|
Name |
Accession |
Description |
Interval |
E-value |
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-377 |
0e+00 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 839.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 1 MNDVMPRPQAKAPKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
Cdd:PRK11607 1 MNDAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 81 VDLARVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVAL 160
Cdd:PRK11607 81 VDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 241 PTTRYSAEFIGSVNVFEGLVKERLEDGLVLSSPGLMHPLKVDPDASVVDNVPVWVALRPEKIMLCDEPPADGYNFAVGEV 320
Cdd:PRK11607 241 PTTRYSAEFIGSVNVFEGVLKERQEDGLVIDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPADGCNFAVGEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 321 IHIAYLGDLSIYHVRLQSGQMISAQLQNEHRHRKGTPTWGDEVRLCWDADSCVVLTV 377
Cdd:PRK11607 321 IHIAYLGDLSIYHVRLKSGQMISAQLQNAHRYRKGLPTWGDEVRLCWEADSCVVLTV 377
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-376 |
0e+00 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 552.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMM 96
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 257 EGLVKERleDGLVLSSPGlmHPLKVDPDASVVDNVPVWVALRPEKIMLCDEPPADGYNfavGEVIHIAYLGDLSIYHVRL 336
Cdd:COG3842 243 PGTVLGD--EGGGVRTGG--RTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPENGLP---GTVEDVVFLGSHVRYRVRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1616137381 337 QSGQMISAQLQNEHRHRkgtPTWGDEVRLCWDADSCVVLT 376
Cdd:COG3842 316 GDGQELVVRVPNRAALP---LEPGDRVGLSWDPEDVVVLP 352
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
50-375 |
0e+00 |
|
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: 518.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 50 LLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITAR 129
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 130 VQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHD 209
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 210 QEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGLVKERLEDGLVLSSpGLMHPLKVDPDASVVD 289
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAG-VEGRRCDIYTDVPVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 290 NVPVWVALRPEKIMLCDEPPADGYNFAVGEVIHIAYLGDLSIYHVRLQSGQ--MISAQLQNEHRHRKgtPTWGDEVRLCW 367
Cdd:TIGR01187 240 DQPLHVVLRPEKIVIEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQkvLVSEFFNEDDPHMS--PSIGDRVGLTW 317
|
....*...
gi 1616137381 368 DADSCVVL 375
Cdd:TIGR01187 318 HPGSEVVL 325
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-374 |
9.72e-150 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 426.80 E-value: 9.72e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:COG3839 84 YALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFE 257
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSppMNLLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 258 GlvkERLEDGLVLSSpglmHPLKVDPDASVVDNVPVWVALRPEKIMLCDEPPADgynfAVGEVIHIAYLGDLSIYHVRLQ 337
Cdd:COG3839 244 G---TVEGGGVRLGG----VRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGG----LEATVEVVEPLGSETLVHVRLG 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 1616137381 338 sGQMISAQLQNEHRHRKgtptwGDEVRLCWDADSCVV 374
Cdd:COG3839 313 -GQELVARVPGDTRLRP-----GDTVRLAFDPERLHL 343
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-369 |
1.67e-138 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 397.98 E-value: 1.67e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-ARVPPYQRPINMMFQ 98
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 259 LVK-ERLE-DGLVLsspglmhplkvdPDASVVDNVPVWVALRPEKIMLCDEPpaDGYNFAVGEVIHIAYLGDLSIYHVRL 336
Cdd:COG1118 243 RVIgGQLEaDGLTL------------PVAEPLPDGPAVAGVRPHDIEVSREP--EGENTFPATVARVSELGPEVRVELKL 308
|
330 340 350
....*....|....*....|....*....|....*
gi 1616137381 337 Q--SGQMISAQLQNEHRHRKGtPTWGDEVRLCWDA 369
Cdd:COG1118 309 EdgEGQPLEAEVTKEAWAELG-LAPGDPVYLRPRP 342
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-344 |
6.97e-138 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 397.40 E-value: 6.97e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMM 96
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 257 EGLVKERLEDGLVLSS-PGLMHPLKVDPDASVVDNVPvwVALRPEKI---MLCDEPPADGYnfaVGEVIHIAYLG---DL 329
Cdd:PRK09452 252 DATVIERLDEQRVRANvEGRECNIYVNFAVEPGQKLH--VLLRPEDLrveEINDDEHAEGL---IGYVRERNYKGmtlDS 326
|
330
....*....|....*
gi 1616137381 330 SIyhvRLQSGQMISA 344
Cdd:PRK09452 327 VV---ELENGKMVMV 338
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-251 |
5.31e-137 |
|
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: 389.67 E-value: 5.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
18-355 |
5.00e-124 |
|
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: 361.66 E-value: 5.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMF 97
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:TIGR03265 83 QSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
Cdd:TIGR03265 163 SALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 258 GlvkERLEDGLVLSSPGLMHPLKVDPDASvvdnVPVWVALRPEKIMLcdEPPADGYNFAVGEVIHIAYLGdlSIYHVRLQ 337
Cdd:TIGR03265 243 G---TRGGGSRARVGGLTLACAPGLAQPG----ASVRLAVRPEDIRV--SPAGNAANLLLARVEDMEFLG--AFYRLRLR 311
|
330 340
....*....|....*....|..
gi 1616137381 338 ----SGQMISAQLQNEHRHRKG 355
Cdd:TIGR03265 312 leglPGQALVADVSASEVERLG 333
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-232 |
7.36e-121 |
|
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: 347.97 E-value: 7.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-252 |
4.97e-103 |
|
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: 303.88 E-value: 4.97e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLK----QDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-249 |
6.29e-103 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 304.32 E-value: 6.29e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPyqrPI 93
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvqiGEPEEIYE-------HPTTRYS 246
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP----GRIVEEIDvdlprprDRELRTS 238
|
...
gi 1616137381 247 AEF 249
Cdd:COG1116 239 PEF 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-359 |
1.05e-101 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 304.84 E-value: 1.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQ 98
Cdd:PRK11650 4 LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSpaMNLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 257 EGLVkerLEDGLVLSSPGLMhPLKVDPDASVVDNVPVWVALRPEKIMLCDEPPAdgynfAVGEVIHIAYLGDLSIYHVRL 336
Cdd:PRK11650 244 DGRV---SADGAAFELAGGI-ALPLGGGYRQYAGRKLTLGIRPEHIALSSAEGG-----VPLTVDTVELLGADNLAHGRW 314
|
330 340
....*....|....*....|...
gi 1616137381 337 qSGQMISAQLQNEHRHRKGTPTW 359
Cdd:PRK11650 315 -GGQPLVVRLPHQERPAAGSTLW 336
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-232 |
1.48e-101 |
|
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: 299.17 E-value: 1.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-255 |
2.49e-99 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 294.40 E-value: 2.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-225 |
1.16e-98 |
|
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: 292.07 E-value: 1.16e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDG----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPyqrPINM 95
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1616137381 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-350 |
2.07e-94 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 285.85 E-value: 2.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGl 259
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPA- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 260 vkeRLEDGLVlSSPGLMHPLKvDPDASVVDNVPVWVALRPEKIMLCDEppadGYNFAVGEVIHIAYLGdlSIYHVRLQ-S 338
Cdd:PRK11432 246 ---TLSGDYV-DIYGYRLPRP-AAFAFNLPDGECTVGVRPEAITLSEQ----GEESQRCTIKHVAYMG--PQYEVTVDwH 314
|
330
....*....|..
gi 1616137381 339 GQMISAQLQNEH 350
Cdd:PRK11432 315 GQELLLQVNATQ 326
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-252 |
2.26e-92 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 278.90 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMMF 97
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHM--QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-311 |
8.47e-90 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 274.27 E-value: 8.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLK----QDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 256 FEGLVKerledGLVLSSPGLMHPLKVDPdasvVDNVPVWVALRPEKIMLCDEPPAD 311
Cdd:PRK10851 243 LQGTIR-----GGQFHVGAHRWPLGYTP----AYQGPVDLFLRPWEVDISRRTSLD 289
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-252 |
4.93e-89 |
|
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: 268.40 E-value: 4.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMM 96
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHM--QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-329 |
9.03e-88 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 268.87 E-value: 9.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQ 98
Cdd:NF040840 1 MIRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEG 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 259 LVKERlEDGLVLSSPGlmhpLKVDPDASVVDnvPVWVALRPEKIMLCDEP-PADGYNFAVGEVIHIAYLGDL 329
Cdd:NF040840 240 VAEKG-GEGTILDTGN----IKIELPEEKKG--KVRIGIRPEDITISTEKvKTSARNEFKGKVEEIEDLGPL 304
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-255 |
7.70e-87 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 267.74 E-value: 7.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFdGQH-------------------------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP 71
Cdd:COG4175 1 MPKIEVRNLYKIF-GKRperalklldqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 72 TAGQIMLDGVDLARVPPYQ------RPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKR 145
Cdd:COG4175 80 TAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 146 KPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKD 239
|
250 260 270
....*....|....*....|....*....|
gi 1616137381 226 GKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:COG4175 240 GRIVQIGTPEEILTNPANDYVADFVEDVDR 269
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-255 |
2.45e-86 |
|
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: 261.12 E-value: 2.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
22-377 |
2.45e-86 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 265.70 E-value: 2.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP--TAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:TIGR03258 8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKRGLALLFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:TIGR03258 88 YALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 180 LDKKLRDRMQLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG 258
Cdd:TIGR03258 168 LDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 259 LVKERLE-DGLVLSSPGLMHPLKV-DPDASVVDNVpvwVALRPEKIMLCDEPPADGYNFAVGEVIHiaYLGDLSIYHVRL 336
Cdd:TIGR03258 248 IALGITEaPGLVDVSCGGAVIFAFgDGRHDGRDKL---ACIRPEHLALTPRPAGEGRFHATIASVE--WHGAALHLLCDL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1616137381 337 QSGQMISAqLQNEHRHRKGTPTWGDEVRLCWDADSCVVLTV 377
Cdd:TIGR03258 323 DAACDEPM-LVTMLRGRGPAPERGAKLALDCEADDAVLIEP 362
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-252 |
9.45e-84 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 259.19 E-value: 9.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQSYA 101
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 102 LFPHMTVEQNIAFGLKQDRLPKAEITARVQ---EMLALVHMQEfakRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-250 |
1.36e-83 |
|
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: 254.13 E-value: 1.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ-----R 91
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQNIAFGLKQ-DRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 171 LLLDEP--------MGALD---KKLRDRMqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY- 238
Cdd:COG1127 163 LLYDEPtagldpitSAVIDeliRELRDEL-----------GLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLa 231
|
250
....*....|...
gi 1616137381 239 -EHPTTRysaEFI 250
Cdd:COG1127 232 sDDPWVR---QFL 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-253 |
6.68e-82 |
|
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: 259.07 E-value: 6.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLTKSF-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 78 LDGVDLARVP-----PYQRPINMMFQ--SYALFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQ-EFAKRKPR 148
Cdd:COG1123 324 FDGKDLTKLSrrslrELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPpDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLrdlqRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
250 260
....*....|....*....|....*....
gi 1616137381 225 RGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:COG1123 480 DGRIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-255 |
1.81e-79 |
|
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: 244.86 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ------RPINMMFQSYALFPHMT 107
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 188 MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDR 266
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-253 |
2.41e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 243.36 E-value: 2.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----ARVPPYQRPIN 94
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYALFPHMTVEQNIAFGLKQDR-LPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKkMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 174 DEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:COG1126 161 DEPTSALDPELVG----EVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
...
gi 1616137381 251 GSV 253
Cdd:COG1126 237 SKV 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
20-251 |
1.94e-78 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 240.81 E-value: 1.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAvdDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA-KRPkLLLLDEPMG 178
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
27-274 |
2.47e-78 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 245.15 E-value: 2.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 27 KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ------RPINMMFQSY 100
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 ALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGL- 259
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFd 240
|
250
....*....|....*...
gi 1616137381 260 ---VKERLEDGLVLSSPG 274
Cdd:TIGR01186 241 aerIAQRMNTGPITKTAD 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-253 |
4.55e-78 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 243.45 E-value: 4.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ----- 90
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 171 LLLDEPMGALD-----------KKLRDRMqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:COG1135 162 LLCDEATSALDpettrsildllKDINREL-----------GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|....
gi 1616137381 240 HPTTRYSAEFIGSV 253
Cdd:COG1135 231 NPQSELTRRFLPTV 244
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-229 |
1.91e-77 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 238.02 E-value: 1.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSF-DGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP 92
Cdd:COG1136 2 SPLLELRNLTKSYgTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 ------INMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAK 166
Cdd:COG1136 82 rlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 167 RPKLLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDqEEAMTMAGRIAIMNRGKFV 229
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGE----EVLELLRELnrelGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-237 |
2.11e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 238.42 E-value: 2.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRPINMMFQ 98
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAF--GLKqdRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLY--GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 177 MGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-227 |
3.23e-77 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 235.93 E-value: 3.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR----VPPYQRPINM 95
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHMTVEQNIAFGlkqdrlpkaeitarvqemlalvhmqefakrkprqLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-241 |
7.58e-75 |
|
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: 231.45 E-value: 7.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMM 96
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQS--YALFpHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:COG1122 160 EPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-258 |
3.94e-73 |
|
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: 227.76 E-value: 3.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRP 92
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSY--ALFPHMTVEQNIAFGLKQDRLPkaEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSLAKRPK 169
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 170 LLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
Cdd:COG1124 159 LLLLDEPTSALDVS----VQAEILNLLKDLreerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
250
....*....|...
gi 1616137381 246 SAEFIGSVNVFEG 258
Cdd:COG1124 235 TRELLAASLAFER 247
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-237 |
5.34e-73 |
|
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: 227.00 E-value: 5.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ-----RPIN 94
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYALFPHMTVEQNIAFGLKQD-RLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-223 |
8.42e-72 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 224.74 E-value: 8.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDG----QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARvPPYQRPI 93
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 nmMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1616137381 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-232 |
1.08e-71 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 222.94 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIyKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------ARVPPYQRPINMMFQSYALFPHMTVEQ 110
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 111 NIAFGLKqdRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQL 190
Cdd:cd03297 95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1616137381 191 EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-227 |
1.53e-71 |
|
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: 222.75 E-value: 1.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP--- 92
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 ---INMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPK 169
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 170 LLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDQEEAMtMAGRIAIMNRGK 227
Cdd:cd03255 161 IILADEPTGNLDSETGK----EVMELLRELnkeaGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-241 |
3.15e-71 |
|
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: 222.46 E-value: 3.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-----Y 89
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPK 169
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-236 |
7.12e-71 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 221.08 E-value: 7.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR-----VPPYQRPI 93
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 174 DEPMGALDKKLRdrmqLEVVDILE---RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:COG2884 162 DEPTGNLDPETS----WEIMELLEeinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-244 |
4.88e-70 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 222.68 E-value: 4.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR 85
Cdd:COG4608 5 EPLLEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 VP-----PYQRPINMMFQ-SYA-LFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQ 156
Cdd:COG4608 85 LSgrelrPLRRRMQMVFQdPYAsLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 157 RVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILE----RVGVTCVMVTHDQeeAMT--MAGRIAIMNRGKFVQ 230
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVS----IQAQVLNLLEdlqdELGLTYLFISHDL--SVVrhISDRVAVMYLGKIVE 238
|
250
....*....|....*..
gi 1616137381 231 IGEPEEIYE---HPTTR 244
Cdd:COG4608 239 IAPRDELYArplHPYTQ 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-241 |
6.87e-69 |
|
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: 217.21 E-value: 6.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---I 93
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIA---------------FGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRV 158
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
...
gi 1616137381 239 EHP 241
Cdd:COG0411 242 ADP 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-311 |
7.11e-68 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 218.05 E-value: 7.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG---VDLAR---VPPYQRPINMMFQSYALFPHMTVEQ 110
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 111 NIAFGLKqdRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmql 190
Cdd:COG4148 97 NLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 191 EVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGLVKERLED 266
Cdd:COG4148 171 EILPYLERLrdelDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPD 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1616137381 267 -GLV-LSSPGlmHPLKVdPDASVVDNVPVWVALRPEKIMLCDEPPAD 311
Cdd:COG4148 251 yGLTrLALGG--GRLWV-PRLDLPPGTRVRVRIRARDVSLALEPPEG 294
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-232 |
2.82e-67 |
|
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: 211.98 E-value: 2.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP-----PY 89
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QRPINMMFQSY--ALFPHMTVEQNIAFGLK--QDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSL 164
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
20-227 |
1.04e-66 |
|
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: 210.08 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----ARVPPYQRPINM 95
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHMTVEQNIAFGLKQDR-LPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKgMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 175 EPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03262 161 EPTSALDPELVG----EVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-220 |
2.24e-65 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 206.56 E-value: 2.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVDLARVPPYQRPINMM 96
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKqDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1616137381 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRI 220
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRV 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-241 |
2.40e-65 |
|
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: 207.29 E-value: 2.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---INMM 96
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNI----------AFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAK 166
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 167 RPKLLLLDEPMGALDKKLRDRMqlevVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEEL----AELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-227 |
6.31e-65 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 205.39 E-value: 6.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMM 96
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQsyalFP-HM----TVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03225 157 LLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
21-253 |
7.66e-65 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 209.66 E-value: 7.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ-----R 91
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 172 LLDEPMGALDKKLRDRMqLEVV-DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK11153 163 LCDEATSALDPATTRSI-LELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
...
