD--DVSQ---LHVRdRNIGFVFQ--HYALFrH 88
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKrglLALR-QQVATVFQdpEQQIF-Y 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAFGLESLPKkqrpSKQEIRQRVAKLLEMIQLPELaKRYPAQ-LSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PRK13638 93 TDIDSDIAFSLRNLGV----PEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 168 DAKVRKDLRRWLRALHDEYHFTsIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPE 229
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-216 |
1.89e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.51 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINkhfGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLeSSDSGRV-----LFGGDDVSQLHVRDR- 74
Cdd:COG4170 9 LTIEIDTPQ---GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 75 -----NIGFVFQHYAlfRHLTVAENIAFGL-ESLPKKQRPSK-----QEIRQRVAKLLEMIQLPE---LAKRYPAQLSGG 140
Cdd:COG4170 85 kiigrEIAMIFQEPS--SCLDPSAKIGDQLiEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDhkdIMNSYPHELTEG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 141 QKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ-VE 216
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQtVE 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-224 |
2.79e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.85 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVR--DRNIGFVFQHYALFRHLTVAENI 95
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDL 175
Cdd:PRK10575 107 AIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 176 RRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGL 224
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-215 |
3.45e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.56 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHF-GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLhVRDRNIGFVF 80
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYAL---FRHLtVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRI 157
Cdd:PRK15056 85 QSEEVdwsFPVL-VEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDqVVVMSQGQV 215
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-214 |
4.85e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.56 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD---SGRVLFGGDDVSQL------HVRDRNIGFVFQH- 82
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLpekelnKLRAEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 -YALFRHLTVAENIafgLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKR---YPAQLSGGQKQRVALARALATQPRIL 158
Cdd:PRK09473 107 mTSLNPYMRVGEQL---MEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-217 |
6.97e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.09 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHV---RDRnIGFVFQHYALFRHlTVAE 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRSR-LAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGleslpkkqRP--SKQEIrQRVAKLL----EMIQLP-----ELAKRyPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK10789 408 NIALG--------RPdaTQQEI-EHVARLAsvhdDILRLPqgydtEVGER-GVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 163 PFGALDAK----VRKDLRRWLRalhdeyHFTSIFVTHdQEEALELSDQVVVMSQGQVEQ 217
Cdd:PRK10789 478 ALSAVDGRtehqILHNLRQWGE------GRTVIISAH-RLSALTEASEILVMQHGHIAQ 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-163 |
2.01e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.96 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRN---IGFV 79
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVcprIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 FQHYA--LFRHLTVAENIAF-----GLeslpkkqrpSKQEIRQRVAKLLEMIQLPELAKRyPA-QLSGGQKQRVALARAL 151
Cdd:NF033858 82 PQGLGknLYPTLSVFENLDFfgrlfGQ---------DAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCAL 151
|
170
....*....|..
gi 1430737237 152 ATQPRILLLDEP 163
Cdd:NF033858 152 IHDPDLLILDEP 163
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-215 |
5.31e-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: 89.51 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESS--DSGRVLFGGDDVSQLHVRDR---NIGFVFQHYALFR 87
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAE-----NIAFgleslpkkqrpskqeirqrvakllemiqlpelakrypaqlSGGQKQRVALARALATQPRILLLDE 162
Cdd:cd03217 91 GVKNADflryvNEGF----------------------------------------SGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHdQEEALEL--SDQVVVMSQGQV 215
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRI 183
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-214 |
7.64e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.10 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVlfggddvsqlhvrdrnigfvfqhyalfrHLTVAENIAF 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------------------------ARPAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 glesLPkkQRP---------------SKQEI-RQRVAKLLEMIQLPELAKRY------PAQLSGGQKQRVALARALATQP 155
Cdd:COG4178 431 ----LP--QRPylplgtlreallypaTAEAFsDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 156 RILLLDEPFGALDAKVRKDLrrwLRALHDEY-HFTSIFVTHdQEEALELSDQVVVMSQGQ 214
Cdd:COG4178 505 DWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-215 |
1.57e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSdSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHLTVAENI 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGLESLPkkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALAT-------QPRILLLDEPFGALD 168
Cdd:COG4138 91 ALHQPAGA-----SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1430737237 169 AKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:COG4138 166 VAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-169 |
2.59e-20 |
|
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: 87.93 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLF-GGDDVSQLHVRDRNIGFVFQHYALFRHLTV 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 92 AENIAFGleslpkkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:cd03231 91 LENLRFW----------HADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-210 |
2.73e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.09 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 1 MSITIDQINKHFggfqaLKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESsdsgrvlfGGDDVSQLHVRDRNIGfvf 80
Cdd:COG2401 34 FGVELRVVERYV-----LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--------GTPVAGCVDVPDNQFG--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 qhyalfRHLTVAENIafgleslpkkqrPSKQEIRQrVAKLLEMIQL--PELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:COG2401 98 ------REASLIDAI------------GRKGDFKD-AVELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 159 LLDEpFGA-LDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVM 210
Cdd:COG2401 159 VIDE-FCShLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-215 |
2.96e-20 |
|
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: 87.70 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 10 KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLES---SDSGRVLFGGDDVSQLHVR-DRNIGFVFQHYAL 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKyPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 86 FRHLTVAENIAFgleslpkkqrpskqeirqrVAKLlemiqlpeLAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:cd03233 95 FPTLTVRETLDF-------------------ALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQ--EEALELSDQVVVMSQGQV 215
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLK-TTTFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-221 |
3.50e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 87.93 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAEN 94
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGLESlpkkqrpSKQEIRQrvakLLEMIQLPELAKRYP-----------AQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:cd03244 98 LDPFGEY-------SDEELWQ----ALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 164 FGALD----AKVRKDLRRWLRalhdeyHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSP 221
Cdd:cd03244 167 TASVDpetdALIQKTIREAFK------DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-169 |
3.95e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAE 93
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLFNR-SIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGleslpkkqRPSKQEIRQRVAklLEMIQLPELAKRYPA-----------QLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK13657 428 NIRVG--------RPDATDEEMRAA--AERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDE 497
|
....*..