gi 1616137381 251 GSV 253
Cdd:PRK11153 242 QST 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
35-244 |
1.80e-64 |
|
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: 205.01 E-value: 1.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRpinMMFQSYALFPHMTVEQNIAF 114
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 115 GLKQDR--LPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:TIGR01184 78 AVDRVLpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI-YEHPTTR 244
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-241 |
2.76e-63 |
|
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: 210.53 E-value: 2.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTA---GQIMLDGVDLARVPPYQR 91
Cdd:COG1123 2 TPLLEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 P--INMMFQS--YALFPhMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKR 167
Cdd:COG1123 82 GrrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-237 |
4.77e-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: 4.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMM 96
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFG----LKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 173 LDEPMGALDkkLrdRMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1120 161 LDEPTSHLD--L--AHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-241 |
5.51e-63 |
|
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: 204.13 E-value: 5.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVDLARVPPYQ- 90
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 -----RPINMMFQ-SY-ALFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHM---QEFAKRKPRQLSGGQRQRVA 159
Cdd:COG0444 81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQAQILNLLkdlqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*.
gi 1616137381 236 EIYEHP 241
Cdd:COG0444 237 ELFENP 242
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-232 |
6.92e-63 |
|
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: 200.41 E-value: 6.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 25 LTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQSYALF 103
Cdd:cd03298 3 LDKIRFSyGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 104 PHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:cd03298 83 AHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1616137381 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-239 |
9.68e-63 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 200.85 E-value: 9.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRPINMMF 97
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 178 GALDkkLRDRMQLevVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:COG4555 161 NGLD--VMARRLL--REILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-240 |
1.07e-60 |
|
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: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA---RVPPYQRPIN 94
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeeNLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSyalfPH-----MTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPK 169
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 170 LLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:TIGR04520 157 IIILDEATSMLDPKGRK----EVLETIRKLnkeeGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
18-237 |
1.11e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 195.66 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-----YQR 91
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQNIAFGlkqdRL-------------PKAEItARVQEMLALVHMQEFAKRKPRQLSGGQRQRV 158
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAG----RLgrtstwrsllglfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-228 |
4.53e-60 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 192.72 E-value: 4.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPINMMF 97
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPhMTVEQNIA--FGLKQDRLPKAeitaRVQEMLALVHMQE-FAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:COG4619 81 QEPALWG-GTVRDNLPfpFQLRERKFDRE----RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-228 |
5.86e-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: 191.46 E-value: 5.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP-INMMFQ 98
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIafglkqdrlpkaeitarvqemlalvhmqefakrkprQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:cd03230 125 GLDPESRREF-WELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-237 |
1.46e-59 |
|
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: 192.40 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDLA--RVPPYQ-- 90
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYdlDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPINMMFQSYALFPhMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQEFAKRK--PRQLSGGQRQRVALARSLAKR 167
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 168 PKLLLLDEPMGALD-----------KKLRDRMqlevvdilervgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:cd03260 160 PEVLLLDEPTSALDpistakieeliAELKKEY-------------TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1616137381 237 I 237
Cdd:cd03260 227 I 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-242 |
7.17e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.07 E-value: 7.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR-------VPpy 89
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigyVP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QRpinmmFQSYALFPhMTVEQNIAFGLKQD----RLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA 165
Cdd:COG1121 82 QR-----AEVDWDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 166 KRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKfVQIGEPEEIYEHPT 242
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAA----TEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEEVLTPEN 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-253 |
1.30e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 190.30 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----ARVPPYQRPI 93
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVlHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDR-LPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
Cdd:PRK09493 160 FDEPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQH 238
|
.
gi 1616137381 253 V 253
Cdd:PRK09493 239 V 239
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-237 |
3.05e-58 |
|
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: 188.48 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP-INMM 96
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAF--GLKqdRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 175 EPMGALDKKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03263 159 EPTSGLDPASRR----AIWDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-227 |
3.16e-58 |
|
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: 188.23 E-value: 3.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR-----VPPYQRP 92
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 173 LDEPMGALDkklrDRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:TIGR02673 161 ADEPTGNLD----PDLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
39-237 |
1.47e-57 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 187.10 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQ 118
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 119 DRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILER 198
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1616137381 199 VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-240 |
4.54e-57 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 187.53 E-value: 4.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--ARVPPYQRPI 93
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSY-ALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 173 LDEPMGALDKKLRDRMqLEVVDIL-ERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13635 164 LDEATSMLDPRGRREV-LETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-226 |
5.80e-57 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 186.44 E-value: 5.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARvPPYQRPInmMFQ 98
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-275 |
4.84e-56 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 188.70 E-value: 4.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ------RPINMMFQSYALFPHMT 107
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 188 MQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGL----VKER 263
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFsakdIARR 282
|
250
....*....|..
gi 1616137381 264 LEDGLVLSSPGL 275
Cdd:PRK10070 283 TPNGLIRKTPGF 294
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-240 |
1.22e-55 |
|
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: 182.77 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-----YQRPI 93
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDR---------LPKAEItARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSL 164
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 165 AKRPKLLLLDEPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:cd03256 160 MQQPKLILADEPVASLDPASsRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-242 |
1.57e-55 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 183.42 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA-----RVPPYQRPINMMFQ--SYALFp 104
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQfpEHQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 105 HMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:TIGR04521 97 EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
39-232 |
2.94e-55 |
|
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: 180.83 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKq 118
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 119 drlPKAEITARVQEMLALVHMQ----EFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVD 194
Cdd:TIGR01277 97 ---PGLKLNAEQQEKVVDAAQQvgiaDYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1616137381 195 ILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-227 |
4.62e-54 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 179.10 E-value: 4.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLeIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVppyQRPINMM 96
Cdd:PRK11247 11 TPLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA---REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKQDRLPKAEitarvqEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-237 |
9.16e-54 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 184.84 E-value: 9.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP---YQRPI 93
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGlkqdRLPK-------AEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAK 166
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLG----REPRrgglidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1129 158 DARVLILDEPTASLTEREVERL-FRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-245 |
3.10e-53 |
|
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: 184.12 E-value: 3.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 7 RPQAKAPKALTPLLEIRNLTKSFDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQ 75
Cdd:COG4172 263 GDPRPVPPDAPPLLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 76 IMLDGVDLARVP-----PYQRPINMMFQS-YA-LFPHMTVEQNIAFGLK--QDRLPKAEITARVQEMLALVHMQ-EFAKR 145
Cdd:COG4172 342 IRFDGQDLDGLSrralrPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDpAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 146 KPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIA 221
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQAQILDLLrdlqREHGLAYLFISHDLAVVRALAHRVM 497
|
250 260
....*....|....*....|....
gi 1616137381 222 IMNRGKFVQIGEPEEIYEHPTTRY 245
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDAPQHPY 521
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-250 |
9.74e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 175.20 E-value: 9.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--------VDLARVPPYQR 91
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQN-IAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 171 LLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpEEIYEHPTTRYSA 247
Cdd:COG4161 163 LLFDEPTAALDPEITA----QVVEIireLSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFA 237
|
...
gi 1616137381 248 EFI 250
Cdd:COG4161 238 HYL 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-240 |
1.01e-52 |
|
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: 185.81 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 1 MNDVM-------PRPQAKAPKALTPLLEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP 71
Cdd:COG2274 448 LDDILdlppereEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 72 TAGQIMLDGVDLARVPP--YQRPINMMFQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKP- 147
Cdd:COG2274 528 TSGRILIDGIDLRQIDPasLRRQIGVVLQDVFLF-SGTIRENITLG-------DPDATdEEIIEAARLAGLHDFIEALPm 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 ----------RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV--GVTCVMVTHDqEEAMT 215
Cdd:COG2274 600 gydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI----ILENLRRLlkGRTVIIIAHR-LSTIR 674
|
250 260
....*....|....*....|....*
gi 1616137381 216 MAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
13-220 |
1.04e-52 |
|
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: 174.54 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 13 PKALTPLLEIRNLTKSF-DGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----- 83
Cdd:COG4181 2 SSSSAPIIELRGLTKTVgTGAGELtilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 84 ---ARVppyqRPINM--MFQSYALFPHMTVEQNIAFGLKQDRLPKAEitARVQEMLALVHMQEFAKRKPRQLSGGQRQRV 158
Cdd:COG4181 82 darARL----RARHVgfVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDIL----ERVGVTCVMVTHDQEEA------MTM-AGRI 220
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQ----IIDLLfelnRERGTTLVLVTHDPALAarcdrvLRLrAGRL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
35-176 |
1.66e-52 |
|
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: 171.29 E-value: 1.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR--VPPYQRPINMMFQSYALFPHMTVEQNI 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 113 AFGLKQDRLPKAEITARVQEMLALVHMQEFAKRK----PRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-244 |
2.80e-52 |
|
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: 173.50 E-value: 2.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---INMM 96
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 177 MGALDKKLRDRMQlEVVDILERVGVTcVMVT-HDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:cd03218 161 FAGVDPIAVQDIQ-KIIKILKDRGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-220 |
3.44e-52 |
|
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: 172.41 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP------YQRPINM 95
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1616137381 176 PMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAmTMAGRI 220
Cdd:TIGR03608 161 PTGSLDPKNRD----EVLDLLLELndeGKTIIIVTHDPEVA-KQADRV 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-237 |
3.50e-52 |
|
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: 172.94 E-value: 3.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP-PYQRPINMMFQ 98
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-232 |
1.00e-51 |
|
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: 171.61 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRPINMMFQ 98
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQkLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 179 ALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-232 |
1.31e-51 |
|
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: 169.92 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRpinmmfqsy 100
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 AlfphmtveQNIAFglkqdrLPKAeitarvqemLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:cd03214 72 A--------RKIAY------VPQA---------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 181 DKKlrdrMQLEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03214 129 DIA----HQIELLELLRRlareRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-237 |
1.77e-51 |
|
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: 171.08 E-value: 1.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---INMM 96
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKqdRLPKAEITARVQEMLALV-HMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 176 PMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03224 159 PSEGLAPKIVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-227 |
3.48e-51 |
|
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: 170.28 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA-----RVPPYQRPI 93
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 174 DEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03292 161 DEPTGNLDPD----TTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-213 |
3.82e-51 |
|
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: 169.58 E-value: 3.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRPINMM 96
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKQDRLPKAEitARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1616137381 177 MGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEA 213
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-240 |
4.24e-51 |
|
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: 170.94 E-value: 4.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP-----PYQRP 92
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSYALFPHMTVEQNI---AFGLKQ------DRLPKAEiTARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARS 163
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKPtwrsllGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 164 LAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQ----VMDYLKRInkedGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
.
gi 1616137381 240 H 240
Cdd:TIGR02315 236 E 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-270 |
5.61e-51 |
|
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: 174.14 E-value: 5.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR------VPPYQRPINMMFQSYALFPHMTVEQ 110
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 111 NIAFGLKQDRLPKAEIT-ARVQEMLALVHMQEfakRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmq 189
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 190 lEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY----SAEFIGSVNVFE---- 257
Cdd:TIGR02142 169 -EILPYLERLhaefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWlareDQGSLIEGVVAEhdqh 247
|
250
....*....|....
gi 1616137381 258 -GLVKERLEDGLVL 270
Cdd:TIGR02142 248 yGLTALRLGGGHLW 261
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-244 |
6.53e-51 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 170.21 E-value: 6.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQR------ 91
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 --PinmmfQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPK 169
Cdd:COG1137 82 ylP-----QEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 170 LLLLDEPMGALD-----------KKLRDRmqlevvDIlervGvtcVMVT-HDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1137 157 FILLDEPFAGVDpiavadiqkiiRHLKER------GI----G---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
....*..
gi 1616137381 238 YEHPTTR 244
Cdd:COG1137 224 LNNPLVR 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-244 |
8.09e-51 |
|
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: 169.78 E-value: 8.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---I 93
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQdRLPKAEITARVQEMLALV-HMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYA-RRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 173 LDEP-MGaLDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:COG0410 160 LDEPsLG-LAPLIVE----EIFEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-229 |
1.78e-50 |
|
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: 168.16 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPINMMFQS 99
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGLKQDRLPKaeitARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 180 LD----KKLRDRMQLevvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03268 157 LDpdgiKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-250 |
2.68e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 168.65 E-value: 2.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLARVP------PYQR 91
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPsdkairELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQN-IAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 171 LLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpEEIYEHPTTRYSA 247
Cdd:PRK11124 163 LLFDEPTAALDPEITA----QIVSIireLAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFK 237
|
...
gi 1616137381 248 EFI 250
Cdd:PRK11124 238 NYL 240
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
3.41e-50 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 169.14 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMM 96
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYAL-FPhMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA-------KRP 168
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 169 KLLLLDEPMGALDKKLrdrmQLEVVDIL-----ERVGVTCVMvtHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:COG4559 160 RWLFLDEPTSALDLAH----QHAVLRLArqlarRGGGVVAVL--HDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-298 |
3.35e-49 |
|
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: 173.33 E-value: 3.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDG----QHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVDLARVPP 88
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 YQ------RPINMMFQ--SYALFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQEFAKR---KPRQLSGGQRQ 156
Cdd:COG4172 84 RElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 157 RVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDqeeaMT----MAGRIAIMNRGKF 228
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTV----QAQILDLLkdlqRELGMALLLITHD----LGvvrrFADRVAVMRQGEI 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 229 VQIGEPEEIYEHPTTRYSAEfigsvnvfeglvkerledgLVLSSPGlMHPLKVDPDASV---VDNVPVWVALR 298
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRK-------------------LLAAEPR-GDPRPVPPDAPPlleARDLKVWFPIK 288
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-229 |
3.96e-49 |
|
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: 162.98 E-value: 3.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlarvppyqRPINmmFQS 99
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------KEVS--FAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 yalfphmtveqniafglkqdrlPKAEITARVqemlALVHmqefakrkprQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:cd03216 69 ----------------------PRDARRAGI----AMVY----------QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1616137381 180 LDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03216 113 LTPAEVERL-FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-252 |
5.81e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 165.74 E-value: 5.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 13 PKALTPLLEIRNLTKSFdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA------- 84
Cdd:COG4598 2 TDTAPPALEVRDLHKSF-GDLEVlKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 85 -RVPPYQRPIN-------MMFQSYALFPHMTVEQNIAFG----LKQdrlPKAEITARVQEMLALVHMQEFAKRKPRQLSG 152
Cdd:COG4598 81 eLVPADRRQLQrirtrlgMVFQSFNLWSHMTVLENVIEApvhvLGR---PKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEV-LKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
250 260
....*....|....*....|
gi 1616137381 233 EPEEIYEHPTTRYSAEFIGS 252
Cdd:COG4598 237 PPAEVFGNPKSERLRQFLSS 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-230 |
7.78e-49 |
|
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: 165.75 E-value: 7.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTK-----SFDGQHA----VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP- 88
Cdd:TIGR02769 2 LLEVRDVTHtyrtgGLFGAKQrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 ----YQRPINMMFQ-SYALF-PHMTVEQNIAFGLKQ-DRLPKAEITARVQEMLALVHMQ-EFAKRKPRQLSGGQRQRVAL 160
Cdd:TIGR02769 82 qrraFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 161 ARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVL----QAVILELLRklqqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-228 |
1.86e-48 |
|
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: 163.09 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYqrpINMMFQSY 100
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 AL---FPhMTVEQNIAFGLKQD----RLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 174 DEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:cd03235 157 DEPFAGVDPK----TQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-240 |
1.97e-48 |
|
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: 171.86 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
Cdd:COG4988 320 PAAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 82 DLARVPP--YQRPINMMFQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKP----------- 147
Cdd:COG4988 400 DLSDLDPasWRRQIAWVPQNPYLF-AGTIRENLRLG-------RPDASdEELEAALEAAGLDEFVAALPdgldtplgegg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLE--VVDILERV--GVTCVMVTHDqEEAMTMAGRIAIM 223
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD------AETEaeILQALRRLakGRTVILITHR-LALLAQADRILVL 544
|
250
....*....|....*..
gi 1616137381 224 NRGKFVQIGEPEEIYEH 240
Cdd:COG4988 545 DDGRIVEQGTHEELLAK 561
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-270 |
2.53e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 165.28 E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP-------PYQRp 92
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 inmmfqsyALFPHMTV-EQNIAFG-LKQdrLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:COG4152 81 --------GLYPKMKVgEQLVYLArLKG--LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 171 LLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE-HPTTRYSAEF 249
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRqFGRNTLRLEA 229
|
250 260
....*....|....*....|....*
gi 1616137381 250 IGSVNVFEGL----VKERLEDGLVL 270
Cdd:COG4152 230 DGDAGWLRALpgvtVVEEDGDGAEL 254
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-227 |
4.23e-48 |
|
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: 160.10 E-value: 4.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPyqrpinmmfqsy 100
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 alfphmtveqniafglkqdrlpkaeitARVQEMLALVHmqefakrkprQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:cd00267 69 ---------------------------EELRRRIGYVP----------QLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1616137381 181 DKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-238 |
8.31e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 163.68 E-value: 8.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----ARVPPYQRPINMMFQ--SYALFPHmT 107
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkVKLSDIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGLKQDRLPKAEITARVQEMLALVHM--QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-266 |
1.09e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 162.85 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR--VPPYQRP 92
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSY-ALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEhpttrySAEFIG 251
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN------NKEILE 237
|
250
....*....|....*...
gi 1616137381 252 SVNV---FEGLVKERLED 266
Cdd:PRK13632 238 KAKIdspFIYKLSKKLKG 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-236 |
2.80e-47 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 161.48 E-value: 2.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINM 95
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYAL-FPhMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA------KRP 168
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 169 KLLLLDEPMGALDKklrdRMQLEVVDILER------VGVTCVMvtHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:PRK13548 160 RWLLLDEPTSALDL----AHQHHVLRLARQlahergLAVIVVL--HDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-227 |
2.83e-47 |
|
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: 158.32 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPINM 95
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFpHMTVEQNIafglkqdrlpkaeitarvqemlalvhmqefakrkprqLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 176 PMGALDKKLRDRmqleVVDILERV--GVTCVMVTHDqEEAMTMAGRIAIMNRGK 227
Cdd:cd03228 123 ATSALDPETEAL----ILEALRALakGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-232 |
5.45e-47 |
|
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: 159.46 E-value: 5.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP-PYQRPI 93
Cdd:cd03266 1 MITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAF-----GLKQDrlpkaEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRP 168
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaglyGLKGD-----ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 169 KLLLLDEPMGALDkKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03266 156 PVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-241 |
9.88e-47 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 159.82 E-value: 9.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 10 AKAPKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRML-------AGFEqpTAGQIMLDGVD 82
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 83 L--ARVPPYQ--RPINMMFQSYALFPhMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQEFAKRKPRQ----LSGG 153
Cdd:COG1117 80 IydPDVDVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRlHGIKSKSELDEIVEESLRKAALWDEVKDRLKKsalgLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 154 QRQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRDRMqlevvdilervgvTCVMVTHDQEEAMTMAGRIAI 222
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQQAARVSDYTAF 225
|
250
....*....|....*....
gi 1616137381 223 MNRGKFVQIGEPEEIYEHP 241
Cdd:COG1117 226 FYLGELVEFGPTEQIFTNP 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-264 |
1.29e-46 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 161.67 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKS-------FDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARV 86
Cdd:PRK11308 3 QPLLQAIDLKKHypvkrglFKPErlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 87 PPYQ-----RPINMMFQS-YA-LFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQ-EFAKRKPRQLSGGQRQR 157
Cdd:PRK11308 83 DPEAqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
250 260
....*....|....*....|....*...
gi 1616137381 238 YEHPTTRYSAEFIGSV-NVFEGLVKERL 264
Cdd:PRK11308 243 FNNPRHPYTQALLSATpRLNPDDRRERI 270
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-241 |
1.29e-46 |
|
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: 167.25 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 8 PQAKAPKALTPLLEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR 85
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 VPPYQ--RPINMMFQSYALFpHMTVEQNIafglkqdRLPKAEIT-ARVQEMLALVHMQEFAKRKP-----------RQLS 151
Cdd:COG4987 402 LDEDDlrRRIAVVPQRPHLF-DTTLRENL-------RLARPDATdEELWAALERVGLGDWLAALPdgldtwlgeggRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR-MQlevvDILERV-GVTCVMVTHDqEEAMTMAGRIAIMNRGKFV 229
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQAlLA----DLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRIV 548
|
250
....*....|..
gi 1616137381 230 QIGEPEEIYEHP 241
Cdd:COG4987 549 EQGTHEELLAQN 560
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-250 |
1.53e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 159.15 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----------ARVPPY 89
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QRPINMMFQSYALFPHMTVEQNIAFG-LKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRP 168
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 169 KLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
..
gi 1616137381 249 FI 250
Cdd:PRK11264 243 FL 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-244 |
4.39e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 158.70 E-value: 4.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTK-----SFDGQHA----VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP 87
Cdd:PRK10419 1 MTLLNVSGLSHhyahgGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 88 -----PYQRPINMMFQSY--ALFPHMTVEQNIAFGLKQ-DRLPKAEITARVQEMLALVHMQ-EFAKRKPRQLSGGQRQRV 158
Cdd:PRK10419 81 raqrkAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ---I 231
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVL----QAGVIRLLKKLqqqfGTACLFITHDLRLVERFCQRVMVMDNGQIVEtqpV 236
|
250
....*....|...
gi 1616137381 232 GEPEEiYEHPTTR 244
Cdd:PRK10419 237 GDKLT-FSSPAGR 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-238 |
6.56e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 158.74 E-value: 6.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA--RVPPYQRPI 93
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSY-ALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-236 |
1.18e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 163.27 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlARVPPyQRP---- 92
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRI-RSPrdai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 ---INMMFQSYALFPHMTVEQNIAFGL---KQDRLPKAEITARVQEMlalvhMQEF-----AKRKPRQLSGGQRQRVALA 161
Cdd:COG3845 79 algIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIREL-----SERYgldvdPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 162 RSLAKRPKLLLLDEP------------MGALdKKLRDRmqlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:COG3845 154 KALYRGARILILDEPtavltpqeadelFEIL-RRLAAE------------GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
....*..
gi 1616137381 230 QIGEPEE 236
Cdd:COG3845 221 GTVDTAE 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-232 |
9.67e-45 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 153.21 E-value: 9.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLArvPPYQRPINMMFQS 99
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTV-EQNIAFG-LKQdrLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:cd03269 79 RGLYPKMKViDQLVYLAqLKG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 178 GALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03269 157 SGLDPVNVELL-KDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-229 |
3.14e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 151.01 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP-- 92
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSYAL--FPHMTVEQNIA--------FGLKQdRLPKAEItARVQEMLALVHMQeFAKR---KPRQLSGGQRQRVA 159
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR-GLTKKRR-ELFRELLATLGLG-LENRldtKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDKKLRDR-MQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALvLEL-TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-237 |
3.62e-43 |
|
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: 149.98 E-value: 3.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---INMM 96
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLkqDRLPKAEiTARVQEMLAL--VhMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGL--AALPRRS-RKIPDEIYELfpV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-236 |
2.11e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 2 NDVMPRPQAKAPKALTPLLEIRNLtkSF---DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 79 DGVDLARVPP--YQRPINMMFQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKP-------- 147
Cdd:COG1132 400 DGVDIRDLTLesLRRQIGVVPQDTFLF-SGTIRENIRYG-------RPDATdEEVEEAAKAAQAHEFIEALPdgydtvvg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 ---RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD--------KKLRDRMQlevvdilervGVTCVMVTH-------- 208
Cdd:COG1132 472 ergVNLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiqEALERLMK----------GRTTIVIAHrlstirna 541
|
250 260
....*....|....*....|....*...
gi 1616137381 209 DqeeamtmagRIAIMNRGKFVQIGEPEE 236
Cdd:COG1132 542 D---------RILVLDDGRIVEQGTHEE 560
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-227 |
3.22e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 147.11 E-value: 3.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP----YQ 90
Cdd:TIGR02211 1 LLKCENLGKRYqEGKLDTRvlkGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSneraKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPINMMF--QSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRP 168
Cdd:TIGR02211 81 RNKKLGFiyQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 169 KLLLLDEPMGALDKklrdRMQLEVVDILERV----GVTCVMVTHDqeeaMTMAGRIAI---MNRGK 227
Cdd:TIGR02211 161 SLVLADEPTGNLDN----NNAKIIFDLMLELnrelNTSFLVVTHD----LELAKKLDRvleMKDGQ 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-241 |
3.94e-42 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 147.83 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQrpINMM 96
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ--IARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 -----FQSYALFPHMTVEQN-------------IAFGLKQDRLPKAEITA--RVQEMLALVHMQEFAKRKPRQLSGGQRQ 156
Cdd:PRK11300 81 gvvrtFQHVRLFREMTVIENllvaqhqqlktglFSGLLKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*
gi 1616137381 237 IYEHP 241
Cdd:PRK11300 241 IRNNP 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-229 |
4.28e-42 |
|
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: 146.25 E-value: 4.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARvPPYQRPINMMFQS 99
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 --YALFPHmTVEQNIAFGLKqdrlPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 178 GALDkklRDRMQL--EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03226 155 SGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-229 |
1.96e-41 |
|
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: 145.04 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY--QRPINM 95
Cdd:cd03245 3 IEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFpHMTVEQNIAFGlkqdrLPKAEiTARVQEMLALVHMQEFAKRKP-----------RQLSGGQRQRVALARSL 164
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLG-----APLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 165 AKRPKLLLLDEPMGALD----KKLRDRMQLEVVDIlervgvTCVMVTHDQeEAMTMAGRIAIMNRGKFV 229
Cdd:cd03245 156 LNDPPILLLDEPTSAMDmnseERLKERLRQLLGDK------TLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-253 |
2.80e-41 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 147.93 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQ-------------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA 84
Cdd:PRK15079 7 VLLEVADLKVHFDIKdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 85 RVPPYQR-----PINMMFQS--YALFPHMTVEQNIAFGLK--QDRLPKAEITARVQEMLALVHMQE-FAKRKPRQLSGGQ 154
Cdd:PRK15079 87 GMKDDEWravrsDIQMIFQDplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSI----QAQVVNLLQQLqremGLSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242
|
250 260
....*....|....*....|...
gi 1616137381 231 IGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK15079 243 LGTYDEVYHNPLHPYTKALMSAV 265
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-245 |
3.68e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 145.90 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LARVPPYQRPIN 94
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQS-YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 174 DEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
Cdd:PRK13644 161 DEVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-247 |
1.02e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 144.84 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG----VDLARVPPYQRPI 93
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSY--ALFPHmTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
Cdd:PRK13639 160 VLDEPTSGLDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-242 |
1.28e-40 |
|
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: 149.95 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTK---SFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML----DGVDL----- 83
Cdd:TIGR03269 278 PIIKVRNVSKryiSVDRGvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMtkpgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 84 ---ARVPPYqrpINMMFQSYALFPHMTVEQNI--AFGLKqdrLPKAeiTARVQEMLALV-------HMQEFAKRKPRQLS 151
Cdd:TIGR03269 358 dgrGRAKRY---IGILHQEYDLYPHRTVLDNLteAIGLE---LPDE--LARMKAVITLKmvgfdeeKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
250
....*....|.
gi 1616137381 232 GEPEEIYEHPT 242
Cdd:TIGR03269 510 GDPEEIVEELT 520
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-237 |
2.49e-40 |
|
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: 151.17 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY--QRPINM 95
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKP-----------RQLSGGQRQRVALARS 163
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALG-------APYADdEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 164 LAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERV--GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMD----NRSEERFKDRLKRWlaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-242 |
2.62e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 144.01 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML------DGVDLARVPPYQRPINMMFQsyalFP-HM 106
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 107 ----TVEQNIAFGLKQDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13634 98 lfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 182 KKLRdrmqLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK13634 178 PKGR----KEMMEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-238 |
8.46e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 142.53 E-value: 8.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LARVPPYQRPINMMFQSyalfPH----- 105
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdEENLWDIRNKAGMVFQN----PDnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 106 MTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-244 |
8.59e-40 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 142.21 E-value: 8.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LARVPPYQ--RPI 93
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTvrKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQ-DRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 173 LDEP--------MGALDKklrdrmqleVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
Cdd:PRK11831 167 FDEPfvgqdpitMGVLVK---------LISELNSaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
.
gi 1616137381 244 R 244
Cdd:PRK11831 238 R 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-237 |
1.09e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 141.37 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPINMMFQ 98
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGlkqdRLP------KAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG4604 83 ENHINSRLTVRELVAFG----RFPyskgrlTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 173 LDEPMGALD-KKLRDRMQL--EVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG4604 159 LDEPLNNLDmKHSVQMMKLlrRLADELGK---TVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-220 |
1.94e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 140.34 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL------ARV 86
Cdd:PRK11629 3 KILLQCDNLCKRYqEGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 87 PPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAK 166
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqeeaMTMAGRI 220
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-237 |
2.87e-39 |
|
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: 140.22 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM------LDGVDLARVppyq 90
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPiNMMFQSYALF----PHMTVEQNIA------FGLKQDrlPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVAL 160
Cdd:COG1119 77 RK-RIGLVSPALQlrfpRDETVLDVVLsgffdsIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDIL-ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELL-LALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-214 |
2.06e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 136.21 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 28 SFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARVPpyqrpinmmfQSYAL---F 103
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVP----------QRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 104 PhMTVEQNIAFGLKQDRLP----KAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:NF040873 71 P-LTVRDLVAMGRWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1616137381 180 LDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAM 214
Cdd:NF040873 150 LDAESRERI-IALLAEEHARGATVVVVTHDLELVR 183
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-239 |
9.12e-38 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 135.82 E-value: 9.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARV--PPYQRPINM 95
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKPR-----------QLSGGQRQRVALARS 163
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG-------RPGATrEEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 164 LAKRPKLLLLDEPMGALDKKLRDRMQlevvDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQ----AALERlmKNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-238 |
1.63e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 136.38 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 16 LTPLLEIRNLTKSFDGQHAVDD---VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA--RVPPYQ 90
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPINMMFQSY-ALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPK 169
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-235 |
2.41e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.02 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY--QRPINMM 96
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSY--ALFPhMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
Cdd:PRK13647 164 EPMAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-240 |
3.10e-37 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 134.82 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSF----------------------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 75 QIMLDGvdlaRVPPyqrPINMM--FQsyalfPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSG 152
Cdd:COG1134 82 RVEVNG----RVSA---LLELGagFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 153 GQRQRVALARSLAKRPKLLLLDEPMGALD----KKLRDRMQlevvDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDaafqKKCLARIR----ELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
250
....*....|..
gi 1616137381 229 VQIGEPEEIYEH 240
Cdd:COG1134 225 VMDGDPEEVIAA 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-245 |
4.50e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.58 E-value: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDL--ARVPPYQ-- 90
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPIEvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPINMMFQSYALFPHMTVEQNIAFGLKQDRL--PKAEITARVQEMLALVHMQEFAKRK----PRQLSGGQRQRVALARSL 164
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP--- 241
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPehe 242
|
....*
gi 1616137381 242 -TTRY 245
Cdd:PRK14267 243 lTEKY 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-241 |
5.95e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 134.93 E-value: 5.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLARVPPYQRPINM 95
Cdd:PRK13652 3 LIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSY--ALFPhMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK13652 83 VFQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
34-242 |
6.52e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.93 E-value: 6.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTA---GQIMLDGVDLAR--VPPYQRPINMMFQSY-ALFPHMT 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAktVWDIREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 188 MQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-245 |
7.59e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 133.88 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDLARVP--PYQRP 92
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDviELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSYALFPHMTVEQNIAFGLKQDRL--PKAEITARVQEMLALVHMQEFAKRK----PRQLSGGQRQRVALARSLAK 166
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 167 RPKLLLLDEPMGALDKKlrDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP----T 242
Cdd:PRK14247 164 QPEVLLADEPTANLDPE--NTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhelT 241
|
...
gi 1616137381 243 TRY 245
Cdd:PRK14247 242 EKY 244
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-227 |
1.16e-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: 130.80 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPINM 95
Cdd:cd03246 1 LEVENVSFRYpGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHmTVEQNIafglkqdrlpkaeitarvqemlalvhmqefakrkprqLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 176 PMGALDKKlRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
Cdd:cd03246 123 PNSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGR 172
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-229 |
1.43e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 132.31 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR-----VPPYQRPINMMFQSYALFPH 105
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknreVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 106 MTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1616137381 186 DRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK10908 174 EGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-275 |
7.25e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 132.28 E-value: 7.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLAR--VPPYQRPI 93
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQS--YALFPhMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEhpttrySAEFIG 251
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA------EKEMLR 237
|
250 260
....*....|....*....|....*....
gi 1616137381 252 SVNVFE---GLVKERLE--DGLVLSSPGL 275
Cdd:PRK13636 238 KVNLRLpriGHLMEILKekDGFVFDELDL 266
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-223 |
1.07e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 136.65 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRP-QAKAPKALTPL--LEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
Cdd:TIGR02857 302 DAAPRPlAGKAPVTAAPAssLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 79 DGVDLARVPP--YQRPINMMFQSYALFPHmTVEQNIAFGlkqdrLPKAEITArVQEMLALVHMQEFAKRKP--------- 147
Cdd:TIGR02857 382 NGVPLADADAdsWRDQIAWVPQHPFLFAG-TIAENIRLA-----RPDASDAE-IREALERAGLDEFVAALPqgldtpige 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 --RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERV--GVTCVMVTHDqEEAMTMAGRIAIM 223
Cdd:TIGR02857 455 ggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD----AETEAEVLEALRALaqGRTVLLVTHR-LALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
13-236 |
1.33e-35 |
|
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: 137.78 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 13 PKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR--VPP 88
Cdd:TIGR03797 445 PGKLSGAIEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 YQRPINMMFQSYALFPHmTVEQNIAFGlkqdrlpkAEITA-RVQEMLALVHMQEFAKRKPRQ-----------LSGGQRQ 156
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSG-SIFENIAGG--------APLTLdEAWEAARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQ 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 157 RVALARSLAKRPKLLLLDEPMGALDkklrDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEE 236
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-229 |
1.75e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 137.16 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 16 LTPLLEIRNLTKSF---DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQR 91
Cdd:PRK10535 1 MTALLELKDIRRSYpsgEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PI------NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA 165
Cdd:PRK10535 81 AQlrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 166 KRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAmTMAGRIAIMNRGKFV 229
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGE----EVMAILHQLrdrGHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-228 |
1.98e-35 |
|
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: 127.93 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTksfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRpIN--M 95
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA-IRagI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MF-----QSYALFPHMTVEQNIAFglkqdrlpkaeitarvqemlalvhmqefakrkPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:cd03215 78 AYvpedrKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 171 LLLDEPMGALD--------KKLRDrmqlevvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:cd03215 126 LILDEPTRGVDvgakaeiyRLIRE---------LADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-237 |
2.15e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 137.56 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPqakAPKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-----DG 80
Cdd:NF033858 256 PRP---ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 81 VDLA---RVpPYqrpinmMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQR 157
Cdd:NF033858 333 GDIAtrrRV-GY------MSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
Cdd:NF033858 406 LSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-240 |
3.83e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 130.70 E-value: 3.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-ARVPPYQRPI 93
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-240 |
4.31e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.87 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLARVPPYQRP 92
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQS-YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-237 |
5.46e-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: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 5 MPRPQAKapkaltplLEIRNLTKSFDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD 82
Cdd:COG4618 324 LPRPKGR--------LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 83 LARVPPYQ--RPINMMFQSYALFPHmTVEQNIAfglkqdRLPKAEiTARVQE--MLALVHmqEFAKRKP----------- 147
Cdd:COG4618 396 LSQWDREElgRHIGYLPQDVELFDG-TIAENIA------RFGDAD-PEKVVAaaKLAGVH--EMILRLPdgydtrigegg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRDRmqlevvdilervGVTCVMVTHDQeEAMTM 216
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalaaaiRALKAR------------GATVVVITHRP-SLLAA 532
|
250 260
....*....|....*....|.