gi 1430737237 163 PFGALDA 169
Cdd:PRK13657 498 ATSALDV 504
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-216 |
5.19e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.15 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLfggddvsqlhvRDRNIGFVFQHyALFRHLTVAENIAF 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 GLEslpkkQRPSKQEIRQRVAKL-LEMIQLP-----ELAKRyPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKV 171
Cdd:PTZ00243 744 FDE-----EDAARLADAVRVSQLeADLAQLGggletEIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1430737237 172 RKDLRR--WLRALHDEyhfTSIFVTHdQEEALELSDQVVVMSQGQVE 216
Cdd:PTZ00243 818 GERVVEecFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-196 |
5.28e-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: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGgddvsqlhvRDRNIGFVFQHYALFRHLTVAENIAF 97
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------PGIKVGYLPQEPQLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 GLESLPKKQRpSKQEIRQRVA-------KLL-EMIQLPEL------------------AKRYP------AQLSGGQKQRV 145
Cdd:TIGR03719 92 GVAEIKDALD-RFNEISAKYAepdadfdKLAaEQAELQEIidaadawdldsqleiamdALRCPpwdadvTKLSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 146 ALARALATQPRILLLDEPFGALDAKVRKDLRRWLRalhdEYHFTSIFVTHD 196
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHD 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-212 |
7.85e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.86 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVlfggddvsqLHVRDRNIGFVFQ- 81
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 -HYALFRHLTVAENIAFgleslpkkqRPSKQeiRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:PRK09544 76 lYLDTTLPLTVNRFLRL---------RPGTK--KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 161 DEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQ 212
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-227 |
8.33e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.34 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 10 KHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRV-LFGGD-DVSQLHVRdRNIGFVFQHYALFR 87
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPvDAGDIATR-RRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIA-----FGLEslpkkqrpsKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:NF033858 353 ELTVRQNLElharlFHLP---------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 163 PFGALDAKVRKDLRRWLRALHDEYHFTsIFV-THDQEEAlELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-214 |
1.28e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.85 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL--ESSDSGRVLFGGDDVSQLHVRD---RNIGFVFQH 82
Cdd:NF040905 7 ITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDseaLGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFGLEslpkkqrPSK------QEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:NF040905 87 LALIPYLSIAENIFLGNE-------RAKrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-215 |
1.75e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFqalKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR-NIGFVF-----QHYALFR 87
Cdd:PRK15439 278 GF---RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENI-AFGLESLPKKQRPSKQEI---RQRVAKLLEMIQLPELAKRypaqLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:PRK15439 355 DAPLAWNVcALTHNRRGFWIKPARENAvleRYRRALNIKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 164 FGALDAKVRKDLRRWLRALHdEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-217 |
4.31e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.62 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL-H-VRDRNIGFVFQHYALFRHlTVAENI 95
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLsHsVLRQGVAMVQQDPVVLAD-TFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGleslpkkqRPSKQEirqRVAKLLEMIQLPELAKRYPA-----------QLSGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PRK10790 436 TLG--------RDISEE---QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 165 GALDAKVRKDLRRWLRALHDeyHFTSIFVTHDQEEALElSDQVVVMSQGQ-VEQ 217
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQaVEQ 555
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-213 |
1.30e-18 |
|
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: 83.53 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGG---DDVSQLHVRDRN---IGFVFQHYALFr 87
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNkneSEPSFEATRSRNrysVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAFGleSLPKKQRpSKQEIR----QRVAKLLEMIQLPELAKRyPAQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:cd03290 92 NATVEENITFG--SPFNKQR-YKAVTDacslQPDIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 164 FGALDAKVRKDLRR--WLRALHDEYHfTSIFVTHdQEEALELSDQVVVMSQG 213
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKR-TLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-195 |
1.59e-18 |
|
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: 81.82 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVlfggddvsqlhvrdrnigfvfqhyalfrHLTVAENIAF 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------------------GMPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 glesLPkkQRP--SKQEIRQRVAkllemiqlpelakrYP--AQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVrk 173
Cdd:cd03223 69 ----LP--QRPylPLGTLREQLI--------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES-- 126
|
170 180
....*....|....*....|..
gi 1430737237 174 dLRRWLRALHDEyHFTSIFVTH 195
Cdd:cd03223 127 -EDRLYQLLKEL-GITVISVGH 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-227 |
1.61e-18 |
|
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: 87.69 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGddvsqlhvrdrNIGFVFQHyALFRHLTVAENIAF 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 GLESLPKKQrpskQEIRQRVAKLLEMIQLP-----ELAKRyPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:TIGR00957 722 GKALNEKYY----QQVLEACALLPDLEILPsgdrtEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 173 KDLRRWLRA----LHDEyhfTSIFVTHDQeEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:TIGR00957 797 KHIFEHVIGpegvLKNK---TRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-214 |
3.64e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 8 INKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV---SQLHVRDRNIGFVFQHYA 84
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 LFRHLTVAENIAFGleSLPKKQRPSKQEIRQRVAK-LLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEP 163
Cdd:PRK10982 84 LVLQRSVMDNMWLG--RYPTKGMFVDQDKMYRDTKaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 164 FGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-247 |
8.59e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 83.31 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLeSSDSGRVL---FGGDDVSQLHVRDR--------NIGFVFQ 81
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrMRFDDIDLLRLSPRerrklvghNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYAlfRHLTVAENIAFGL-ESLP----KKQRPSKQEIRQRVA-KLLEMIQLPE---LAKRYPAQLSGGQKQRVALARALA 152
Cdd:PRK15093 97 EPQ--SCLDPSERVGRQLmQNIPgwtyKGRWWQRFGWRKRRAiELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQV-------EQVNSPTGLY 225
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTvetapskELVTTPHHPY 254
|
250 260
....*....|....*....|....*...
gi 1430737237 226 ARPESRFVFDF---LGH---VNVLSGLV 247
Cdd:PRK15093 255 TQALIRAIPDFgsaMPHksrLNTLPGAI 282
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-231 |
4.36e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 19 KNVSLDIPEGQLTALLGPSGSGKT----TLLRII-AGLESSdSGRVLFGGDDVSQLHVRDRNIGFVFQH-YALFRHL-TV 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPCALRGRKIATIMQNpRSAFNPLhTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AeniAFGLESLPKKQRPSKqeiRQRVAKLLEMIQLPE---LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK10418 99 H---THARETCLALGKPAD---DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 169 AKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESR 231
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-168 |
5.97e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.45 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ-LHVRDRNIGFVFQHYALFRHLTVAENIA 96
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 97 FGLESlpkkqRPSKQEIRQ--RVAKLLEMIQLPelakryPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK13540 97 YDIHF-----SPGAVGITElcRLFSLEHLIDYP------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-196 |
1.42e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.13 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFgGDDVsqlhvrdrNIGFVFQ- 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLE--SLPKKQRPSKQEI----------RQRVakllemiqlpelakrypAQLSGGQKQRVALAR 149