gi 1616137381 217 AGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEV 553
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-237 |
1.45e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 127.82 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQrpinmMFQS 99
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFP--HMT-----VEQNIAFGlkqdRLP--------KAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSL 164
Cdd:PRK11231 78 LALLPqhHLTpegitVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 165 AKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDIN----HQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-226 |
2.16e-34 |
|
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: 126.78 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSF-----DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD----GVDLAR 85
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 VPPYQ------RPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEfakR----KPRQLSGGQR 155
Cdd:COG4778 82 ASPREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPE---RlwdlPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV---GVTCVMVTHDqEEAM-TMAGRIAIMNRG 226
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAV----VVELIEEAkarGTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
36-239 |
2.18e-34 |
|
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: 126.89 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPINMMFQSYALFPhMTVEQNIA 113
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIGLVSQEPVLFD-GTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 114 FGLKQDRLPKAEITARvqemLALVHmqEFAKRKPR-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
Cdd:cd03249 99 YGKPDATDEEVEEAAK----KANIH--DFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 183 KlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:cd03249 173 E----SEKLVQEALDRAmkGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-240 |
2.85e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 128.20 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-------DLARVPPYQRPINMMFQ--SYALFP 104
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipanlkKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 105 HmTVEQNIAFGLKQDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 184 LRDrmqlEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13645 185 GEE----DFINLFERLnkeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-250 |
4.02e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.01 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFdGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP---------- 88
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVlKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 -----YQRPINMMFQSYALFPHMTVEQNIAFGLKQDR-LPKAEITARVQEMLALVHMQEFAKRK-PRQLSGGQRQRVALA 161
Cdd:PRK10619 85 nqlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLgLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
....*....
gi 1616137381 242 TTRYSAEFI 250
Cdd:PRK10619 244 QSPRLQQFL 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
30-237 |
6.91e-34 |
|
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: 125.68 E-value: 6.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPINMMFQSYALFpHMT 107
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGlkqDRLPKAEitaRVQEMLALVHMQEFAKRKPR-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03252 92 IRDNIALA---DPGMSME---RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-257 |
9.02e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 132.29 E-value: 9.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 5 MPRPQAKAPKALT-------PLLEIRNLTKSFDGQ-----------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA 66
Cdd:PRK10261 292 LEHPAKQEPPIEQdtvvdgePILQVRNLVTRFPLRsgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 67 GFEQPTAGQIMLDGVDLARVPPYQ-----RPINMMFQS-YA-LFPHMTVEQNIAFGLKQDRLPKAEITA-RVQEMLALVH 138
Cdd:PRK10261 372 RLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 139 MQ-EFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMA 217
Cdd:PRK10261 452 LLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIS 531
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1616137381 218 GRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257
Cdd:PRK10261 532 HRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVAD 571
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-240 |
2.05e-33 |
|
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: 130.61 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQA--KAPKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
Cdd:TIGR02203 312 DSPPEKDTgtRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 79 DGVDLA--RVPPYQRPINMMFQSYALFPHmTVEQNIAFGlkqdRLPKAEiTARVQEMLALVHMQEFAKRKPR-------- 148
Cdd:TIGR02203 392 DGHDLAdyTLASLRRQVALVSQDVVLFND-TIANNIAYG----RTEQAD-RAEIERALAAAYAQDFVDKLPLgldtpige 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 149 ---QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERV--GVTCVMVTHdQEEAMTMAGRIAIM 223
Cdd:TIGR02203 466 ngvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQ----AALERLmqGRTTLVIAH-RLSTIEKADRIVVM 540
|
250
....*....|....*..
gi 1616137381 224 NRGKFVQIGEPEEIYEH 240
Cdd:TIGR02203 541 DDGRIVERGTHNELLAR 557
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-244 |
2.55e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 126.91 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIrNLTKSFdGQHAVDdVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG---VDLAR---VPPYQRPI 93
Cdd:PRK11144 2 LEL-NFKQQL-GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEitaRVQEMLALVHMqefAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK11144 79 GYVFQDARLFPHYKVRGNLRYGMAKSMVAQFD---KIVALLGIEPL---LDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 174 DEPMGALDKKlRDRmqlEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:PRK11144 153 DEPLASLDLP-RKR---ELLPYLERlareINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-237 |
3.51e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 129.38 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLT-KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 82 DLARVPPYQRpINMMF-------QSYALFPHMTVEQNIAFGlKQDRLP--------KAEITARVQEMlalvhMQEFAKRK 146
Cdd:COG3845 321 DITGLSPRER-RRLGVayipedrLGRGLVPDMSVAENLILG-RYRRPPfsrggfldRKAIRAFAEEL-----IEEFDVRT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 147 P------RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD-----------KKLRDRmqlevvdilervGVTCVMVTHD 209
Cdd:COG3845 394 PgpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiefihqrlLELRDA------------GAAVLLISED 461
|
250 260
....*....|....*....|....*...
gi 1616137381 210 QEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG3845 462 LDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-250 |
3.94e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 124.38 E-value: 3.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLDG-VDLARVPPYQRPIN 94
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrVEFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 ---------MMFQSYALFPhMTVEQNIAFGLKQ-DRLPKAEITARVQEMLALVHMQEFAKRKPRQ----LSGGQRQRVAL 160
Cdd:PRK14258 83 lnrlrrqvsMVHPKPNLFP-MSVYDNVAYGVKIvGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 161 ARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM----NR-GKFVQIGEPE 235
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgneNRiGQLVEFGLTK 241
|
250
....*....|....*
gi 1616137381 236 EIYEHPTTRYSAEFI 250
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-253 |
5.86e-33 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.88 E-value: 5.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI---MLDG--VDLARVPPYQR 91
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrMRDGqlRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 piNMMFQSYALFphmtVEQNIAFGLKQD---------RLPKA------EITARVQEMLALVHMQefAKR---KPRQLSGG 153
Cdd:PRK11701 84 --RRLLRTEWGF----VHQHPRDGLRMQvsaggnigeRLMAVgarhygDIRATAGDWLERVEID--AARiddLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARL----LDLLRGLvrelGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|....
gi 1616137381 230 QIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
29-240 |
7.66e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 124.09 E-value: 7.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 29 FDGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR------VPPYQRPINMMFQsyal 102
Cdd:PRK13649 18 FEGR-ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 103 FPHM-----TVEQNIAFGLKQDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:PRK13649 93 FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 177 MGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13649 173 TAGLDPKGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-229 |
8.83e-33 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 128.12 E-value: 8.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG------FEqptaGQIMLDGVDL--ARVPPY 89
Cdd:PRK13549 4 YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtYE----GEIIFEGEELqaSNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QRP-INMMFQSYALFPHMTVEQNIAFG---LKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA 165
Cdd:PRK13549 80 ERAgIAIIHQELALVKELSVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 166 KRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK13549 160 KQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-237 |
9.32e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 122.69 E-value: 9.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP---INM 95
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 175 EPMGALDKklrdrmqLEVVDI------LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10895 163 EPFAGVDP-------ISVIDIkriiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-237 |
1.51e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 124.04 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD------------ 82
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 83 --------------LARVPPYQRPINMMFQ--SYALFpHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHM-QEFAKR 145
Cdd:PRK13651 83 vleklviqktrfkkIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 146 KPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|..
gi 1616137381 226 GKFVQIGEPEEI 237
Cdd:PRK13651 241 GKIIKDGDTYDI 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-237 |
1.55e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 127.59 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP---YQRPI 93
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGlkqdRLPK-----------AEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALAR 162
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIG----RHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 163 SLAKRPKLLLLDEPMGALDKKLRDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-213 |
1.71e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 121.81 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP-- 92
Cdd:PRK10584 6 IVEVHHLKKSVgQGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 ----INMMFQSYALFPHMTVEQNIafglkqdRLP-----KAEITARVQ--EMLALVHMQEFAKRKPRQLSGGQRQRVALA 161
Cdd:PRK10584 86 rakhVGFVFQSFMLIPTLNALENV-------ELPallrgESSRQSRNGakALLEQLGLGKRLDHLPAQLSGGEQQRVALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 162 RSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDIL----ERVGVTCVMVTHDQEEA 213
Cdd:PRK10584 159 RAFNGRPDVLFADEPTGNLDRQTGDK----IADLLfslnREHGTTLILVTHDLQLA 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-244 |
1.84e-32 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 125.72 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINM 95
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHMTVEQNIAFGL-----KQDRLPKAEITArVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 171 LLLDEPMGALDKKLRDRmQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
Cdd:PRK09536 161 LLLDEPTASLDINHQVR-TLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-257 |
1.88e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 127.61 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PTAGQIM-------------------- 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 78 -------------LDGVDLARVPPY--QRPINMMFQ-SYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQE 141
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRRriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 142 FAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIA 221
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1616137381 222 IMNRGKFVQIGEPEEIyehpttrySAEFIGSVNVFE 257
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV--------VAVFMEGVSEVE 268
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
2.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.81 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 11 KAPKALTPL-----LEIRNLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-- 78
Cdd:PRK13631 8 KKLKVPNPLsddiiLRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 79 ----DGVDLARVPPYQRP------------INMMFQ--SYALFPHmTVEQNIAFG---LKQDRLPKAEITARVQEMLALv 137
Cdd:PRK13631 88 iyigDKKNNHELITNPYSkkiknfkelrrrVSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLNKMGL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 138 hMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMA 217
Cdd:PRK13631 166 -DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTMEHVLEVA 243
|
250 260
....*....|....*....|....*
gi 1616137381 218 GRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-246 |
2.57e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 128.30 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPQAKAPKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD 82
Cdd:TIGR00958 465 PLTGTLAPLNLEGLIEFQDVSFSYPNRPDVpvlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 83 LARVPP--YQRPINMMFQSYALFPHmTVEQNIAFGLkqDRLPKAEITARVQEMLALVHMQEFAK-------RKPRQLSGG 153
Cdd:TIGR00958 545 LVQYDHhyLHRQVALVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 154 QRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGT 696
|
250
....*....|...
gi 1616137381 234 PEEIYEHPTTRYS 246
Cdd:TIGR00958 697 HKQLMEDQGCYKH 709
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-236 |
3.68e-32 |
|
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: 120.79 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMMF 97
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHmTVEQNIAFGlkqDRLPKAEitaRVQEMLALVHMQEFAKRKPR-----------QLSGGQRQRVALARSLAK 166
Cdd:cd03254 84 QDTFLFSG-TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-250 |
6.24e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 125.97 E-value: 6.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 12 APKALTPLLEIRNLTKSF-----------DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAgfeqpTAGQI 76
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 77 MLDGVDLARVP-----PYQRPINMMFQ--SYALFPHMTVEQNIAFGLK--QDRLPKAEITARVQEMLALVHMQ-EFAKRK 146
Cdd:PRK15134 343 WFDGQPLHNLNrrqllPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 147 PRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAI 222
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV----QAQILALLkslqQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260
....*....|....*....|....*...
gi 1616137381 223 MNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-240 |
9.80e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 9.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 10 AKAPKALTPLLEIRNLTksfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY 89
Cdd:COG1129 247 KRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QRpIN--MMF-----QSYALFPHMTVEQNIAFGLkQDR------LPKAEITARVQEMlalvhMQEFAKRKP------RQL 150
Cdd:COG1129 323 DA-IRagIAYvpedrKGEGLVLDLSIRENITLAS-LDRlsrgglLDRRRERALAEEY-----IKRLRIKTPspeqpvGNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 151 SGGQRQRVALARSLAKRPKLLLLDEP-----MGAldKKlrdrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAI 222
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPtrgidVGA--KA-------EIYRLIRELaaeGKAVIVISSELPELLGLSDRILV 466
|
250
....*....|....*...
gi 1616137381 223 MNRGKFVQIGEPEEIYEH 240
Cdd:COG1129 467 MREGRIVGELDREEATEE 484
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
16-239 |
9.87e-32 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 126.60 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 16 LTPLLEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPyqrpi 93
Cdd:TIGR03796 474 LSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR----- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALfphmtVEQNIA-FG--------LKQDRLPKAEITARVQEmlALVHmQEFAKRK----------PRQLSGGQ 154
Cdd:TIGR03796 549 EVLANSVAM-----VDQDIFlFEgtvrdnltLWDPTIPDADLVRACKD--AAIH-DVITSRPggydaelaegGANLSGGQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 155 RQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVGVTCVMVTH------DQEEamtmagrIAIMNRGKF 228
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDPE----TEKIIDDNLRRRGCTCIIVAHrlstirDCDE-------IIVLERGKV 689
|
250
....*....|.
gi 1616137381 229 VQIGEPEEIYE 239
Cdd:TIGR03796 690 VQRGTHEELWA 700
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-232 |
1.48e-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: 118.79 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlaRVPPyqrPINMMfqsYALFPHMTVEQNI 112
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSS---LLGLG---GGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 113 AFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1616137381 193 VDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-240 |
2.60e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.48 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPQAKAPKALtpllEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-A 84
Cdd:PRK13536 32 SIPGSMSTVAI----DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 85 RVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSL 164
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE-IYEH 240
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAlIDEH 263
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-239 |
3.16e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 119.84 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA------RVPPYQRPINMMFQsyalFPHM- 106
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 107 ----TVEQNIAFGLKQDRLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13643 97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 182 KKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:PRK13643 177 PKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-250 |
5.05e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 118.34 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDL--ARVPPYQ 90
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 --RPINMMFQSYALFPhMTVEQNIAFGLKQDRLP-KAEITARVQEMLALVHMQEFAKRKPRQ----LSGGQRQRVALARS 163
Cdd:PRK14239 84 lrKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
....*..
gi 1616137381 244 RYSAEFI 250
Cdd:PRK14239 241 KETEDYI 247
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-212 |
5.09e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 117.51 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP--YQRPIN 94
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYALFPHmTVEQNIAFGLkQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPW-QIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1616137381 175 EPMGALDKKLRDRmqleVVDILERV----GVTCVMVTHDQEE 212
Cdd:PRK10247 163 EITSALDESNKHN----VNEIIHRYvreqNIAVLWVTHDKDE 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-253 |
1.07e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 118.27 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG-----QIMLDG---VDLARV 86
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGrsiFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 87 PPYQRPINMMFQSYALFPhMTVEQNIAFGLKQDRL-PKAEITARVQEMLALVHMQEFAKRK----PRQLSGGQRQRVALA 161
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
250
....*....|....*.
gi 1616137381 242 ----TTRYSAEFIGSV 253
Cdd:PRK14271 254 khaeTARYVAGLSGDV 269
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
34-251 |
1.31e-30 |
|
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: 116.70 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLARVPPYQRPINMMFQS--YALFPHMT 107
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGLKQDRLPKAEITARVQEML---ALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALeavGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 185 rdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
Cdd:TIGR02770 160 ---NQARVLKLLRELrqlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-227 |
1.38e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.10 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLARVPpyqrpinmmfQSY 100
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP----------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 ALFPHMTVEQNIAFGLK-----QDRLPKAEIT-----------ARVQEMLALVH-----------------MQEFAKRKP 147
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAelralEAELEELEAKlaepdedlerlAELQEEFEALGgweaearaeeilsglgfPEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV-----GvTCVMVTHDQE--EAmtMAGRI 220
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LESIEWLEEFlknypG-TVLVVSHDRYflDR--VATRI 219
|
....*..
gi 1616137381 221 AIMNRGK 227
Cdd:COG0488 220 LELDRGK 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-236 |
1.45e-30 |
|
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: 116.56 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARV--PPYQRPINMM 96
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFpHMTVEQNIAFGlkqdrlpkaEITARVQEMLALV---HMQEFAKRKPRQ-----------LSGGQRQRVALAR 162
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG---------RPDATDEEVIEAAkaaQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 163 SLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEE 236
Cdd:cd03253 151 AILKNPPILLLDEATSALDTH----TEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-241 |
1.71e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 118.85 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLARVPPY 89
Cdd:COG4170 2 PLLDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QR------PINMMFQ--SYALFPHMTVEQNIAFGLKQDRLPK---AEITARVQEMLALVH----------MQEFakrkPR 148
Cdd:COG4170 82 ERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIPSWTFKGkwwQRFKWRKKRAIELLHrvgikdhkdiMNSY----PH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMN 224
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST----TQAQIFRLLARLnqlqGTSILLISHDLESISQWADTITVLY 233
|
250
....*....|....*..
gi 1616137381 225 RGKFVQIGEPEEIYEHP 241
Cdd:COG4170 234 CGQTVESGPTEQILKSP 250
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-209 |
2.09e-30 |
|
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: 121.70 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPQAKAPKALT-----PLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
Cdd:TIGR02868 316 PVAEGSAPAAGAvglgkPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 80 GVDLARVP--PYQRPINMMFQSYALFpHMTVEQNIafglkqdRLPKAEIT-ARVQEMLALVHMQEFAKRKP--------- 147
Cdd:TIGR02868 396 GVPVSSLDqdEVRRRVSVCAQDAHLF-DTTVRENL-------RLARPDATdEELWAALERVGLADWLRALPdgldtvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 148 --RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHD 209
Cdd:TIGR02868 468 ggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
40-237 |
2.34e-30 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 115.72 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlARVPPYQRPINMMFQSYAL---FPhMTVEQNIAFG- 115
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---ASPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 116 ---LKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEV 192
Cdd:TIGR03771 77 tghIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1616137381 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNrGKFVQIGEPEEI 237
Cdd:TIGR03771 156 FIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-237 |
3.11e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 120.93 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP---YQR 91
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEM---LALvHMQEFAkrkprqLSGGQRQRVALARSLAKRP 168
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALgcqLDL-DSSAGS------LEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-209 |
4.86e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARVPPYQRpinmm 96
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDQHQE----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 fqsyALFPHMTVEQNIAFGLKQDRlpKAEITARVQEMLalvhmqeF----AKRKPRQLSGGQRQRVALARSLAKRPKLLL 172
Cdd:COG0488 389 ----ELDPDKTVLDELRDGAPGGT--EQEVRGYLGRFL-------FsgddAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1616137381 173 LDEPMGALDkklrdrmqLEVVDILERV-----GvTCVMVTHD 209
Cdd:COG0488 456 LDEPTNHLD--------IETLEALEEAlddfpG-TVLLVSHD 488
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-289 |
9.37e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 116.73 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQ---------------------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
Cdd:COG4586 3 EVENLSKTYRVYekepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 80 GVDlarvpPYQ------RPINMMF-QSYALFPHMTVEQNiaFGLKQD--RLPKAEITARVQEMLALVHMQEFAKRKPRQL 150
Cdd:COG4586 83 GYV-----PFKrrkefaRRIGVVFgQRSQLWWDLPAIDS--FRLLKAiyRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD----KKLRDRmqleVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDvvskEAIREF----LKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 227 KFVQIGEPEEIyehpTTRYSAEFIGSVNVFEGLVKERLEDGL-VLSSPGLMHPLKVDPDASVVD 289
Cdd:COG4586 232 RIIYDGSLEEL----KERFGPYKTIVLELAEPVPPLELPRGGeVIEREGNRVRLEVDPRESLAE 291
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-229 |
1.45e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 113.97 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQH---------------------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 79 DGVDlarvpPYQRPIN-------MMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLS 151
Cdd:cd03267 81 AGLV-----PWKRRKKflrrigvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-240 |
2.06e-29 |
|
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: 112.62 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLARVPPYQRP---IN 94
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERArlgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYALFPhmtveqniafGLKqdrlpkaeitarVQEMLALVHMqefakrkprQLSGGQRQRVALARSLAKRPKLLLLD 174
Cdd:cd03217 81 LAFQYPPEIP----------GVK------------NADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 175 EPMGALDKklrDRMQL--EVVDILERVGVTCVMVTHDQEEAMTM-AGRIAIMNRGKFVQIGEPE---EIYEH 240
Cdd:cd03217 130 EPDSGLDI---DALRLvaEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKElalEIEKK 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
35-240 |
3.07e-29 |
|
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: 118.60 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMMFQSYALFPHmTVEQNI 112
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 113 A-FGLKQDrlPKAEITARVqemLALVHmqEFAKRKPR-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:TIGR01842 413 ArFGENAD--PEKIIEAAK---LAGVH--ELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 181 DKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:TIGR01842 486 DEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-241 |
3.17e-29 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 114.12 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKS-------FDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLArVPPY 89
Cdd:PRK15112 4 LLEVRNLSKTfryrtgwFRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 ----QRpINMMFQ--SYALFPHMTVEQNIAFGLKQD-RLPKAEITARVQEMLALVHM-QEFAKRKPRQLSGGQRQRVALA 161
Cdd:PRK15112 83 syrsQR-IRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVThdQEEAMT--MAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLA 239
|
..
gi 1616137381 240 HP 241
Cdd:PRK15112 240 SP 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-230 |
4.56e-29 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 117.70 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLArvppYQRP---- 92
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR----FASTtaal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 ---INMMFQSYALFPHMTVEQNIAFGlkqdRLP-------KAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALAR 162
Cdd:PRK11288 78 aagVAIIYQELHLVPEMTVAENLYLG----QLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 163 SLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQL-FRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-227 |
6.30e-29 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 112.18 E-value: 6.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 12 APKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLarvPP 88
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYPTRPDTlvlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 YQ-----RPINMMFQSYALFPHmTVEQNIAFGLKQdrLPKAEITARVQEMLALVHMQEFAK-------RKPRQLSGGQRQ 156
Cdd:cd03248 81 YEhkylhSKVSLVGQEPVLFAR-SLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASgydtevgEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-237 |
6.86e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 117.64 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLT-KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLARVPP--YQRPINMM 96
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPesWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKPR-----------QLSGGQRQRVALARSL 164
Cdd:PRK11174 429 GQNPQLP-HGTLRDNVLLG-------NPDASdEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 165 AKRPKLLLLDEPMGALDKKLRDRmqleVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQL----VMQALNAAsrRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-250 |
1.02e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.45 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 11 KAPKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV------DLA 84
Cdd:PRK14246 2 EAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 85 RVPPYQ--RPINMMFQSYALFPHMTVEQNIAFGLKQDRLP-KAEITARVQEMLALVHM-QEFAKR---KPRQLSGGQRQR 157
Cdd:PRK14246 82 QIDAIKlrKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|...
gi 1616137381 238 YEHPTTRYSAEFI 250
Cdd:PRK14246 240 FTSPKNELTEKYV 252
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-232 |
1.42e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 116.98 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
Cdd:PRK13657 318 DVRDPPGAIDLGRVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 82 DLARV--PPYQRPINMMFQSYALFpHMTVEQNIafglkqdRLPKAEIT-ARVQEMLALVHMQEFAKRKP----------- 147
Cdd:PRK13657 398 DIRTVtrASLRRNIAVVFQDAGLF-NRSIEDNI-------RVGRPDATdEEMRAAAERAQAHDFIERKPdgydtvvgerg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVK-AALDEL-MKGRTTFIIAH-RLSTVRNADRILVFDNGR 546
|
....*
gi 1616137381 228 FVQIG 232
Cdd:PRK13657 547 VVESG 551
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-238 |
1.45e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.57 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR------VPPYQRPINMMFQsyalFPHM- 106
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 107 ----TVEQNIAFGLKQDRLPKAEITARVQEML-ALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13646 98 lfedTVEREIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-229 |
2.92e-28 |
|
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: 115.31 E-value: 2.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTA---GQIMLDGVDL--ARVPPYQRP- 92
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLkaSNIRDTERAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INMMFQSYALFPHMTVEQNIAFG----LKQDRLPKAEITARVQEMLALVHMQEFAKRKP-RQLSGGQRQRVALARSLAKR 167
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 168 PKLLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-232 |
4.78e-28 |
|
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: 108.17 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRP-INMM 96
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFpHMTVEQNIAfglkqdrlpkaeitarvqemlalvhmqefakrkpRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 177 MGALDKKlRDRMQLEVV-DILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03247 126 TVGLDPI-TERQLLSLIfEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-226 |
4.98e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.49 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF---EQPTAGQIMLDGVDLARVPPYQRPI-- 93
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 -----NMMFQSYALFPHMTVEQNIAFG-LKQDRLPKAEIT--ARVQEMLAL-----VHMQEFAKRKPRQLSGGQRQRVAL 160
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVLENVLIGaLGSTPFWRTCFSwfTREQKQRALqaltrVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 161 ARSLAKRPKLLLLDEPMGALDKKlRDRMQLEVV-DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPE-SARIVMDTLrDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-208 |
7.55e-28 |
|
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: 108.21 E-value: 7.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRPINMMFQ 98
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFglKQDRLPKAEITarVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:TIGR01189 81 LPGLKPELSALENLHF--WAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTcVMVTH 208
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIV-LLTTH 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-250 |
1.29e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.49 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLR-------MLAGFEqpTAGQIMLDGVDL--AR 85
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLyaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 VPPYQ--RPINMMFQSYALFPHmTVEQNIAFGLKQDRLpKAEITARVQEMLALVHMQEFAKRKPRQ----LSGGQRQRVA 159
Cdd:PRK14243 84 VDPVEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHDQEEAMTMAGRIAIMN---------RGKFVQ 230
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVE 239
|
250 260
....*....|....*....|
gi 1616137381 231 IGEPEEIYEHPTTRYSAEFI 250
Cdd:PRK14243 240 FDRTEKIFNSPQQQATRDYV 259
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
47-238 |
2.66e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.94 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 47 IFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLAR--VPPYQRPINMMFQ--SYALFpHMTVEQNIAFGLKQDR 120
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKrgLLALRQQVATVFQdpEQQIF-YTDIDSDIAFSLRNLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 121 LPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILERV- 199
Cdd:PRK13638 108 VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM----IAIIRRIv 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1616137381 200 --GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
Cdd:PRK13638 184 aqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-242 |
6.35e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 107.57 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA--RVPPYQRPINMMFQS 99
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFGlkqdRLP--------KAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK10575 94 LPAAEGMTVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 172 LLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PRK10575 170 LLDEPTSALDIA----HQVDVLALVHRLsqerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-232 |
7.03e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 8 PQAKAPKALTPLLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR 85
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 VPPYQRPINMMF--QSYALFPHmTVEQNIafglkqdRLPKAEIT-ARVQEMLALVHMQEFAKRKP----------RQLSG 152
Cdd:PRK11160 407 YSEAALRQAISVvsQRVHLFSA-TLRDNL-------LLAAPNASdEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDA----ETERQILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQIIE 553
|
..
gi 1616137381 231 IG 232
Cdd:PRK11160 554 QG 555
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-208 |
7.51e-27 |
|
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: 105.65 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRPINMMFQ 98
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFglkqdrLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03231 81 APGIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMQLEVVDILERVGVTcVMVTH 208
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMV-VLTTH 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-183 |
8.50e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 105.66 E-value: 8.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP-YQRpiNMMF 97
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQ--DLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYA--LFPHMTVEQNIAFGLKQDRLPKAEitaRVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:PRK13538 79 LGHQpgIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
....*...
gi 1616137381 176 PMGALDKK 183
Cdd:PRK13538 156 PFTAIDKQ 163
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-234 |
3.17e-26 |
|
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: 110.87 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 15 ALTPLLEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-ARVPPYQR 91
Cdd:TIGR01257 924 GLVPGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 172 LLDEPMGALDKKLRDrmqlEVVDIL--ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRR----SIWDLLlkYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-232 |
3.85e-26 |
|
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: 104.66 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVDLARvPPYQRPINMMFQSYALFPHMTVEQNIA 113
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP-DQFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 114 FGLK---QDRLPKAEITARV-QEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQ 189
Cdd:cd03234 104 YTAIlrlPRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1616137381 190 LEVVDILERVGVT--CVMVTHDQ--EEAMTMAGRIAIMNRGKFVQIG 232
Cdd:cd03234 180 LNLVSTLSQLARRnrIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-253 |
6.94e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.35 E-value: 6.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 8 PQAKAPKALTPLLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGfEQPTAGQIMLD 79
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 80 GVDLARVPPYQ------RPINMMFQS--YALFPHMTV-EQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRK---P 147
Cdd:PRK09473 80 GREILNLPEKElnklraEQISMIFQDpmTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI-MTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
250 260
....*....|....*....|....*..
gi 1616137381 227 KFVQIGEPEEIYEHPTTRYSAEFIGSV 253
Cdd:PRK09473 239 RTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-229 |
1.16e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.42 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ---RPIN 94
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYALFPHMTVEQNIAF-GLKQDRLPKAEITARVQEMLAlvHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 174 DEP-MGaldkkLRDRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK11614 162 DEPsLG-----LAPIIIQQIFDTIEQLreqGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-230 |
1.24e-25 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 107.95 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG------FEqptaGQIMLDGvDLARV----PP 88
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDG-EVCRFkdirDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDR---LPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA 165
Cdd:NF040905 76 EALGIVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 166 KRPKLLLLDEPMGALD----KKLRDRMqLEvvdiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:NF040905 156 KDVKLLILDEPTAALNeedsAALLDLL-LE----LKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-235 |
1.94e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.84 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLARVPPYQRP---IN 94
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERAragIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYALFPHMTVEQ--NIAFG-LKQDRLPKAEITARVQEMLALVHM-QEFAKRkprQL----SGGQRQRVALARSLAK 166
Cdd:COG0396 81 LAFQYPVEIPGVSVSNflRTALNaRRGEELSAREFLKLLKEKMKELGLdEDFLDR---YVnegfSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 167 RPKLLLLDEPMGALDkklRDRMQLeVVDILERV---GVTCVMVTHDQeeamtmagRI---------AIMNRGKFVQIGEP 234
Cdd:COG0396 158 EPKLAILDETDSGLD---IDALRI-VAEGVNKLrspDRGILIITHYQ--------RIldyikpdfvHVLVDGRIVKSGGK 225
|
.
gi 1616137381 235 E 235
Cdd:COG0396 226 E 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
6-237 |
2.04e-25 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 107.91 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPQAKAPKALTPLL----EIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
Cdd:TIGR01846 438 PTEPRSAGLAALPELrgaiTFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVD 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 80 GVDLARVPP--YQRPINMMFQSYALFPHmTVEQNIAFGLKQdrLPKAEITARVQemLALVHmqEFAKRKPR--------- 148
Cdd:TIGR01846 518 GVDLAIADPawLRRQMGVVLQENVLFSR-SIRDNIALCNPG--APFEHVIHAAK--LAGAH--DFISELPQgyntevgek 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 149 --QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRG 226
Cdd:TIGR01846 591 gaNLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKG 667
|
250
....*....|.
gi 1616137381 227 KFVQIGEPEEI 237
Cdd:TIGR01846 668 QIAESGRHEEL 678
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-208 |
6.03e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLT-KSFDGQHAVDDVSLTIYKGEifALL--GASGCGKSTLLRMLAGFEQPTAGQIML- 78
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARp 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 79 DGVDLARVPpyQRPinmmfqsYalFPHMTVEQNIAFGLKQDRLPKAEItarvQEMLALVHMQEFAKR------KPRQLSG 152
Cdd:COG4178 424 AGARVLFLP--QRP-------Y--LPLGTLREALLYPATAEAFSDAEL----REALEAVGLGHLAERldeeadWDQVLSL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM-QLevvdILERV-GVTCVMVTH 208
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALyQL----LREELpGTTVISVGH 542
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-208 |
7.33e-25 |
|
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: 99.93 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLT---KSFDGQHA---VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDGVDLARVPPYQR 91
Cdd:cd03213 4 LSFRNLTvtvKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 pINMMFQSYALFPHMTVEQNIAFGlkqdrlpkAEItarvqemlalvhmqefakrkpRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:cd03213 84 -IGYVPQDDILHPTLTVRETLMFA--------AKL---------------------RGLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1616137381 172 LLDEPMGALDKklrdRMQLEVVDILERV---GVTCVMVTH 208
Cdd:cd03213 134 FLDEPTSGLDS----SSALQVMSLLRRLadtGRTIICSIH 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-241 |
7.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA------RVPPYQRPINMMFQsyalFPHM-- 106
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 107 ---TVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQE-FAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 183 KLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK13641 179 EGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-211 |
1.24e-24 |
|
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: 97.90 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLARVPpyqrpinmmfq 98
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGsTVKIGYFE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 syalfphmtveqniafglkqdrlpkaeitarvqemlalvhmqefakrkprQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:cd03221 70 --------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|...
gi 1616137381 179 ALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE 211
Cdd:cd03221 100 HLD--LESIEALE--EALKEYPGTVILVSHDRY 128
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-209 |
1.51e-24 |
|
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: 105.02 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARVPpyqrpinmmfQ 98
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVD----------Q 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SY-ALFPHMTVEQNIAFGLKQDRLPKAEITARvqemlALVHMQEFA----KRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGLDIIKLGKREIPSR-----AYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|....*..
gi 1616137381 174 DEPMGALD-KKLRdrmQLEvvDILERVGVTCVMVTHD 209
Cdd:TIGR03719 468 DEPTNDLDvETLR---ALE--EALLNFAGCAVVISHD 499
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
38-237 |
1.85e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 100.30 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLARVPPYQ--RPINMMFQSYALFPHMTVEQNIAFG 115
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 116 LkQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAK-------RPKLLLLDEPMGALDKklrdRM 188
Cdd:COG4138 94 Q-PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV----AQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 189 QLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:COG4138 169 QAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-282 |
2.17e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 102.13 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQP---TAGQIMLDGVDLARVPPYQ 90
Cdd:PRK11022 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 R------PINMMFQS--YALFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHMQEFAKR---KPRQLSGGQRQRV 158
Cdd:PRK11022 83 RrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTI----QAQIIELLlelqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1616137381 235 EEIYEHPTTRYSAEFIGSVNVF-EGlvKERLEdglvlSSPGLMhPLKVD 282
Cdd:PRK11022 239 HDIFRAPRHPYTQALLRALPEFaQD--KARLA-----SLPGVV-PGKYD 279
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-181 |
2.03e-23 |
|
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: 101.82 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
Cdd:COG5265 341 EVADAPDAPPLVVGGGEVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 82 DLARVPP--YQRPINMMFQSYALFpHMTVEQNIAFGlkqdrlpKAEIT-ARVQEMLALVHMQEFAKRKPRQ--------- 149
Cdd:COG5265 421 DIRDVTQasLRAAIGIVPQDTVLF-NDTIAYNIAYG-------RPDASeEEVEAAARAAQIHDFIESLPDGydtrvgerg 492
|
170 180 190
....*....|....*....|....*....|....
gi 1616137381 150 --LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-237 |
3.06e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 101.35 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMM 96
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHmTVEQNIAFGLK----QDRLPKA----EITARVQEMlALVHMQEFAKRKpRQLSGGQRQRVALARSLAKRP 168
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKenvsQDEIWAAceiaEIKDDIENM-PLGYQTELSEEG-SSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERvgvTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-252 |
3.58e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.94 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQP----TAGQIMLDGVDLARVP 87
Cdd:PRK15134 3 QPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 88 PYQ------RPINMMFQS--YALFPHMTVEQNIAFGLKQDRLPKAEiTARVqEMLAL---VHMQEFAKR---KPRQLSGG 153
Cdd:PRK15134 83 EQTlrgvrgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRRE-AARG-EILNCldrVGIRQAAKRltdYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250
....*....|....*....