Cdd:TIGR03719 394 RDALDPNKTVWEEISGGLDiiKLGKREIPSRAYVgrfnfkgsdqQKKV-----------------GQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1430737237 150 ALATQPRILLLDEPFGALDAKVrkdlrrwLRALHD---EYHFTSIFVTHD 196
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVET-------LRALEEallNFAGCAVVISHD 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-196 |
2.11e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.55 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSdsgrvlFGGDDVSQLHVRdrnIGFVFQHYALFRHLTVAENI 95
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPAPGIK---VGYLPQEPQLDPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGL-ESLPKKQR------------PSKQEIRQRVAKLLEMI----------QLpELAK---RYP------AQLSGGQKQ 143
Cdd:PRK11819 92 EEGVaEVKAALDRfneiyaayaepdADFDALAAEQGELQEIIdaadawdldsQL-EIAMdalRCPpwdakvTKLSGGERR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 144 RVALARALATQPRILLLDEPFGALDAK-VrkdlrRWL-RALHDeYHFTSIFVTHD 196
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAEsV-----AWLeQFLHD-YPGTVVAVTHD 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-214 |
2.70e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 28 GQLTALLGPSGSGKTTLLRIIAG-LESSD-SGRVLFGGDDVSQLHVRdrNIGFVFQHYALFRHLTVAENIAF-GLESLPK 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTKQILK--RTGFVTQDDILYPHLTVRETLVFcSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 105 KQrpSKQEiRQRVAKllEMIQLPELAK--------RYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLR 176
Cdd:PLN03211 172 SL--TKQE-KILVAE--SVISELGLTKcentiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 1430737237 177 RWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQ 214
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-268 |
2.82e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.01 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLlRIIAGLESSDSGRV--LFGGDDVSQLHVRdRNIGFv 79
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRpwRF*TWCANRRALR-RTIG*- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 fqhyalFRHLTVAENIAF-GLESLPKKQRP---SKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQP 155
Cdd:NF000106 90 ------HRPVR*GRRESFsGRENLYMIGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVV------VMSQGQVEQVNSPTG---LYA 226
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTvidrgrVIADGKVDELKTKVGgrtLQI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1430737237 227 RPESRFVFDFLGHVNVLSGL--VKGQKLVQGDAWVSLPGIRQDQ 268
Cdd:NF000106 243 RPAHAAELDRMVGAIAQAGLdgIAGATADHEDGVVNVPIVSDEQ 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-217 |
3.27e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.41 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAG-LESSDSGRVLFGGddvsqlhvrdrNIGFVFQHYALFrHLTVAENIA 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRG-----------SVAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 97 FGLESLPKKQ-RPSKQEIRQRVAKLLEMIQLPELAKRyPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDL 175
Cdd:PLN03232 701 FGSDFESERYwRAIDVTALQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1430737237 176 rrWLRALHDEYH-FTSIFVThDQEEALELSDQVVVMSQGQVEQ 217
Cdd:PLN03232 780 --FDSCMKDELKgKTRVLVT-NQLHFLPLMDRIILVSEGMIKE 819
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-211 |
3.53e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.46 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 55 DSGRVLFGGDDVSQLHVRD-RNIGFVFQHYALFRHLTVAENIAFGleslpkKQRPSKQEIRQ--RVAKLLEMIQ-LPELA 130
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRacKFAAIDEFIEsLPNKY 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 131 KR----YPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHdQEEALELSDQ 206
Cdd:PTZ00265 1349 DTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
....*
gi 1430737237 207 VVVMS 211
Cdd:PTZ00265 1428 IVVFN 1432
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-213 |
5.13e-16 |
|
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: 75.36 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD--SGRVLFGGDDVSQLHvrDRNIGFVFQHYALFRHLTVAE 93
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNF--QRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAFGleslpkkqrpskqeirqrvAKLLEmiqlpelakrypaqLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRK 173
Cdd:cd03232 99 ALRFS-------------------ALLRG--------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1430737237 174 DLRRWLRALHDeyHFTSIFVTHDQEEA--LELSDQVVVMSQG 213
Cdd:cd03232 146 NIVRFLKKLAD--SGQAILCTIHQPSAsiFEKFDRLLLLKRG 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-214 |
6.51e-16 |
|
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: 77.20 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGddvsqlhvrdrNIGFVFQhYALFRHLTVAENIAF 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQ-FSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 GLeslpkkqrpSKQEIRQRvaKLLEMIQLPELAKRYPAQ-----------LSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:cd03291 121 GV---------SYDEYRYK--SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 167 LDAKVRKDLRRW----LRAlhdeyHFTSIFVTHDQEEaLELSDQVVVMSQGQ 214
Cdd:cd03291 190 LDVFTEKEIFEScvckLMA-----NKTRILVTSKMEH-LKKADKILILHEGS 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-224 |
1.01e-15 |
|
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: 75.91 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 7 QINKHFGGFQaLKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVS----------QLHVRDrni 76
Cdd:cd03237 5 TMKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadyEGTVRD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 gfvFQHYALFRHLTVAEniafgleslpkkqrpskqeIRQRVAKLLEMIQLPElakRYPAQLSGGQKQRVALARALATQPR 156
Cdd:cd03237 81 ---LLSSITKDFYTHPY-------------------FKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDAD 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 157 ILLLDEPFGALDAKVR----KDLRRWlrALHDEYhfTSIFVTHDQEEALELSDQVVVMS--QGQVEQVNSPTGL 224
Cdd:cd03237 136 IYLLDEPSAYLDVEQRlmasKVIRRF--AENNEK--TAFVVEHDIIMIDYLADRLIVFEgePSVNGVANPPQSL 205
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
32-168 |
1.40e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 32 ALL--GPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHvRDRNIGFVFQHYALFRHLTVAENIAF--GLESLPKKQR 107
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLENLHFlcGLHGRRAKQM 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 108 PSKQeirqrvaklLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK13543 118 PGSA---------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-213 |
1.87e-15 |
|
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: 78.03 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAG-LESSDsGRVLFGGddvsqlhvrdrNIGFVFQhYALFRHLTVAENIA 96
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSE-GKIKHSG-----------RISFSPQ-TSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 97 FGLeslpkkqrpSKQEIRQRvaKLLEMIQLPELAKRYPAQ-----------LSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:TIGR01271 509 FGL---------SYDEYRYT--SVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 166 ALDAKVRKDL-RRWLRALHDEYhfTSIFVThDQEEALELSDQVVVMSQG 213
Cdd:TIGR01271 578 HLDVVTEKEIfESCLCKLMSNK--TRILVT-SKLEHLKKADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-213 |
1.92e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.23 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAglESSDSGrVLFGGDDVSQLHVRD----RNIGFVFQHYALFRHLTV 91
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFGL-----ESLPKKQrpsKQEIRQRVAKLLEMIQLPELAKRYPAQ-LSGGQKQRVALARALATQPRILL-LDEPF 164
Cdd:TIGR00956 854 RESLRFSAylrqpKSVSKSE---KMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 165 GALDAKVRKDLRRWLRALHDeyHFTSIFVTHDQEEA--LELSDQVVVMSQG 213
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLAD--HGQAILCTIHQPSAilFEEFDRLLLLQKG 979
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-229 |
1.93e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAG--LESSDSGRVLFGGD-----------DVSQLhVRDRNI-------G 77
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDvtlngeplaaiDAPRL-ARLRAVlpqaaqpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFqhyalfrhlTVAENIAFGleSLPKKQRPSKQEIRQR--VAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALA--- 152
Cdd:PRK13547 96 FAF---------SAREIVLLG--RYPHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 153 ------TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYa 226
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL- 243
|
...