gi 1616137381 234 PEEIYEHPTTRYSAEFIGS 252
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNS 259
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
24-237 |
5.33e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.98 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQ--RPINMMFQSYA 101
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 102 LFPHMTVEQNIAFGlkqdRLPKAEITAR--------VQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK10253 92 TPGDITVQELVARG----RYPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 174 DEPMGALDKKLRDRMqLEVVDILERV-GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10253 168 DEPTTWLDISHQIDL-LELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
38-237 |
5.80e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 96.16 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDG--------VDLARVPPY----QRPINMM--FQSYALF 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGqpleawsaAELARHRAYlsqqQTPPFAMpvFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 104 phmtveqniafglKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALA-------RSLAKRPKLLLLDEP 176
Cdd:PRK03695 94 -------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 177 MGALD---KKLRDRmqleVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK03695 161 MNSLDvaqQAALDR----LLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-234 |
6.20e-23 |
|
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: 95.64 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLagfeQPTAGQIMLDGVDLARVPPYQ--R 91
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHmTVEQNIA-FGLKQDrlpkaeitARVQEMLALVHMQEFAKRKP-----------RQLSGGQRQRVA 159
Cdd:cd03244 79 RISIIPQDPVLFSG-TIRSNLDpFGEYSD--------EELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEP 234
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQ-KTIR-EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-211 |
7.24e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 95.41 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLARvppyQRPInmmfqsyalfphmtVE 109
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR----EASL--------------ID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 110 qniAFGLKQDRLPKAEITARVqemlALVHMQEFaKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
Cdd:COG2401 105 ---AIGRKGDFKDAVELLNAV----GLSDAVLW-LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|..
gi 1616137381 190 LEVVDILERVGVTCVMVTHDQE 211
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYD 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-293 |
8.72e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 8.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQpTAGQIMLDGVDLAR-------- 85
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRRrsrqviel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 ----VPPYQR----PINMMFQS--YALFPHMTVEQNIAFGLK-QDRLPKAEITARVQEMLALVHM---QEFAKRKPRQLS 151
Cdd:PRK10261 91 seqsAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQI-LQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 231 IGEPEEIYEHPTTRYSAEFIGSVNVFEGLVKERLEDGLVLssPGLMHPLKVDPDA---SVVDNVPV 293
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPL--ISLEHPAKQEPPIeqdTVVDGEPI 313
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-244 |
2.16e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.77 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQhAVDDVSLTIYKGEIFALLGASGCGKS----TLLRML-AGFEQpTAGQIMLDGVDLARVPPYQRPIN 94
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQS--YALFPHMTVEQNIAFGLKQDRLPKAEIT-ARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK10418 83 TIMQNprSAFNPLHTMHTHARETCLALGKPADDATlTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 172 LLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR 244
Cdd:PRK10418 163 IADEPTTDLDVV----AQARILDLLESIvqkrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFnapKHAVTR 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-181 |
3.20e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.17 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA--RVPPYQRPINM 95
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFpHMTVEQNIAFGlKQDRLPKAEITARVQemlaLVHMQEFAKRKPR-----------QLSGGQRQRVALARSL 164
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYA-RTEQYSREQIEEAAR----MAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARAL 495
|
170
....*....|....*..
gi 1616137381 165 AKRPKLLLLDEPMGALD 181
Cdd:PRK11176 496 LRDSPILILDEATSALD 512
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-208 |
9.16e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 9.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlARVPPYQRPINMMF 97
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHMTVEQNIAF--GLKQDRLPkaeitaRVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSL-AKRPkLLLLD 174
Cdd:PRK13539 80 HRNAMKPALTVAENLEFwaAFLGGEEL------DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLvSNRP-IWILD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1616137381 175 EPMGALDKKlRDRMQLEVVDI-LERVGvTCVMVTH 208
Cdd:PRK13539 153 EPTAALDAA-AVALFAELIRAhLAQGG-IVIAATH 185
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-227 |
1.22e-21 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 91.38 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLARVPpyQRPIN 94
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVS--QEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MmfqsyalfpHMTVEQNIAFGLK--QDRLpkaeitARVQEMLALVH-MQEFAKR-------KPRQLSGGQRQRVALARSL 164
Cdd:cd03250 78 Q---------NGTIRENILFGKPfdEERY------EKVIKACALEPdLEILPDGdlteigeKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 165 AKRPKLLLLDEPMGALDKKLRDRmqlevvdILERV-------GVTCVMVTHdQEEAMTMAGRIAIMNRGK 227
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRH-------IFENCilglllnNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-227 |
1.41e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 96.19 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLARVPPYQRPINMM 96
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMtveqniafgLKQDRLPKAEitARVQEMLALVHMQEfakrKPR---------QLSGGQRQRVALARSLAKR 167
Cdd:PRK10522 403 FTDFHLFDQL---------LGPEGKPANP--ALVEKWLERLKMAH----KLEledgrisnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGK 227
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-256 |
1.93e-21 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 93.71 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSF---DGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLARVPPY 89
Cdd:PRK15093 2 PLLDIRNLTIEFktsDGWvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QR------PINMMFQ--SYALFPHMTVE----QNIAFGLKQDRLPKaEITARVQEMLALVHMQEFAKRK------PRQLS 151
Cdd:PRK15093 82 ERrklvghNVSMIFQepQSCLDPSERVGrqlmQNIPGWTYKGRWWQ-RFGWRKRRAIELLHRVGIKDHKdamrsfPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPT----TQAQIFRLLTRLnqnnNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
250 260
....*....|....*....|....*....
gi 1616137381 228 FVQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
Cdd:PRK15093 237 TVETAPSKELVTTPHHPYTQALIRAIPDF 265
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-236 |
5.46e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAgFEQPT----AGQIMLDGVDLARvpPYQRPINMMFQSYALF-PHMT 107
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDA--KEMRAISAYVQQDDLFiPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFG--LK-QDRLPKAEITARVQEMLALVHMQEFAKRK------PRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:TIGR00955 116 VREHLMFQahLRmPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 179 ALDKKlrdrMQLEVVDILERV---GVTCVMVTHD-QEEAMTMAGRIAIMNRGKFVQIGEPEE 236
Cdd:TIGR00955 196 GLDSF----MAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-209 |
1.43e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 93.26 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARVPpyqrpinmmfQ 98
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVD----------Q 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SY-ALFPHMTVEQNIAFGLKQDRLPKAEITARvqemlALVHMQEFA----KRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:PRK11819 395 SRdALDPNKTVWEEISGGLDIIKVGNREIPSR-----AYVGRFNFKggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
170 180 190
....*....|....*....|....*....|....*...
gi 1616137381 174 DEPMGALD-KKLRdrmQLEVVdILERVGvtCVMV-THD 209
Cdd:PRK11819 470 DEPTNDLDvETLR---ALEEA-LLEFPG--CAVViSHD 501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-211 |
1.89e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 93.09 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLArvppYqrpinmmFQS 99
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEVA----Y-------FDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 Y--ALFPHMTVEQNIAFGlkqdrlpKAEITARVQEMLALVHMQEF------AKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK11147 390 HraELDPEKTVMDNLAEG-------KQEVMVNGRPRHVLGYLQDFlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1616137381 172 LLDEPMGALDkklrdrmqLEVVDILERV-----GvTCVMVTHDQE 211
Cdd:PRK11147 463 ILDEPTNDLD--------VETLELLEELldsyqG-TVLLVSHDRQ 498
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
30-209 |
2.39e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPyQRPINMMFQSYAL---FPhM 106
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-KNLVAYVPQSEEVdwsFP-V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 107 TVEQNIAFG----LKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
Cdd:PRK15056 96 LVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*..
gi 1616137381 183 KLRDRMqLEVVDILERVGVTCVMVTHD 209
Cdd:PRK15056 176 KTEARI-ISLLRELRDEGKTMLVSTHN 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-237 |
1.27e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.57 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTA-------GQIMLDGVDLARVPPYQ 90
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 ---RPINMMFQSYALFPhMTVEQNIAFGlkqdRLPKA----EITARVQEM----LALVHMQEFAKRKPRQLSGGQRQRVA 159
Cdd:PRK13547 81 larLRAVLPQAAQPAFA-FSAREIVLLG----RYPHArragALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 160 LARSLAK---------RPKLLLLDEPMGALDKKLRDRMqLEVVDILER---VGVtcVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK13547 156 FARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRL-LDTVRRLARdwnLGV--LAIVHDPNLAARHADRIAMLADGA 232
|
250
....*....|
gi 1616137381 228 FVQIGEPEEI 237
Cdd:PRK13547 233 IVAHGAPADV 242
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-209 |
1.93e-19 |
|
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: 86.69 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 41 TIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYqrpINMMFQsyalfphMTVEQ---NIAFGLK 117
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY---IKADYE-------GTVRDllsSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 118 QDRLPKAEITARVQemlalvhMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILE 197
Cdd:cd03237 91 THPYFKTEIAKPLQ-------IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170
....*....|..
gi 1616137381 198 RVGVTCVMVTHD 209
Cdd:cd03237 164 NNEKTAFVVEHD 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-232 |
2.66e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.07 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LARVPPYQRPI 93
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 174 DEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:TIGR01257 2095 DEPTTGMDPQAR-RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-228 |
2.75e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTksfdGQHAVDdVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQR----- 91
Cdd:PRK15439 266 APVLTVEDLT----GEGFRN-ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlargl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 ---PINMmfQSYALFPHMTVEQNIAfGLKQDRLPKAEITARVQEMLALVHMQ-----EFAKRKPRQLSGGQRQRVALARS 163
Cdd:PRK15439 341 vylPEDR--QSSGLYLDAPLAWNVC-ALTHNRRGFWIKPARENAVLERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 164 LAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARN----DIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-233 |
3.00e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.91 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPP---YQRPI 93
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNI--------AFGlkqdRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLA 165
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIflgrefvnRFG----RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 166 KRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFvqIGE 233
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESL-FRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IAE 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-209 |
4.10e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 88.71 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPQAKAPkaltPLLEIRNLTKSFDgqhavdDVSL-----TIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDg 80
Cdd:PRK13409 331 PRDESERE----TLVEYPDLTKKLG------DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 81 VDLARVPPYQRPInmmfqsyalfPHMTVEQNI-----AFGlkqDRLPKAEITARvqemLALVHMQEfakRKPRQLSGGQR 155
Cdd:PRK13409 400 LKISYKPQYIKPD----------YDGTVEDLLrsitdDLG---SSYYKSEIIKP----LQLERLLD---KNVKDLSGGEL 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRdrmqLEVVDILERV----GVTCVMVTHD 209
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQR----LAVAKAIRRIaeerEATALVVDHD 513
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-250 |
5.60e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLARVPpyqrpin 94
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYVP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 mmfQSYALFPHM--TVEQNIAF--GLK-QDRLPKAEitaRVQEmlalVHMQEFAKRKprqLSGGQRQRVALARSLAKRPK 169
Cdd:PRK09544 74 ---QKLYLDTTLplTVNRFLRLrpGTKkEDILPALK---RVQA----GHLIDAPMQK---LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 170 LLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEIYEHPttry 245
Cdd:PRK09544 141 LLVLDEPTQGVDVN----GQVALYDLIDQLrrelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP---- 211
|
....*
gi 1616137381 246 saEFI 250
Cdd:PRK09544 212 --EFI 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-227 |
7.20e-19 |
|
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: 88.07 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlarvPPYQrpINMMFQSY 100
Cdd:TIGR03719 7 MNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIK--VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 ALFPHMTVEQNIAFGL-----KQDRL---------PKAEITARVQEMLAL---------------VHMQEFAKRKP---- 147
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVaeikdALDRFneisakyaePDADFDKLAAEQAELqeiidaadawdldsqLEIAMDALRCPpwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 148 --RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILERV-----GvTCVMVTHDQEEAMTMAGRI 220
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA--------ESVAWLERHlqeypG-TVVAVTHDRYFLDNVAGWI 228
|
....*..
gi 1616137381 221 AIMNRGK 227
Cdd:TIGR03719 229 LELDRGR 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-209 |
1.28e-18 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 87.15 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGqhavddVSLT-----IYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVDLARVPPYQRP 92
Cdd:COG1245 340 TLVEYPDLTKSYGG------FSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 INmmfqsyalfpHMTVEQNIAFGLKqDRLP----KAEITARvqemLALVHMQEfakRKPRQLSGGQRQRVALARSLAKRP 168
Cdd:COG1245 413 DY----------DGTVEEFLRSANT-DDFGssyyKTEIIKP----LGLEKLLD---KNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1616137381 169 KLLLLDEPMGALDkkLRDRMqlEVVDILERV----GVTCVMVTHD 209
Cdd:COG1245 475 DLYLLDEPSAHLD--VEQRL--AVAKAIRRFaenrGKTAMVVDHD 515
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-227 |
1.80e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 6 PRPQAKApkaltpLLEIRNLtksfDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLar 85
Cdd:PRK11288 250 PRPLGEV------RLRLDGL----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 86 vpPYQRPINMMFQSYAL----------FPHMTVEQNIAFGLKQDRLPKAEITARVQEM-LALVHMQEFAKRKP------R 148
Cdd:PRK11288 318 --DIRSPRDAIRAGIMLcpedrkaegiIPVHSVADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIKTPsreqliM 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH----EIYNViyeLAAQGVAVLFVSSDLPEVLGVADRIVVMRE 471
|
..
gi 1616137381 226 GK 227
Cdd:PRK11288 472 GR 473
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
295-375 |
2.54e-18 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 78.43 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 295 VALRPEKIMLcdeppADGYNFAVGEVIHIAYLGDLSIYHVRLQSGQMISAQLQNEHRHRkgtPTWGDEVRLCWDADSCVV 374
Cdd:pfam08402 1 LAIRPEKIRL-----AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARP---PAPGDRVGLGWDPEDAHV 72
|
.
gi 1616137381 375 L 375
Cdd:pfam08402 73 L 73
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-208 |
3.07e-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: 81.05 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLT-KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLARVPpyQRPinmmf 97
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLLFLP--QRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 qsYalFPHMTVEQNIAFglkqdrlpkaeitarvqemlalvhmqefakrkP--RQLSGGQRQRVALARSLAKRPKLLLLDE 175
Cdd:cd03223 74 --Y--LPLGTLREQLIY--------------------------------PwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 1616137381 176 PMGALDKKLRDRMqlevVDILERVGVTCVMVTH 208
Cdd:cd03223 118 ATSALDEESEDRL----YQLLKELGITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-175 |
6.06e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 85.23 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPLLEIRNLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
Cdd:COG4615 311 PAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 78 LDG--VDLARVPPYQRPINMMFQSYALFPHMtveqniaFGLKQDRLPkaeitARVQEMLALVHMQE---FAKRK--PRQL 150
Cdd:COG4615 391 LDGqpVTADNREAYRQLFSAVFSDFHLFDRL-------LGLDGEADP-----ARARELLERLELDHkvsVEDGRfsTTDL 458
|
170 180
....*....|....*....|....*.
gi 1616137381 151 SGGQRQRVALARSLA-KRPkLLLLDE 175
Cdd:COG4615 459 SQGQRKRLALLVALLeDRP-ILVFDE 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-237 |
7.96e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 83.63 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCG--KSTLLRMLAGfeqPTAGQ-------IMLDGVDLARVPPYQ 90
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrf*tWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 91 RPINMMFQSyalfpHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKL 170
Cdd:NF000106 91 RPVR*GRRE-----SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 171 LLLDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-227 |
9.69e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSfdgqhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQRPIN-MMFQ 98
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SY-----ALFPHMTVEQNIA------FGLKQDRLPKAEITARVQEMLALvhmqeFAKRKPRQ------LSGGQRQRVALA 161
Cdd:PRK10762 333 SEdrkrdGLVLGMSVKENMSltalryFSRAGGSLKHADEQQAVSDFIRL-----FNIKTPSMeqaiglLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 162 RSLAKRPKLLLLDEPMGALD---KKlrdrmqlEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDvgaKK-------EIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-186 |
1.21e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 80.30 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP-PYQRPINmmfQSYALFPHMTVEQNIAFG 115
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYCTYIG---HNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 116 lkqdrlpkAEITARVQEMLALVH---MQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
Cdd:PRK13541 95 --------SEIYNSAETLYAAIHyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-183 |
1.58e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.99 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR-VPPYQRPINMMF 97
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHMTVEQNIAFGLKqdrlpKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIH-----FSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....*.
gi 1616137381 178 GALDKK 183
Cdd:PRK13540 156 VALDEL 161
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-234 |
7.99e-17 |
|
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: 78.22 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVP--PYQRPINM 95
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 96 MFQSYALFPHmTVEQNIAfglKQDRLPKAEITA--RVQEmlalvhmqefakrKPRQLSGGQRQRVALARSLAKRPKLLLL 173
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLD---PFDEYSDEEIYGalRVSE-------------GGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 174 DEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEP 234
Cdd:cd03369 150 DEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-208 |
1.08e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT--AGQIMLDGVDLARvpPYQRPINMMFQS 99
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK--QILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 100 YALFPHMTVEQNIAFgLKQDRLPKAeITARVQEMLALVHMQEFAKRK----------PRQLSGGQRQRVALARSLAKRPK 169
Cdd:PLN03211 149 DILYPHLTVRETLVF-CSLLRLPKS-LTKQEKILVAESVISELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190
....*....|....*....|....*....|....*....