gi 1430737237 227 RPE 229
Cdd:PRK13547 244 TPA 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-217 |
2.07e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAG--LESSDSGRVLFGgddvsqlhvrdrNIGFVFQHYALFrHLTVAENI 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGelPPRSDASVVIRG------------TVAYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGLESLPKK-QRPSKQEIRQRVAKLLEMIQLPELAKRyPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKV--- 171
Cdd:PLN03130 700 LFGSPFDPERyERAIDVTALQHDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrq 778
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1430737237 172 --RKDLRRWLRalhdeyHFTSIFVThDQEEALELSDQVVVMSQGQVEQ 217
Cdd:PLN03130 779 vfDKCIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKE 819
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-214 |
3.33e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.46 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIA----GLESSDSGRVLFGGddVSQLHVRDRNIGFVF---QHYALFR 87
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG--ITPEEIKKHYRGDVVynaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAFGLESLPKKQRP---SKQEIRQRVAKL------LEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRIL 158
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPdgvSREEYAKHIADVymatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRALHDEYHFTSiFVTHDQ--EEALELSDQVVVMSQGQ 214
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTP-LVAIYQcsQDAYELFDKVIVLYEGY 288
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-196 |
3.49e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.91 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 12 FGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD-DVSQLHvRD--RNI-GFVFQHyalfr 87
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQ-QDppRNVeGTVYDF----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 hltVAENIAFGLESLPKKQR--------PSKQEIRQ------------------RVAKLLEMIQLPELAKRypAQLSGGQ 141
Cdd:PRK11147 87 ---VAEGIEEQAEYLKRYHDishlvetdPSEKNLNElaklqeqldhhnlwqlenRINEVLAQLGLDPDAAL--SSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 142 KQRVALARALATQPRILLLDEPFGALDAkvrkDLRRWLRALHDEYHFTSIFVTHD 196
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
9.48e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNiGFVF-----QHYALFRHLT 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglAN-GIVYisedrKRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAF-GLESLPKKQ-RPSKQEIRQRVAKLLEM--IQLPELAKRYpAQLSGGQKQRVALARALATQPRILLLDEPFGA 166
Cdd:PRK10762 347 VKENMSLtALRYFSRAGgSLKHADEQQAVSDFIRLfnIKTPSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1430737237 167 LDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK10762 426 VDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-202 |
1.11e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFgGDDVSqlhvrdrnIGFVFQH 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK--------LAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YAlfrHL----TVAENIAFGLE--SLPKKQRPSKQEI---------RQRVAKllemiqlpelakrypaQLSGGQKQRVAL 147
Cdd:PRK11819 396 RD---ALdpnkTVWEEISGGLDiiKVGNREIPSRAYVgrfnfkggdQQKKVG----------------VLSGGERNRLHL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 148 ARALATQPRILLLDEPFGALDAKVrkdlrrwLRALhdeyhftsifvthdqEEALE 202
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVET-------LRAL---------------EEALL 489
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-215 |
1.47e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 21 VSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSdSGRVLFGGDDVSQLHVRD--RNIGF------------VFQHYALf 86
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElaRHRAYlsqqqtppfampVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 87 rhltvaeniafgleSLPKKQRPskQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALA-------RALATQPRILL 159
Cdd:PRK03695 93 --------------HQPDKTRT--EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHdEYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-221 |
2.09e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.59 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAE 93
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NiafglesLPKKQRPSKQEIRqrvaKLLEMiqlpelaKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGAL----DA 169
Cdd:cd03369 101 N-------LDPFDEYSDEEIY----GALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 170 KVRKDLRrwlralhDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSP 221
Cdd:cd03369 163 LIQKTIR-------EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-227 |
3.00e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 70.98 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFqALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQlHVRDR---NIGFVFQHYALFRHL 89
Cdd:COG4615 344 EGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-DNREAyrqLFSAVFSDFHLFDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 tvaeniaFGLESLPkkqrpskqeIRQRVAKLLEMIQLPE--------LAKRypaQLSGGQKQRVALARALATQPRILLLD 161
Cdd:COG4615 422 -------LGLDGEA---------DPARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALLVALLEDRPILVFD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 162 E------PfgaldakvrkDLRRW--------LRALhdeyHFTSIFVTHDqEEALELSDQVVVMSQGQVEQVNSPTGLYAR 227
Cdd:COG4615 483 EwaadqdP----------EFRRVfytellpeLKAR----GKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-196 |
6.83e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFqalknvSLDIPEGQL-----TALLGPSGSGKTTLLRIIAGLESSDSGRVlFGGDDVS---QLHVRDR 74
Cdd:COG1245 342 VEYPDLTKSYGGF------SLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISykpQYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 75 NIgfvfqhyalfrhlTVAENiafgLESLPKKQRPS---KQEIRQRvakllemIQLPELAKRYPAQLSGGQKQRVALARAL 151
Cdd:COG1245 415 DG-------------TVEEF----LRSANTDDFGSsyyKTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACL 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1430737237 152 ATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHD 196
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-232 |
8.67e-13 |
|
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: 67.63 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQL--HVRDRNIGFVFQHYALFrhltvAENI 95
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILF-----SGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGLEslpkkqrPSKQEIRQRVAKLLEMIQLPELAKRYPAQL-----------SGGQKQRVALARALATQPRILLLDEPF 164
Cdd:cd03288 112 RFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 165 GALDAKVRKDLRR-WLRALHDEyhfTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSPTGLYARPESRF 232
Cdd:cd03288 185 ASIDMATENILQKvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-214 |
8.74e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFqALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHLt 90
Cdd:PRK10522 335 NGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 vaeniafglesLPKKQRPSKQEIRQRVAKLLEMIQLPELA--KRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALD 168
Cdd:PRK10522 413 -----------LGPEGKPANPALVEKWLERLKMAHKLELEdgRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1430737237 169 AKVRKDLRRWLRALHDEYHFTSIFVTHDqEEALELSDQVVVMSQGQ 214
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-220 |
1.21e-12 |
|
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: 67.57 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDsGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlt 90
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 vaeniafgleSLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQL-----------SGGQKQRVALARALATQPRILL 159
Cdd:cd03289 92 ----------TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRalHDEYHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNS 220
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDS 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-218 |
1.89e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDV---SQLHVRDRNIGFVFQHY---ALFRH 88
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYITESRrdnGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 89 LTVAENIAF----------GLESL--PKKQRPSKQEIRQRVAkllemIQLPELAKRYpAQLSGGQKQRVALARALATQPR 156
Cdd:PRK09700 356 FSIAQNMAIsrslkdggykGAMGLfhEVDEQRTAENQRELLA-----LKCHSVNQNI-TELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQGQVEQV 218
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-213 |
2.76e-12 |
|
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: 63.93 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 28 GQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDRNIGFVFqhyalfrhltvaeniafgleslpkkqr 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 108 pskqeirqrvakllemiqlpelaKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLR-----RWLRAL 182
Cdd:smart00382 55 -----------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLL 111
|
170 180 190
....*....|....*....|....*....|....*.
gi 1430737237 183 HDEYHFTSIFVTHDQEEALEL-----SDQVVVMSQG 213
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPAllrrrFDRRIVLLLI 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-215 |
3.54e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 20 NVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL-ESSDSGRVLFGGDDVSQLHVRD---RNIGFVFQ---HYALFRHLTVA 92
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEdrkRDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 ENIAfgLESLPKKQRPSK-------QEIRQRVAKLLEMIQLPELAKrypAQLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:PRK13549 360 KNIT--LAALDRFTGGSRiddaaelKTILESIQRLKVKTASPELAI---ARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-220 |
3.57e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.01 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDsGRVLFGG---DDVSqLHVRDRNIGFVFQHYALFRHl 89
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVT-LQTWRKAFGVIPQKVFIFSG- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 90 tvaeniafgleSLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQL-----------SGGQKQRVALARALATQPRIL 158
Cdd:TIGR01271 1307 -----------TFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 159 LLDEPFGALDAKVRKDLRRWLRalHDEYHFTSIFVTHDQEEALElSDQVVVMSQGQVEQVNS 220
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDS 1434
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-216 |
3.91e-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: 67.16 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 6 DQINKHFggfQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGL-ESSDSGRVLFGGDDV---SQLHVRDRNIGFV-- 79
Cdd:TIGR02633 267 DVINPHR---KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirNPAQAIRAGIAMVpe 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 80 -FQHYALFRHLTVAENIAFG-LESLPKKQR----PSKQEIRQRVAKLLEMIQLPELAKrypAQLSGGQKQRVALARALAT 153
Cdd:TIGR02633 344 dRKRHGIVPILGVGKNITLSvLKSFCFKMRidaaAELQIIGSAIQRLKVKTASPFLPI---GRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 154 QPRILLLDEPFGALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQVE 216
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-198 |
4.33e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 5 IDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGgddvSQLHVrdrniGFVFQHYA 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEV-----AYFDQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 -LFRHLTVAENIAFGleslpkkqrpsKQEI----RQR-VAKLLEMIQLPELAKRYPAQ-LSGGQKQRVALARALATQPRI 157
Cdd:PRK11147 393 eLDPEKTVMDNLAEG-----------KQEVmvngRPRhVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1430737237 158 LLLDEPFGALDAKVRKdlrrWLRALHDEYHFTSIFVTHDQE 198
Cdd:PRK11147 462 LILDEPTNDLDVETLE----LLEELLDSYQGTVLLVSHDRQ 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-196 |
5.82e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFqalknvSLDIPEGQL-----TALLGPSGSGKTTLLRIIAGLESSDSGRVLFggddvsqlhvrDRNIG 77
Cdd:PRK13409 341 VEYPDLTKKLGDF------SLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------ELKIS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 78 FVFQHYALFRHLTVAENiafgLESLPKKQRPS--KQEIRQRvakllemIQLPELAKRYPAQLSGGQKQRVALARALATQP 155
Cdd:PRK13409 404 YKPQYIKPDYDGTVEDL----LRSITDDLGSSyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1430737237 156 RILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFVTHD 196
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-215 |
1.71e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLE--SSDSGRVLFGGDDVSQLHVRDRNIGFVF 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QHYALFRHLTVAENIAFGLESLPKKQRPSKQEIRQR------VAKLLEMIQLPE--LAKRYPAQLSGGQKQRVALARALA 152
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRfdfqdlMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQeEALEL--SDQVVVMSQGQV 215
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQ-RILDYikPDYVHVLYQGRI 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-216 |
2.05e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGgddvsqlhvRDRNIGFVFQ- 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------ENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALF-RHLTVAENIafgleSLPKKQRPSKQEIRQRVAKLLEMiqlPELAKRYPAQLSGGQKQRVALARALATQPRILLL 160
Cdd:PRK15064 391 HAYDFeNDLTLFDWM-----SQWRQEGDDEQAVRGTLGRLLFS---QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 161 DEPFGALDAKVRKDLRRWLralhDEYHFTSIFVTHDQE-------EALELSDQVVVMSQGQVE 216
Cdd:PRK15064 463 DEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREfvsslatRIIEITPDGVVDFSGTYE 521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-232 |
3.36e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAENI 95
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 afgleslpkkqRPSKQEIRQRVAKLLEMIQLPELAKRYPAQL-----------SGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PLN03232 1331 -----------DPFSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 165 GALDAKVRKDLRRWLRalhDEYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVNSPTGLYARPESRF 232
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIR---EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-210 |
3.56e-11 |
|
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: 62.77 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 11 HFGGFQALKNVSLDIP-EGQLTALLGPSGSGKTTLLRIIAGLESSDSGRvlFGG----DDVSQlHVRdrniGFVFQHY-- 83
Cdd:cd03236 8 HRYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDppdwDEILD-EFR----GSELQNYft 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 84 -ALFRHLTVAENIAFgLESLPKKQRPSKQEIRQRVAK------LLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPR 156
Cdd:cd03236 81 kLLEGDVKVIVKPQY-VDLIPKAVKGKVGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTsIFVTHDQEEALELSDQVVVM 210
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDYLSDYIHCL 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-213 |
3.75e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQ--ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD----DVSQLHvrdRNI 76
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVH---QNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 77 GFVFQHYALFRHLTVAENIAF--GLESLPKKqrpskqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQ 154
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLyaRLRGVPAE------EIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 155 PRILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQEEALELSDQVVVMSQG 213
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-200 |
7.97e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLE----SSDSgrVLFGGDDVSQLHVRD--RNIGFVFQHYAL-FRHLT 90
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgySNDL--TLFGRRRGSGETIWDikKHIGYVSSSLHLdYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 91 VAENIAFG--LESLPKKQRPSKQEiRQRVAKLLEMIQLPELAKRYPAQ-LSGGQkQRVAL-ARALATQPRILLLDEPFGA 166
Cdd:PRK10938 354 SVRNVILSgfFDSIGIYQAVSDRQ-QKLAQQWLDILGIDKRTADAPFHsLSWGQ-QRLALiVRALVKHPTLLILDEPLQG 431
|
170 180 190
....*....|....*....|....*....|....
gi 1430737237 167 LDAKVRKDLRRWLRALHDEYHFTSIFVTHDQEEA 200
Cdd:PRK10938 432 LDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
3-214 |
9.14e-11 |
|
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: 60.03 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHfggfqALKNVSLDIPEGQLTALLGPSGSGKTTLLRiiAGLESSDSGRVlfggddVSQLHVRDRN-IGFVFQ 81
Cdd:cd03238 1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL------ISFLPKFSRNkLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALfrhltvaenIAFGLESLPKKQRPSkqeirqrvakllemiqlpelakrypaQLSGGQKQRVALARALA--TQPRILL 159
Cdd:cd03238 68 LQFL---------IDVGLGYLTLGQKLS--------------------------TLSGGELQRVKLASELFsePPGTLFI 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDqEEALELSDQVVVMSQGQ 214
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHN-LDVLSSADWIIDFGPGS 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-217 |
9.45e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 15 FQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGdDVSQLHVrdrNIGFVFQhyalfrhLTVAEN 94
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAI---SAGLSGQ-------LTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFGLESLPKKQRpskqEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEpfgALDAKVRKD 174
Cdd:PRK13546 106 IEFKMLCMGFKRK----EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1430737237 175 LRRWLRALHD--EYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQ 217
Cdd:PRK13546 179 AQKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-195 |
9.85e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 19 KNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFggDDVSQLhvRDRN-------IGFVFQHYALFRHlTV 91
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNL--KDINlkwwrskIGVVSQDPLLFSN-SI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 92 AENIAFGLESL----------------PKKQRPSKQEIRQRVAKLLEMI-------QLPELAKRY--------------- 133
Cdd:PTZ00265 477 KNNIKYSLYSLkdlealsnyynedgndSQENKNKRNSCRAKCAGDLNDMsnttdsnELIEMRKNYqtikdsevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 134 --------------------PAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTSIFV 193
Cdd:PTZ00265 557 lihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
..