gi 1616137381 170 LLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTH 208
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-209 |
2.10e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.55 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 23 RNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARVPpyQRPinmmfqsy 100
Cdd:PRK11819 10 NRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYLP--QEP-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 101 ALFPHMTVEQNIAFGL-----KQDRL---------PKAEITARVQEMLALvhmQEF------------------AKRKP- 147
Cdd:PRK11819 80 QLDPEKTVRENVEEGVaevkaALDRFneiyaayaePDADFDALAAEQGEL---QEIidaadawdldsqleiamdALRCPp 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 148 -----RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdrmqlEVVDILERV-----GvTCVMVTHD 209
Cdd:PRK11819 157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------ESVAWLEQFlhdypG-TVVAVTHD 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
35-226 |
3.49e-16 |
|
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: 76.60 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-DLARVPPYQRPINMMFQSYA----LFPHMTVE 109
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAaqkpWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 110 QNIAFG--LKQDRLPKAEITARVQ---EMLALVHMQEFAKRKPrQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
Cdd:cd03290 97 ENITFGspFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1616137381 185 RDR-MQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRG 226
Cdd:cd03290 176 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-181 |
4.63e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.43 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 5 MPRPQAKAPkaltPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA 84
Cdd:PRK13543 1 MIEPLHTAP----PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 85 RVppyQRPINMMFQSY--ALFPHMTVEQNIAF-----GLKQDRLPKAEitarvqemLALVHMQEFAKRKPRQLSGGQRQR 157
Cdd:PRK13543 77 RG---DRSRFMAYLGHlpGLKADLSTLENLHFlcglhGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKR 145
|
170 180
....*....|....*....|....
gi 1616137381 158 VALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-176 |
5.80e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.40 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA------RVPPYqrpIN 94
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarhrrAVCPR---IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSYA--LFPHMTVEQNIAF-GlkqdRL---PKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRP 168
Cdd:NF033858 80 YMPQGLGknLYPTLSVFENLDFfG----RLfgqDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
....*...
gi 1616137381 169 KLLLLDEP 176
Cdd:NF033858 156 DLLILDEP 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-231 |
5.81e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDGQhaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY---QRPIN 94
Cdd:PRK09700 264 TVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQSY---ALFPHMTVEQNIAFG--LKQDRL--------PKAE--ITARVQEMLAL-VHMQEfakRKPRQLSGGQRQRV 158
Cdd:PRK09700 342 YITESRrdnGFFPNFSIAQNMAISrsLKDGGYkgamglfhEVDEqrTAENQRELLALkCHSVN---QNITELSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-239 |
6.46e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.99 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 3 DVMPRPQAKAPKALTPL----LEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
Cdd:PRK10790 320 ELMDGPRQQYGNDDRPLqsgrIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 78 LDGvdlarvppyqRPInmmfqsyALFPHMTVEQNIAFgLKQDRLPKAE-----IT-------ARVQEMLALVHMQEFAKR 145
Cdd:PRK10790 400 LDG----------RPL-------SSLSHSVLRQGVAM-VQQDPVVLADtflanVTlgrdiseEQVWQALETVQLAELARS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 146 KP-----------RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAM 214
Cdd:PRK10790 462 LPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTI 538
|
250 260
....*....|....*....|....*
gi 1616137381 215 TMAGRIAIMNRGKFVQIGEPEEIYE 239
Cdd:PRK10790 539 VEADTILVLHRGQAVEQGTHQQLLA 563
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-227 |
1.03e-15 |
|
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: 78.33 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTK-SFDGQHA--VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIMLDGVDLARVPPYQ---R 91
Cdd:TIGR02633 257 ILEARNLTCwDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAQairA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQS---YALFPHMTVEQNIAFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPR------QLSGGQRQRVALAR 162
Cdd:TIGR02633 337 GIAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 163 SLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
33-240 |
1.21e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 76.01 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlarvppyqrPINMMFQSYALFPHMTVEQNI 112
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 113 AFGLKQDRLPKAEITARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1616137381 193 VDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13546 187 YEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-229 |
1.89e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.46 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---ARVPPYQRPINMMFQ 98
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTVEQNIAFGlkqdRLPKAEITARVQEM-------LALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLL 171
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLG----RYPTKGMFVDQDKMyrdtkaiFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHL-FTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
73-237 |
3.48e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 73 AGQIMLDGVDLA--RVPPYQRPINMMFQSYALFpHMTVEQNIAFGlKQDrlPKAEITARVQEMLALvhmQEFAKRKPRQ- 149
Cdd:PTZ00265 1276 SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG-KED--ATREDVKRACKFAAI---DEFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 150 ----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGR 219
Cdd:PTZ00265 1349 dtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|...
gi 1616137381 220 IAIMNR----GKFVQI-GEPEEI 237
Cdd:PTZ00265 1428 IVVFNNpdrtGSFVQAhGTHEEL 1450
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
37-263 |
4.04e-15 |
|
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: 74.89 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlarvppyqrPINMMFQSYALFPHmTVEQNIAFGL 116
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 117 KQDRLpkaeitaRVQEMLALVHMQEFAKRKPRQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALD---- 181
Cdd:cd03291 123 SYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfte 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 182 KKLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIyEHPTTRYSAEFIGsVNVFEGLVK 261
Cdd:cd03291 196 KEIFESCVCKLMANKTRILVTSKM------EHLKKADKILILHEGSSYFYGTFSEL-QSLRPDFSSKLMG-YDTFDQFSA 267
|
..
gi 1616137381 262 ER 263
Cdd:cd03291 268 ER 269
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-181 |
1.11e-14 |
|
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: 71.91 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG----FEQPTaGQIMLDGVDLAR-VPPYQRPINMM 96
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPYKEfAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 FQSYALFPHMTVEQNIAFGLKqdrlpkaeitARVQEMLalvhmqefakrkpRQLSGGQRQRVALARSLAKRPKLLLLDEP 176
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALR----------CKGNEFV-------------RGISGGERKRVSIAEALVSRASVLCWDNS 145
|
....*
gi 1616137381 177 MGALD 181
Cdd:cd03233 146 TRGLD 150
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
37-288 |
1.32e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 75.72 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlarvppyqrPINMMFQSYALFPHmTVEQNIAFGL 116
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQTSWIMPG-TIKDNIIFGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 117 KQDRLpkaeitaRVQEMLALVHMQEFAKRKPRQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALD---- 181
Cdd:TIGR01271 512 SYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvte 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 182 KKLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIY-EHPTtrYSAEFIGSVNvFEGLV 260
Cdd:TIGR01271 585 KEIFESCLCKLMSNKTRILVTSKL------EHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEA-FDNFS 655
|
250 260
....*....|....*....|....*...
gi 1616137381 261 KERLEDGLVLSspglMHPLKVDPDASVV 288
Cdd:TIGR01271 656 AERRNSILTET----LRRVSIDGDSTVF 679
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-268 |
1.80e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR--VPPYQRPINMMFQSYALFPHmTVEQNI-AF 114
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFNIdPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 115 GLKQDrlpkaeitARVQEMLALVHMQEFAKRKP-----------RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:PLN03232 1334 SEHND--------ADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 184 LRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS--AEFIGSVNV--FEGL 259
Cdd:PLN03232 1406 TDSLIQRTIRE--EFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFrmVHSTGPANAqyLSNL 1482
|
....*....
gi 1616137381 260 VKERLEDGL 268
Cdd:PLN03232 1483 VFERRENGM 1491
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-220 |
2.53e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.16 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvDLARVPPYQRPINMMF-Q 98
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENANIGYYAQDHAYDFeN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 99 SYALFPHMTveqniafglkQDRLPKAEITArVQEMLA-LVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
Cdd:PRK15064 398 DLTLFDWMS----------QWRQEGDDEQA-VRGTLGrLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1616137381 178 GALDkklrdrMQ-LEVVDI-LERVGVTCVMVTHDQEEAMTMAGRI 220
Cdd:PRK15064 467 NHMD------MEsIESLNMaLEKYEGTLIFVSHDREFVSSLATRI 505
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-235 |
2.82e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.98 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLARVPPYQRP-- 92
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 93 -INMMFQSYALFPHMTVEQ--NIAFGLKQDRLPKAEITA-----RVQEMLALVHMQE-FAKRKPRQ-LSGGQRQRVALAR 162
Cdd:CHL00131 85 gIFLAFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDPlefleIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 163 SLAKRPKLLLLDEPMGALDKklrDRMQL--EVVDILERVGVTCVMVTHDQeeamtmagR---------IAIMNRGKFVQI 231
Cdd:CHL00131 165 MALLDSELAILDETDSGLDI---DALKIiaEGINKLMTSENSIILITHYQ--------RlldyikpdyVHVMQNGKIIKT 233
|
....
gi 1616137381 232 GEPE 235
Cdd:CHL00131 234 GDAE 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-210 |
3.76e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 73.67 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 11 KAPKAL-TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARVPP 88
Cdd:PRK10636 303 RAPESLpNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 YQ----RPINMMFQSYALFPHMTVEQNI-----AFGLKQDRLpkAEITARvqemlalvhmqefakrkprqLSGGQRQRVA 159
Cdd:PRK10636 383 HQleflRADESPLQHLARLAPQELEQKLrdylgGFGFQGDKV--TEETRR--------------------FSGGEKARLV 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvtcVMVTHDQ 210
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDR 487
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-181 |
3.87e-14 |
|
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: 70.35 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP--TAGQIMLDGvdLARVPPYQRPINMMFQSYALFPHMTVEQNIA 113
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILING--RPLDKNFQRSTGYVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 114 FGlkqdrlpkaeitarvqemlALVhmqefakrkpRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:cd03232 102 FS-------------------ALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
37-246 |
4.85e-14 |
|
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: 73.83 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY--QRPINMMFQSYALFPHmTVEQNI-A 113
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdlRFKITIIPQDPVLFSG-SLRMNLdP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 114 FGLKQDRlpkaeitaRVQEMLALVHMQEFAKRKP-----------RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
Cdd:TIGR00957 1383 FSQYSDE--------EVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 183 KLRDRMQLEVVDILErvgvTCVMVT--HDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFE----DCTVLTiaHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
37-241 |
5.41e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLARVPpyQRPINMmfqsyalfpHMTVEQNIAFGL 116
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-SIAYVP--QQAWIM---------NATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 117 KQD--RLPKAEITARVQEMLALVH--MQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:PTZ00243 746 EEDaaRLADAVRVSQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1616137381 193 vdILERV-GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PTZ00243 826 --FLGALaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-229 |
1.45e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQP-TAGQIMLDG-VDLARV---PP----- 88
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIYEQdLIVARLqqdPPrnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 89 -------------------YQRPINMMFQSYAlfphmtvEQNIA-FGLKQDRLPKA---EITARVQEMLALVHMQefAKR 145
Cdd:PRK11147 82 tvydfvaegieeqaeylkrYHDISHLVETDPS-------EKNLNeLAKLQEQLDHHnlwQLENRINEVLAQLGLD--PDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 146 KPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIA 221
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--------IETIEWLEGFlktfQGSIIFISHDRSFIRNMATRIV 224
|
....*...
gi 1616137381 222 IMNRGKFV 229
Cdd:PRK11147 225 DLDRGKLV 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-241 |
1.58e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLA--RVPPYQRPINMMFQSYALFPHmTVEQN 111
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 112 IAFGLKQDRLPKAEITARvqemLALVHmqEFAKRKPR-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
Cdd:PRK10789 409 IALGRPDATQQEIEHVAR----LASVH--DDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 181 DkklrDRMQLEVVDILERVGVT-CVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
Cdd:PRK10789 483 D----GRTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-237 |
1.81e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLARVPpyqrpinmmfqSYALFPHMTVEQNIAFGlK 117
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVP-----------QQAWIQNDSLRENILFG-K 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 118 QDRLPKAEITARVQEMLALVHMQEFAKR-----KPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1616137381 193 V---DILErvGVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:TIGR00957 804 IgpeGVLK--NKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-237 |
2.10e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.12 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgvdlaRVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQ 118
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---------RQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 119 DR----LPKAEI-------TARVQEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDR 187
Cdd:PRK10938 94 GEddtgRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD--VASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 188 MQL-EVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PRK10938 172 QQLaELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-183 |
2.36e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLARV--PPYQRPI 93
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDInlKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHmTVEQNIAFGL-------------------KQDRLPK-----AEITARVQEML------ALVHMQ--- 140
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndSQENKNKrnscrAKCAGDLNDMSnttdsnELIEMRkny 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 141 ------------------EFAKRKP-----------RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
Cdd:PTZ00265 542 qtikdsevvdvskkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-217 |
3.35e-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: 63.55 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 44 KGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARvppyqrpinmmfqsyalfphmtveqniafglkqdrlpk 123
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 124 aeitarvqEMLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVD-----ILER 198
Cdd:smart00382 43 --------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLKSE 114
|
170
....*....|....*....
gi 1616137381 199 VGVTCVMVTHDQEEAMTMA 217
Cdd:smart00382 115 KNLTVILTTNDEKDLGPAL 133
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
36-181 |
9.11e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAgfEQPTAGqIMLDGVDLARVPP----YQRPINMMFQSYALFPHMTVEQN 111
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVNGRPldssFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 112 IAFG--LKQ-DRLPKAEITARVQEMLALVHMQEFAKR----KPRQLSGGQRQRVALARSLAKRPKLLL-LDEPMGALD 181
Cdd:TIGR00956 857 LRFSayLRQpKSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-227 |
3.03e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTkSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIMLDGVDLARVPPYQ---R 91
Cdd:PRK13549 260 LEVRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQaiaQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQS---YALFPHMTVEQNIAFGLkQDRLPKAeitARVQEMLALVHMQEFAKR------KPRQ----LSGGQRQRV 158
Cdd:PRK13549 339 GIAMVPEDrkrDGIVPVMGVGKNITLAA-LDRFTGG---SRIDDAAELKTILESIQRlkvktaSPELaiarLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 159 ALARSLAKRPKLLLLDEPMGALD-------KKLrdrmqlevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDvgakyeiYKL--------INQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-181 |
3.78e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA--------------GFEQPTAG------QIMLD 79
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilHVEQEVVGddttalQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 80 gVDLARVPPYQRPINMMFQSYAL-FPHMTVEQNIAF--GLKQDRLPK--AEI------------TARVQEMLA-LVHMQE 141
Cdd:PLN03073 258 -TDIERTQLLEEEAQLVAQQRELeFETETGKGKGANkdGVDKDAVSQrlEEIykrlelidaytaEARAASILAgLSFTPE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1616137381 142 FAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-237 |
3.90e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR--VPPYQRPINMMFQSYALFPHmTVEQNI-AF 114
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfgLMDLRKVLGIIPQAPVLFSG-TVRFNLdPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 115 GLKQDrlpkaeitARVQEMLALVHMQEFAKRKPRQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALD-- 181
Cdd:PLN03130 1337 NEHND--------ADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDvr 1408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 182 ------KKLRDRMQlevvdilervgvTCVM--VTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PLN03130 1409 tdaliqKTIREEFK------------SCTMliIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-181 |
4.22e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPTAGQIMLDGVDLARVPPYQRP---I 93
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgegI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQ--------SYALFPHMTVEQNIAFgLKQDRLPKAEITARVQEMLALVHMQE--FAKRKPRQLSGGQRQRVALARS 163
Cdd:PRK09580 81 FMAFQypveipgvSNQFFLQTALNAVRSY-RGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQM 159
|
170
....*....|....*...
gi 1616137381 164 LAKRPKLLLLDEPMGALD 181
Cdd:PRK09580 160 AVLEPELCILDESDSGLD 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-213 |
9.30e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 5 MPRPQAKAPKAL------TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIM 77
Cdd:PRK10938 240 VQLPEPDEPSARhalpanEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 78 LDGV---------DLARvppyqrpiNMMFQSYALfpHM------TVEQNI------AFGLKQ---DRLPKaeitaRVQEM 133
Cdd:PRK10938 320 LFGRrrgsgetiwDIKK--------HIGYVSSSL--HLdyrvstSVRNVIlsgffdSIGIYQavsDRQQK-----LAQQW 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 134 LALVHMQEFAKRKP-RQLSGGQrQRVAL-ARSLAKRPKLLLLDEPMGALD---KKLRDRMqlevVDILERVGVTCVM-VT 207
Cdd:PRK10938 385 LDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDplnRQLVRRF----VDVLISEGETQLLfVS 459
|
....*.
gi 1616137381 208 HDQEEA 213
Cdd:PRK10938 460 HHAEDA 465
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
49-210 |
1.12e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIM--------------LDGVDLArvppyQRPINMMFQSYALFPHMTVEQNI-A 113
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLS-----SNPLLYMMRCFPGVPEQKLRAHLgS 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 114 FGLKQDrlpkaeitarvqemLALVHMQefakrkprQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVV 193
Cdd:PLN03073 614 FGVTGN--------------LALQPMY--------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD--------LDAV 663
|
170 180
....*....|....*....|...