gi 1430737237 194 TH 195
Cdd:PTZ00265 637 AH 638
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-232 |
2.65e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFrhltvAENI 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLF-----SGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGLEslpkkqrPSKQEIRQRVAKLLEMIQLPELAKRYPAQL-----------SGGQKQRVALARALATQPRILLLDEPF 164
Cdd:PLN03130 1330 RFNLD-------PFNEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 165 GAL----DAKVRKDLRRWLRALhdeyhfTSIFVTHDQEEALElSDQVVVMSQGQVEQVNSPTGLYARPESRF 232
Cdd:PLN03130 1403 AAVdvrtDALIQKTIREEFKSC------TMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-208 |
4.11e-10 |
|
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: 58.77 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 30 LTALLGPSGSGKTTLLR-IIAGL--ESSDSGRVLFGGDDVSQLHVRDRNIGFVFQH-----YALFRHLTVAENIAFgles 101
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 102 lpkkqrpskqeIRQ-RVAKLLEmiqlpelakRYPAQLSGGQKQ------RVALARALATQPRILLLDEPFGALDA-KVRK 173
Cdd:cd03240 100 -----------CHQgESNWPLL---------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1430737237 174 DLRRWLRALHDEYHFTSIFVTHDqEEALELSDQVV 208
Cdd:cd03240 160 SLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
4.20e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 21 VSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRDR-NIGFVF-----QHYALFRHLTVAEN 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiRAGIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IA---------FGLESLPKKQRPSKQEIRQRVAkllemIQLPElAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFG 165
Cdd:PRK11288 352 INisarrhhlrAGCLINNRWEAENADRFIRSLN-----IKTPS-REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1430737237 166 ALDAKVRKDLRRWLRALHDEyHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-198 |
4.61e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAgLESSD----SGRVL-----FGGDDVSQLH-VR 72
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkNCQILhveqeVVGDDTTALQcVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 73 DRNI--GFVFQHYA--LFRHLTVAENIAFGLESLPKKQRPSKQEIRQRVA---KLLEMIQL-----------------PE 128
Cdd:PLN03073 257 NTDIerTQLLEEEAqlVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEeiyKRLELIDAytaearaasilaglsftPE 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 129 LAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVrkdlRRWLRALHDEYHFTSIFVTHDQE 198
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTFIVVSHARE 402
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-180 |
8.25e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD--SGRVLFGGDDVSQlHVRDRNIGFVFQHYALFRHLTVAE 93
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQ-ETFARISGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 94 NIAF-GLESLPKKQrpSKQEIRQRVAKLLEMIQLPELAKR---YPA--QLSGGQKQRVALARALATQPRILLLDEPFGAL 167
Cdd:PLN03140 973 SLIYsAFLRLPKEV--SKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170
....*....|...
gi 1430737237 168 DAKVRKDLRRWLR 180
Cdd:PLN03140 1051 DARAAAIVMRTVR 1063
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-195 |
1.39e-09 |
|
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: 59.76 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIPEGQLTALLGPSGSGKTTLLRIIAGLESsdsgrvLFGGddvsQLHV-RDRNIGFVFQH-YALFRhlTVAENIAFGL 99
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWP------VYGG----RLTKpAKGKLFYVPQRpYMTLG--TLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 100 ESLPKKQRP-SKQEIRQrvakLLEMIQLPELAKR---------YPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:TIGR00954 540 SSEDMKRRGlSDKDLEQ----ILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*.
gi 1430737237 170 KVRKDLRRWLRalhdEYHFTSIFVTH 195
Cdd:TIGR00954 616 DVEGYMYRLCR----EFGITLFSVSH 637
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-226 |
2.08e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQ--LHVRDRNIGFVFQHYALFRHltvaeni 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFSG------- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 afgleSLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQL-----------SGGQKQRVALARALATQPRILLLDEPF 164
Cdd:TIGR00957 1375 -----SLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 165 GALDAKVRKDLRRWLRALHDEyhFTSIFVTHDQEEALELSdQVVVMSQGQVEQVNSPTGLYA 226
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-215 |
2.63e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSD--SGRVLFGGDDVSQLHVRDRN---IGFVFQhYALfr 87
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAhlgIFLAFQ-YPI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAFGLESLPKKQRPSKQ------EIRQRVAKLLEMIQLPE--LAKRYPAQLSGGQKQRVALARALATQPRILL 159
Cdd:CHL00131 95 EIPGVSNADFLRLAYNSKRKFQGLpeldplEFLEIINEKLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 160 LDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDQeEALE--LSDQVVVMSQGQV 215
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQ-RLLDyiKPDYVHVMQNGKI 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-183 |
2.81e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIPEGQLTALLGPSGSGKTTLLRIIAGlessdsGRVLFGGDDVSQlhvrdrnigfvFQHYALFrhltvaeniafgleS 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG------ELPLLSGERQSQ-----------FSHITRL--------------S 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 102 LPKKQRPSKQEIRQRVAKLL------------EMIQL----PELAKRYPAQ-------------LSGGQKQRVALARALA 152
Cdd:PRK10938 72 FEQLQKLVSDEWQRNNTDMLspgeddtgrttaEIIQDevkdPARCEQLAQQfgitalldrrfkyLSTGETRKTLLCQALM 151
|
170 180 190
....*....|....*....|....*....|.
gi 1430737237 153 TQPRILLLDEPFGALDAKVRKDLRRWLRALH 183
Cdd:PRK10938 152 SEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-210 |
3.73e-09 |
|
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: 58.26 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIP-EGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVlfgGDDVSQLHVRDRNIGFVFQHYalFRHL-----TVAENI 95
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLKRFRGTELQDY--FKKLangeiKVAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFgLESLPK------KQRPSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:COG1245 167 QY-VDLIPKvfkgtvRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1430737237 170 KVRKDLRRWLRALHDEYHfTSIFVTHDqeeaLE----LSDQVVVM 210
Cdd:COG1245 246 YQRLNVARLIRELAEEGK-YVLVVEHD----LAildyLADYVHIL 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-210 |
3.97e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIP-EGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVlfgGDDVSQLHVRDRNIGFVFQHYalFRHL-----TVAENI 95
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKRFRGTELQNY--FKKLyngeiKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFgLESLPKKQRPSKQEIRQRV---AKLLEMIQLPELAK---RYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDA 169
Cdd:PRK13409 167 QY-VDLIPKVFKGKVRELLKKVderGKLDEVVERLGLENildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1430737237 170 KVRKDLRRWLRALHDEYhfTSIFVTHDqeeaLE----LSDQVVVM 210
Cdd:PRK13409 246 RQRLNVARLIRELAEGK--YVLVVEHD----LAvldyLADNVHIA 284
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-173 |
6.01e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 30 LTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHvrDRNIGFVFQHYALFRHLTVAENIAFGleslpkkqrps 109
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFW----------- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737237 110 kQEIRQRVAKLLEMI---QLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRK 173
Cdd:PRK13541 95 -SEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-196 |
1.01e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.63 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIdqinKHFGGFQALKNVSLDipeGQLTALLGPSGSGKTTLLRIIA-GLESSDSGRVLFGGDDVSQLHVRDRnIGFVF 80
Cdd:COG0419 4 RLRL----ENFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEAS-VELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 81 QH----YALFRH------------LTVAENIA--FGLESLPKKQRPSKQEIRQRVAKLLEMIQLPELAKRY--------- 133
Cdd:COG0419 76 EHggkrYRIERRqgefaefleakpSERKEALKrlLGLEIYEELKERLKELEEALESALEELAELQKLKQEIlaqlsgldp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 134 PAQLSGGQKQRVALARALAtqpriLLLDepFGALDAKVRKDLRRWLRALHdeyhftsiFVTHD 196
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-210 |
1.45e-08 |
|
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: 53.52 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 22 SLDIPEGQLTALLGPSGSGKTTLLR---IIAGLESSDSGRVLFGGddvsqlhvRDRNIGFVFQHYALFRHltvaeniafg 98
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVK--------AGCIVAAVSAELIFTRL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 99 leslpkkqrpskqeirqrvakllemiqlpelakrypaQLSGGQKQRVALARALA---TQPRIL-LLDEPFGALDAKVRKD 174
Cdd:cd03227 77 -------------------------------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 1430737237 175 LRRWLRALHDEyHFTSIFVTHDqEEALELSDQVVVM 210
Cdd:cd03227 120 LAEAILEHLVK-GAQVIVITHL-PELAELADKLIHI 153
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-209 |
1.52e-08 |
|
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: 53.73 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 24 DIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQlhvrdrnigfvfqhyalfrhltvaeniafgleslp 103
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY----------------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 104 kkqRPSKqeirqrvakllemiqlpelakrypAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALH 183
Cdd:cd03222 66 ---KPQY------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*.
gi 1430737237 184 DEYHFTSIFVTHDQEEALELSDQVVV 209
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-229 |
3.55e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGD-------------DVSQLHvrdrnigFVFQHYA 84
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALE-------YVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 85 LFRHLTVAENIA------FGLESLPKK-QRPSKQEIRQRVAKLLEMIQLPELAKRYPAQ-LSGGQKQRVALARALATQPR 156
Cdd:PRK10636 90 EYRQLEAQLHDAnerndgHAIATIHGKlDAIDAWTIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 157 ILLLDEPFGALDAKVRKDLRRWLRAlhdeYHFTSIFVTHDQEEALELSDQVVVMSQgqvEQVNSPTGLYARPE 229
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWLKS----YQGTLILISHDRDFLDPIVDKIIHIEQ---QSLFEYTGNYSSFE 235
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-196 |
3.86e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 3 ITIDQINKHFGGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAG-LESSdSGRVlfggddvsQLHVRDRnIGFVFQ 81
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPS-AGNV--------SLDPNER-LGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 82 HYALFRHLTVAENIAFGLESLPKkqrpSKQEiRQRVAKLLEM-----IQLPELAKRYpAQLSG----------------- 139
Cdd:PRK15064 72 DQFAFEEFTVLDTVIMGHTELWE----VKQE-RDRIYALPEMseedgMKVADLEVKF-AEMDGytaearagelllgvgip 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 140 -------------GQKQRVALARALATQPRILLLDEPFGALDAkvrkDLRRWLRALHDEYHFTSIFVTHD 196
Cdd:PRK15064 146 eeqhyglmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDI----NTIRWLEDVLNERNSTMIIISHD 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-215 |
5.95e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 13 GGFQALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLfggddvSQLHVRdrnIGFVFQHYALFRHLTVA 92
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------RSAKVR---MAVFSQHHVDGLDLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 93 EnIAFGLESLPKKqrpSKQEIRqrvAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:PLN03073 591 P-LLYMMRCFPGV---PEQKLR---AHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1430737237 173 KDLRRWLrALhdeYHFTSIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PLN03073 664 EALIQGL-VL---FQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-162 |
7.30e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 17 ALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGddvsqlhvrdrNIGFVFQHYALFRHLTVAENIA 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1430737237 97 F-----GLeslpkkqrpSKQEIRQRVAKLLEMIQLPELAKRYPAQLSGGQKQRVALARALATQPRILLLDE 162
Cdd:PRK13545 108 LkglmmGL---------TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-213 |
1.92e-07 |
|
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: 51.49 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTL----------LRIIAGLesSDSGRVLFGG---DDVSQL--------------- 69
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESL--SAYARQFLGQmdkPDVDSIeglspaiaidqktts 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 70 -HVRDrNIGFVFQHYALFRHLTvaeniafgleslpkkqrpSKQEIRQRVAKLLEmIQLPELA-KRYPAQLSGGQKQRVAL 147
Cdd:cd03270 89 rNPRS-TVGTVTEIYDYLRLLF------------------ARVGIRERLGFLVD-VGLGYLTlSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 148 ARALATQPR--ILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDqEEALELSDQVVVMSQG 213
Cdd:cd03270 149 ATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHD-EDTIRAADHVIDIGPG 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-215 |
4.11e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 4.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1430737237 137 LSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLRRWLRALHDEYHFTsIFVTHDQEEALELSDQVVVMSQGQV 215
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGI-IIISSEMPELLGITDRILVMSNGLV 469
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
14-239 |
9.22e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 50.39 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 14 GFQALKNVSLDIPEGqLTALLGPSGSGKTTLLRIIAGLESSDSGRVL-----FGGDDVSQLHVRdrnIGFVFQHY--ALF 86
Cdd:COG3593 10 NFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfYLGDDPDLPEIE---IELTFGSLlsRLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 87 RHL---TVAENIAFGLESLPKKQRPSKQEIRQRVAKLLEM------------------------IQLPELAKRYPAQLSG 139
Cdd:COG3593 86 RLLlkeEDKEELEEALEELNEELKEALKALNELLSEYLKElldgldlelelsldeledllkslsLRIEDGKELPLDRLGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 140 GQKQRV--ALARALA-----TQPRILLLDEPFGALDAKVRKDLRRWLRALhDEYHFTSIFVTHDQE--EALELsDQVVVM 210
Cdd:COG3593 166 GFQRLIllALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKEL-SEKPNQVIITTHSPHllSEVPL-ENIRRL 243
|
250 260
....*....|....*....|....*....
gi 1430737237 211 SQGQVEQVNSPTGLYARPESRFVFDFLGH 239
Cdd:COG3593 244 RRDSGGTTSTKLIDLDDEDLRKLLRYLGV 272
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-219 |
9.57e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGgddvsqlhvRDRNIGFVFQHYALFrhLTVAENiaf 97
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA---------KGIKLGYFAQHQLEF--LRADES--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 98 gleSLPKKQRPSKQEIRQRVAKLL-----EMIQLPELAKRYpaqlSGGQKQRVALARALATQPRILLLDEPFGALDAKVR 172
Cdd:PRK10636 394 ---PLQHLARLAPQELEQKLRDYLggfgfQGDKVTEETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1430737237 173 KDLRrwlRALHDeYHFTSIFVTHDQEEALELSDQVVVMSQGQVEQVN 219
Cdd:PRK10636 467 QALT---EALID-FEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
86-231 |
1.84e-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: 50.01 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 86 FRHLTVAENIAF--GLESLPKKQ---RPSKQEIRQRVAKLLEmIQLPELA-KRYPAQLSGGQKQRVALARALATQPR--I 157
Cdd:TIGR00630 433 VSELSIREAHEFfnQLTLTPEEKkiaEEVLKEIRERLGFLID-VGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTgvL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 158 LLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDqEEALELSDQVV------------VMSQGQVEQV----NSP 221
Cdd:TIGR00630 512 YVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHD-EDTIRAADYVIdigpgagehggeVVASGTPEEIlanpDSL 589
|
170
....*....|....*..
gi 1430737237 222 TGLY-------ARPESR 231
Cdd:TIGR00630 590 TGQYlsgrkkiEVPAER 606
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
4.32e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.87 E-value: 4.32e-06
10 20
....*....|....*....|....*..