gi 1616137381 194 D------ILERVGVtcVMVTHDQ 210
Cdd:PLN03073 664 EaliqglVLFQGGV--LMVSHDE 684
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-230 |
1.27e-10 |
|
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: 61.41 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLT-KSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGVDLARVP--PYQR 91
Cdd:cd03289 3 MTVKDLTaKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPlqKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHmTVEQNI-AFGLKQDRlpkaEITARVQEmlalVHMQEFAKRKPRQ-----------LSGGQRQRVA 159
Cdd:cd03289 78 AFGVIPQKVFIFSG-TFRKNLdPYGKWSDE----EIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDKklrdrMQLEVV-DILERVGVTC-VMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDP-----ITYQVIrKTLKQAFADCtVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-240 |
1.99e-10 |
|
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: 60.69 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqptaGQIMLDGVDLARVPPY--QR 91
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFphmtvEQNIAFGLKqdrlPKAEIT-ARVQEMLALVHMQEFAKRKPRQL-----------SGGQRQRVA 159
Cdd:cd03288 96 RLSIILQDPILF-----SGSIRFNLD----PECKCTdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 160 LARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGRIA---------IMNRGKFVQ 230
Cdd:cd03288 167 LARAFVRKSSILIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRVStildadlvlVLSRGILVE 234
|
250
....*....|
gi 1616137381 231 IGEPEEIYEH 240
Cdd:cd03288 235 CDTPENLLAQ 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-242 |
3.14e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 17 TPLLEIRNLTKSFDGQHA---VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQimlDGVDLARVPPYQRPI 93
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAET---SSVVIRGSVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSyalfphmTVEQNIAFG--LKQDRLPKAEITARVQEMLALVHMQEFAKRKPR--QLSGGQRQRVALARSLAKRPK 169
Cdd:PLN03232 688 SWIFNA-------TVRENILFGsdFESERYWRAIDVTALQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 170 LLLLDEPMGALDKKLRDRMQLEVVDiLERVGVTCVMVThDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-209 |
5.27e-10 |
|
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: 58.10 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLrmLAGFEqpTAGQIMLdgVDLARVPPYQrPINMMFQSYALfphmtveqn 111
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLY--ASGKARL--ISFLPKFSRN-KLIFIDQLQFL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 112 IAFGLkqdrlpkaeitarvqEMLALvhmqefaKRKPRQLSGGQRQRVALARSLAKRPK--LLLLDEPMGALDKKLRDRMq 189
Cdd:cd03238 72 IDVGL---------------GYLTL-------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL- 128
|
170 180
....*....|....*....|
gi 1616137381 190 LEVVDILERVGVTCVMVTHD 209
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHN 148
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-181 |
5.88e-10 |
|
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: 61.08 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGV--DLARVPPYQR 91
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDGVswNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 92 PINMMFQSYALFPHmTVEQNIAfglKQDRLPKAEITaRVQEMLALVHM-QEFAKRKPRQ-------LSGGQRQRVALARS 163
Cdd:TIGR01271 1293 AFGVIPQKVFIFSG-TFRKNLD---PYEQWSDEEIW-KVAEEVGLKSViEQFPDKLDFVlvdggyvLSNGHKQLMCLARS 1367
|
170
....*....|....*...
gi 1616137381 164 LAKRPKLLLLDEPMGALD 181
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD 1385
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
31-208 |
6.49e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.53 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG-VDLARVPpyQRPI--NMMFQSYALFPhMT 107
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkGKLFYVP--QRPYmtLGTLRDQIIYP-DS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 108 VEQNIAFGLKQDRLpkaeitarvQEMLALVHMQEFAKRK---------PRQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
Cdd:TIGR00954 541 SEDMKRRGLSDKDL---------EQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 1616137381 179 ALDKKLRDRMqlevVDILERVGVTCVMVTH 208
Cdd:TIGR00954 612 AVSVDVEGYM----YRLCREFGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
42-222 |
9.71e-10 |
|
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: 57.20 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 42 IYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPYQrpinmmfqsyalfphmtveqniafglkqdrl 121
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 122 pkaeitarvqemlalvhmqefakrkprQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGV 201
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 1616137381 202 TCVMVTHDQEEAMTMAGRIAI 222
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-237 |
1.41e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PLLEIRNLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTA-GQIMLDGvDLARVPPyqrpI 93
Cdd:PLN03130 613 PAISIKNGYFSWDSkaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG-TVAYVPQ----V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSyalfphmTVEQNIAFGL--KQDRLPKAEITARVQEMLALV---HMQEFAKRKPrQLSGGQRQRVALARSLAKRP 168
Cdd:PLN03130 688 SWIFNA-------TVRDNILFGSpfDPERYERAIDVTALQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 169 KLLLLDEPMGALD---------KKLRDRMQlevvdilervGVTCVMVThDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
Cdd:PLN03130 760 DVYIFDDPLSALDahvgrqvfdKCIKDELR----------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-211 |
2.67e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLTKSFdgqhaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-DLARV----PPYQRP-I 93
Cdd:PRK10636 7 LQIRRGVRVL-----LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVnqetPALPQPaL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 94 NMMFQSYALFPHMTVEQNIA-----------FGLKQDRLPKAEITARVQEML-ALVHMQEFAKRKPRQLSGGQRQRVALA 161
Cdd:PRK10636 82 EYVIDGDREYRQLEAQLHDAnerndghaiatIHGKLDAIDAWTIRSRAASLLhGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 162 RSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILER----VGVTCVMVTHDQE 211
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD--------LDAVIWLEKwlksYQGTLILISHDRD 207
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-250 |
2.81e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 13 PKALTP---LLEIRNLTKSfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLARVPPY 89
Cdd:PRK10982 241 DKENKPgevILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 90 QrPINMMF-------QSYALFPHMTVEQN--IA--------FGLKQDRLPKAEITARVQEMLALVHMQefaKRKPRQLSG 152
Cdd:PRK10982 319 E-AINHGFalvteerRSTGIYAYLDIGFNslISnirnyknkVGLLDNSRMKSDTQWVIDSMRVKTPGH---RTQIGSLSG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDiLERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE-LAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIV 473
|
250
....*....|....*...
gi 1616137381 233 EPEEIYEHPTTRYSAEFI 250
Cdd:PRK10982 474 DTKTTTQNEILRLASLHL 491
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-209 |
3.87e-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: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 44 KGEIFALLGASGCGKSTLLRMLAGFEQPTAGqimldgvDLARVPPYQRPINMmFQSYALFPHMT--VEQNIAFGLK-Q-- 118
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDEVLKR-FRGTELQDYFKklANGEIKVAHKpQyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 119 DRLPKA------EITARVQE-----MLA-LVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
Cdd:COG1245 170 DLIPKVfkgtvrELLEKVDErgkldELAeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180
....*....|....*....|...
gi 1616137381 187 RMQlEVVDILERVGVTCVMVTHD 209
Cdd:COG1245 250 NVA-RLIRELAEEGKYVLVVEHD 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-181 |
6.89e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 15 ALTPLLEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLA----GFEQPTAGQIMLDGVDLAR-V 86
Cdd:TIGR00956 54 LLKILTRGFRKLKKFRDTKTFDilkPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEiK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 87 PPYQRPINMMFQSYALFPHMTVEQNIAFGLKQ----------DRLPKAE-ITARVQEMLALVHMQ------EFAkrkpRQ 149
Cdd:TIGR00956 134 KHYRGDVVYNAETDVHFPHLTVGETLDFAARCktpqnrpdgvSREEYAKhIADVYMATYGLSHTRntkvgnDFV----RG 209
|
170 180 190
....*....|....*....|....*....|..
gi 1616137381 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-209 |
8.41e-09 |
|
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: 55.84 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQimLDGvdlarvPPYQRPINMMFQSYALFPHMT--VEQNIAFGLKQ---D 119
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDD------PPDWDEILDEFRGSELQNYFTklLEGDVKVIVKPqyvD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 120 RLPKAeITARVQEMLALVHMQEF-------------AKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
Cdd:cd03236 98 LIPKA-VKGKVGELLKKKDERGKldelvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 1616137381 187 RMQlEVVDILERVGVTCVMVTHD 209
Cdd:cd03236 177 NAA-RLIRELAEDDNYVLVVEHD 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-240 |
2.19e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 27 KSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlarvppyqrPINMMFQSYALFP 104
Cdd:PRK13545 30 RSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 105 HMTVEQNIAF-----GLKQDRLpkAEITARVQEmlaLVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
Cdd:PRK13545 99 QLTGIENIELkglmmGLTKEKI--KEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 180 LDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
Cdd:PRK13545 174 GDQTFTKKC-LDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-181 |
3.03e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLARVPPYQ------RPIN-- 94
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQfafeefTVLDtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 95 MMFQS------------YALfPHMTVEQniafGLKQDRLP---------KAEitARVQEMLALV------H---MQEFAk 144
Cdd:PRK15064 86 IMGHTelwevkqerdriYAL-PEMSEED----GMKVADLEvkfaemdgyTAE--ARAGELLLGVgipeeqHyglMSEVA- 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1616137381 145 rkPrqlsgGQRQRVALARSLAKRPKLLLLDEPMGALD 181
Cdd:PRK15064 158 --P-----GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
18-223 |
3.84e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 50.35 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 18 PL-LEIRNLTkSFDGQHAVDDVSLTiyKGEIFALLGASGCGKSTLLR--MLAGFEQPTA--GQIMLDGV-----DLARVP 87
Cdd:cd03279 3 PLkLELKNFG-PFREEQVIDFTGLD--NNGLFLICGPTGAGKSTILDaiTYALYGKTPRygRQENLRSVfapgeDTAEVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 88 PYqrpinmmFQ----SYALF--PHMTVEQ--NIAFglkqdrLPKAEItarvqemlalvhmQEFAKRKPRQLSGGQRQRVA 159
Cdd:cd03279 80 FT-------FQlggkKYRVErsRGLDYDQftRIVL------LPQGEF-------------DRFLARPVSTLSGGETFLAS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 160 LARSLA----------KRPKLLLLDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
Cdd:cd03279 134 LSLALAlsevlqnrggARLEALFIDEGFGTLDPEALEAVA-TALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-209 |
4.35e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 44 KGEIFALLGASGCGKSTLLRMLAGFEQPTAGqimldgvDLARVPPYQRPINMmFQSYALFPHMT--VEQNIAFGLK-Q-- 118
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG-------DYEEEPSWDEVLKR-FRGTELQNYFKklYNGEIKVVHKpQyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 119 DRLPKA------EITARVQE------MLALVHMQEFAKRKPRQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRD 186
Cdd:PRK13409 170 DLIPKVfkgkvrELLKKVDErgkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQ 247
|
170 180
....*....|....*....|....*
gi 1616137381 187 RMqlEVVDILERV--GVTCVMVTHD 209
Cdd:PRK13409 248 RL--NVARLIRELaeGKYVLVVEHD 270
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-261 |
2.16e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeQPTAGQIMLDgVDLARVPPYQ----RPINMMFQSYALFPHMTVEQNI 112
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPKKQetfaRISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 113 AFGLKQdRLPKaEITA--------RVQEMLALVHMQEFAKRKP--RQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
Cdd:PLN03140 975 IYSAFL-RLPK-EVSKeekmmfvdEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 183 K---LRDRMQLEVVDilerVGVTCVMVTH----DQEEAMTmagRIAIMNRGKFVqigepeeIYEHPTTRYSAEFIGSVNV 255
Cdd:PLN03140 1053 RaaaIVMRTVRNTVD----TGRTVVCTIHqpsiDIFEAFD---ELLLMKRGGQV-------IYSGPLGRNSHKIIEYFEA 1118
|
....*.
gi 1616137381 256 FEGLVK 261
Cdd:PLN03140 1119 IPGVPK 1124
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-233 |
2.65e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 13 PKALTPLLEIRNLTkSFDGQHA----VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDG--VDLA 84
Cdd:NF040905 251 PKIGEVVFEVKNWT-VYHPLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGkeVDVS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 85 RVPpyqRPINMMF-------QSYALFPHMTVEQNI-AFGLKqdRLPKAEITARVQEMLAlvhMQEFAKR----------K 146
Cdd:NF040905 330 TVS---DAIDAGLayvtedrKGYGLNLIDDIKRNItLANLG--KVSRRGVIDENEEIKV---AEEYRKKmniktpsvfqK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 147 PRQLSGGQRQRVALARSLAKRPKLLLLDEP-----MGAldkklrdrmQLEVVDILERV---GVTCVMVTHDQEEAMTMAG 218
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELLGMCD 472
|
250
....*....|....*
gi 1616137381 219 RIAIMNRGKFVqiGE 233
Cdd:NF040905 473 RIYVMNEGRIT--GE 485
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
20-211 |
2.96e-06 |
|
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: 47.60 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLtKSFDgqhavDDVSLTIYKGeIFALLGASGCGKSTLLrmlagfeqptagqimlDGVDLA---RVPPYQRpinmm 96
Cdd:cd03240 4 LSIRNI-RSFH-----ERSEIEFFSP-LTLIVGQNGAGKTTII----------------EALKYAltgELPPNSK----- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 97 fqSYALFPHMTVEQ------NIAFGLKQDRLPKAEITARVQEMLALVHMQEFAK---RKPRQLSGGQRQ------RVALA 161
Cdd:cd03240 56 --GGAHDPKLIREGevraqvKLAFENANGKKYTITRSLAILENVIFCHQGESNWpllDMRGRCSGGEKVlasliiRLALA 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1616137381 162 RSLAKRPKLLLLDEPMGALDkklRDRMQLEVVDILERVGVTCVM----VTHDQE 211
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQKNFqlivITHDEE 184
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-246 |
4.74e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLAR--VPPYQRPINMMFQSYALFPHmTVEQNIafg 115
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQNV--- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 116 lkqDRLPKAEiTARVQEMLALVHMQEFAKRK-----PRQLSG------GQRQRVALARSLAKR-PKLLLLDEPMGALDKK 183
Cdd:PTZ00243 1405 ---DPFLEAS-SAEVWAALELVGLRERVASEsegidSRVLEGgsnysvGQRQLMCMARALLKKgSGFILMDEATANIDPA 1480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 184 LRDRMQLEVVDILErvGVTCVMVTHdqeEAMTMA--GRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
Cdd:PTZ00243 1481 LDRQIQATVMSAFS--AYTVITIAH---RLHTVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
20-209 |
3.94e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 20 LEIRNLtKSFDGQHAVDdvsltiYKGEIFALLGASGCGKSTLLR--MLAGFEQPTAG-----QIMLDGVDLARV------ 86
Cdd:COG0419 5 LRLENF-RSYRDTETID------FDDGLNLIVGPNGAGKSTILEaiRYALYGKARSRsklrsDLINVGSEEASVelefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 87 --PPYQ--RPINMmFQSYALFPHMTVEQNIA--FGLK-----QDRLP--KAEITARVQEMLALVHMQE--FAK----RKP 147
Cdd:COG0419 78 ggKRYRieRRQGE-FAEFLEAKPSERKEALKrlLGLEiyeelKERLKelEEALESALEELAELQKLKQeiLAQlsglDPI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 148 RQLSGGQRQRVALARSLAkrpklLLLDepMGALDKKLRDRMqlevVDILERVGVtcvmVTHD 209
Cdd:COG0419 157 ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERL----LDALEELAI----ITHV 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-241 |
4.41e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 145 RKPRQLSGGQRQRVALARSLAKRPK--LLLLDEPMGALDKklRDRMQL-EVVDILERVGVTCVMVTHDqEEAMTMAGRI- 220
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQ--RDNRRLiNTLKRLRDLGNTLIVVEHD-EDTIRAADYVi 560
|
90 100
....*....|....*....|....*.
gi 1616137381 221 -----AIMNRGKFVQIGEPEEIYEHP 241
Cdd:TIGR00630 561 digpgAGEHGGEVVASGTPEEILANP 586
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
150-211 |
8.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 8.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616137381 150 LSGGQRQ------RVALARSLAKRPKLLLLDEPMGALDKKLRDRMqlevVDILER-------VgvtcVMVTHDQE 211
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKL----VDIMERylrkipqV----IIVSHDEE 855
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-208 |
1.77e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 1.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1616137381 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALD----KKLrdrmqLEVVDILERVGVTCVMVTH 208
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHfddiKKL-----LEVLQRLVDKGNTVVVIEH 890
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
32-220 |
2.08e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTL-------------LRMLAGFEQPTAGQIMLDGVDLAR-VPPyqrPINMMF 97
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDSIEgLSP---AIAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137381 98 QSYALFPHMTV----EQNIAFGLKQDRLPkaeITARVQEM--LALVHMQefAKRKPRQLSGGQRQRVALARSLAKRPK-- 169
Cdd:cd03270 85 KTTSRNPRSTVgtvtEIYDYLRLLFARVG---IRERLGFLvdVGLGYLT--LSRSAPTLSGGEAQRIRLATQIGSGLTgv 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1616137381 170 LLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDqEEAMTMAGRI 220
Cdd:cd03270 160 LYVLDEPSIGLHPRDNDRL-IETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
150-187 |
3.88e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 3.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1616137381 150 LSGGQRQRVALARSLAKRPK---LLLLDEP------------MGALDkKLRDR 187
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPttglhfhdirklLEVLH-RLVDK 878
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
150-209 |
7.89e-04 |
|
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: 40.68 E-value: 7.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137381 150 LSGGQRQRVALARSLAKR---PKLLLLDEPMGALD----KKLrdrmqLEVVDILERVGVTCVMVTHD 209
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHfhdvKKL-----LEVLQRLVDKGNTVVVIEHN 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
149-211 |
1.46e-03 |
|
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: 38.88 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137381 149 QLSGGQRQRVALARSLA----KRPKLLLLDEPMGALDkkLRDRMQLEVVdILERVGVTCVM--VTHDQE 211
Cdd:cd03227 77 QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD--PRDGQALAEA-ILEHLVKGAQVivITHLPE 142
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
150-176 |
2.47e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 2.47e-03
10 20 30
....*....|....*....|....*....|
gi 1616137381 150 LSGGQRQRVALARSLAKRPK---LLLLDEP 176
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEP 860
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-211 |
3.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 3.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1616137381 147 PRQLSGGQRQ------RVALARSLAK-----RP-KLLLLDEPMGALDKKLRDRMqLEVVDILERVGV-TCVMVTHDQE 211
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEgiegdAPlPPLILDEPTVFLDSGHVSQL-VDLVESMRRLGVeQIVVVSHDDE 855
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
15-66 |
5.63e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 5.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1616137381 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA 66
Cdd:COG5635 150 LLVSLDDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| |