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTL 44
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-163 |
5.66e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLL----------------------RIIAGLESSDS---------GRV------- 59
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkkeqpgnhDRIEGLEHIDKvividqspiGRTprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 60 ----------LF----GG----DDVSQLHVRDRNIGFVFQhyalfrhLTVAENIAFgLESLPKkqrpskqeIRQRVAKL- 120
Cdd:cd03271 91 ytgvfdeireLFcevcKGkrynRETLEVRYKGKSIADVLD-------MTVEEALEF-FENIPK--------IARKLQTLc 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1430737237 121 ---LEMIQLPElakryPA-QLSGGQKQRVALARAL---ATQPRILLLDEP 163
Cdd:cd03271 155 dvgLGYIKLGQ-----PAtTLSGGEAQRIKLAKELskrSTGKTLYILDEP 199
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
3-45 |
5.82e-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: 48.47 E-value: 5.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1430737237 3 ITIDQINKHfggfqALKNVSLDIPEGQLTALLGPSGSGKTTLL 45
Cdd:TIGR00630 614 LTLKGAREN-----NLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-232 |
7.76e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLESSDSGRVLFGGDDVSQLHVRD--RNIGFVFQHYALFRHlTVAENI 95
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 96 AFGLESLPKKQRPSKQEI--RQRVAKLLEMI--QLPELAKRYpaqlSGGQKQRVALARALATQPR-ILLLDEPFGALDAK 170
Cdd:PTZ00243 1405 DPFLEASSAEVWAALELVglRERVASESEGIdsRVLEGGSNY----SVGQRQLMCMARALLKKGSgFILMDEATANIDPA 1480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737237 171 VRKDLRRWLRALHDEYhfTSIFVTHDQEEALELsDQVVVMSQGQVEQVNSPTGLYARPESRF 232
Cdd:PTZ00243 1481 LDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-215 |
1.62e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAG-LESS--DSGRVLFGGDDVSQLhVRDRNIGFVFQHYALFRHLTVAEN 94
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSlkVSGEITYNGYRLNEF-VPRKTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 95 IAFG------------LESLPKKQR-----PSKQE----------------IRQRVAKLL------------EMIQlpel 129
Cdd:PLN03140 260 LDFSarcqgvgtrydlLSELARREKdagifPEAEVdlfmkatamegvksslITDYTLKILgldickdtivgdEMIR---- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 130 akrypaQLSGGQKQRVALARALATQPRILLLDEPFGALDAKVRKDLrrwLRALHDEYHFT--SIFVTHDQ--EEALELSD 205
Cdd:PLN03140 336 ------GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI---VKCLQQIVHLTeaTVLMSLLQpaPETFDLFD 406
|
250
....*....|
gi 1430737237 206 QVVVMSQGQV 215
Cdd:PLN03140 407 DIILLSEGQI 416
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
135-181 |
1.82e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 42.61 E-value: 1.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 135 AQLSGGQKQR---VALARALATQ----------PRILLLDEPFGALDAKVRKDLRRWLRA 181
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| TOBE_3 |
pfam12857 |
TOBE-like domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
285-344 |
2.23e-05 |
|
TOBE-like 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 sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 432835 Cd Length: 59 Bit Score: 41.47 E-value: 2.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 285 PAAKARLPLRIEAISLIGSEVRIELAPEGwqSDEIWEIGMSHAEFARQNPTRGELWYAVP 344
Cdd:pfam12857 1 PPAGGGIPATVRRIRRVGPIVRLELERLD--TGELIEIELPRDRFRELGLAEGETVRLRP 58
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-45 |
3.46e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 3.46e-05
10 20
....*....|....*....|....*...
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTLL 45
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-122 |
3.90e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.99 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 2 SITIdqinKHFGGFqalKNVSLDIPEG-QLTALLGPSGSGKTTLLRIIA-GLESSDSGRVLFGGDDVSQLHVRDRNIGFV 79
Cdd:COG3950 5 SLTI----ENFRGF---EDLEIDFDNPpRLTVLVGENGSGKTTLLEAIAlALSGLLSRLDDVKFRKLLIRNGEFGDSAKL 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1430737237 80 FQHYALFRHLTVAEniafglESLPKKQRPSKQEIRQRVAKLLE 122
Cdd:COG3950 78 ILYYGTSRLLLDGP------LKKLERLKEEYFSRLDGYDSLLD 114
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
3.96e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 3.96e-05
10 20
....*....|....*....|....*..
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTL 44
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-44 |
1.82e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 1.82e-04
10 20
....*....|....*....|....*..
gi 1430737237 18 LKNVSLDIPEGQLTALLGPSGSGKTTL 44
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
83-208 |
1.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 83 YALFRHLTVAENIAFgLESLPKKQrPSKQEI----RQRVAKLLEMiQLPELA-KRYPAQLSGGQKQRVALARALATQPR- 156
Cdd:PRK00635 421 FAEFQQMSLQELFIF-LSQLPSKS-LSIEEVlqglKSRLSILIDL-GLPYLTpERALATLSGGEQERTALAKHLGAELIg 497
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1430737237 157 -ILLLDEPFGALDAKVRKDLRRWLRALHDEYHfTSIFVTHDqEEALELSDQVV 208
Cdd:PRK00635 498 iTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRII 548
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-44 |
1.49e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 1.49e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
2-45 |
1.58e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1430737237 2 SITIDQINKHfggfqALKNVSLDIPEGQLTALLGPSGSGKTTLL 45
Cdd:PRK00635 600 TLTLSKATKH-----NLKDLTISLPLGRLTVVTGVSGSGKSSLI 638
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-163 |
1.72e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 16 QALKNVSLDIPEGQLTALLGPSGSGKTTLLRIIAGLE--SSDSGRVLFGGDDVSQLHVR---DRNIGFVFQ---HYALFR 87
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSdaiDAGLAYVTEdrkGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737237 88 HLTVAENIAfgLESLPK----------KQRPSKQEIRQRVAkllemIQLPELAKRYpAQLSGGQKQRVALARALATQPRI 157
Cdd:NF040905 354 IDDIKRNIT--LANLGKvsrrgvidenEEIKVAEEYRKKMN-----IKTPSVFQKV-GNLSGGNQQKVVLSKWLFTDPDV 425
|
....*.
gi 1430737237 158 LLLDEP 163
Cdd:NF040905 426 LILDEP 431
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-281 |
3.95e-03 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 34.73 E-value: 3.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1430737237 241 NVLSGLVKGQKLVQGDAWVSLPGI--RQDQEAQLYLRPHEVQL 281
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPELagAEGSEVVAYVRPHDLEI 43
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-188 |
3.96e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 3.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737237 136 QLSGGQKQRVALARALATQ-----PrILLLDEPFGALDAKVRKDLRRWLRALHDEYHF 188
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALDAQYRTAVANMIKELSDGAQF 214
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
14-48 |
7.87e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.09 E-value: 7.87e-03
10 20 30
....*....|....*....|....*....|....*
gi 1430737237 14 GFQALKNVSLDIPEGqLTALLGPSGSGKTTLLRII 48
Cdd:pfam13476 5 NFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-45 |
8.52e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 8.52e-03
10 20 30
....*....|....*....|....*....|...
gi 1430737237 13 GGFQalkNVSLDIPEGQLTALLGPSGSGKTTLL 45
Cdd:pfam13555 10 GTFD---GHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| |
